NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|31982393|ref|NP_031966|]
View 

bifunctional epoxide hydrolase 2 isoform a [Mus musculus]

Protein Classification

HAD_sEH-N_like and Abhydrolase_1 domain-containing protein( domain architecture ID 11552356)

HAD_sEH-N_like and Abhydrolase_1 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 3-214 2.44e-59

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 195.26  E-value: 2.44e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   3 LRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLgayQTEFPEGPTEQLMKGKITFSQwvplMDESYRKSSKACganl 82
Cdd:cd02603   1 IRAVLFDFGGVLIDPDPAAAVARFEALTGEPSEFVL---DTEGLAGAFLELERGRITEEE----FWEELREELGRP---- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  83 PENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkrdslAQMMC--ELSQHFDFLIESCQVGMIK 160
Cdd:cd02603  70 LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-----FQLELlpRRGDLFDGVVESCRLGVRK 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 31982393 161 PEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELE 214
Cdd:cd02603 142 PDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 257-530 2.84e-45

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


:

Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 159.98  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   257 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 336
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   337 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 416
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   417 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 496
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 31982393   497 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 530
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
 
Name Accession Description Interval E-value
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 3-214 2.44e-59

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 195.26  E-value: 2.44e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   3 LRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLgayQTEFPEGPTEQLMKGKITFSQwvplMDESYRKSSKACganl 82
Cdd:cd02603   1 IRAVLFDFGGVLIDPDPAAAVARFEALTGEPSEFVL---DTEGLAGAFLELERGRITEEE----FWEELREELGRP---- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  83 PENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkrdslAQMMC--ELSQHFDFLIESCQVGMIK 160
Cdd:cd02603  70 LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-----FQLELlpRRGDLFDGVVESCRLGVRK 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 31982393 161 PEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELE 214
Cdd:cd02603 142 PDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 5-203 2.07e-46

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 160.66  E-value: 2.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393     5 VAAFDLDGVLALPSIAGAF-RRSEEALALPRDFLLGAYQtefpegpteqLMKGKITFSQWvplmdESYRKSSKACGANLP 83
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKlINREELGLVPDELGVSAVG----------RLELALRRFKA-----QYGRTISPEDAQLLY 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393    84 ENFSISQIFSQAMAArsINRPMLQAAIALKKKGFTTCIVTNNWlddgdKRDSLAQMMCELSQHFDFLIESCQVGMIKPEP 163
Cdd:TIGR01509  66 KQLFYEQIEEEAKLK--PLPGVRALLEALRARGKKLALLTNSP-----RAHKLVLALLGLRDLFDVVIDSSDVGLGKPDP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 31982393   164 QIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV 203
Cdd:TIGR01509 139 DIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 257-530 2.84e-45

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 159.98  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   257 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 336
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   337 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 416
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   417 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 496
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 31982393   497 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 530
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 236-542 1.32e-39

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 143.60  E-value: 1.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 236 SHGYVTVkPGIRLHFVEMG-SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSSPPEieEYAMELLCKE 314
Cdd:COG0596   3 TPRFVTV-DGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLADD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 315 MVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVaslntpfmppdpdvspmkvirsipvfnyqlyfqepgvaeae 394
Cdd:COG0596  79 LAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGL----------------------------------------- 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 395 leknmsrtfksffrasdetgfiavhkateiggILVNtpedpnlskitteEEIEFYIQQFKKTGfRGPLNWYRNTERNWKW 474
Cdd:COG0596 118 --------------------------------VLVD-------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982393 475 SCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQ 542
Cdd:COG0596 152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-204 1.87e-23

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 98.56  E-value: 1.87e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   8 FDLDGVLAL--PSIAGAFRRSEEALALPRDF--LLGAYQTEFPEGpTEQLMKGKITFSQWVPLMDESYrksskacgaNLP 83
Cdd:COG1011   6 FDLDGTLLDfdPVIAEALRALAERLGLLDEAeeLAEAYRAIEYAL-WRRYERGEITFAELLRRLLEEL---------GLD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  84 ENFSISQIFSQAMAARSINRP-MLQAAIALKKKGFTTCIVTNNWLDDGDKRdsLAQmmCELSQHFDFLIESCQVGMIKPE 162
Cdd:COG1011  76 LAEELAEAFLAALPELVEPYPdALELLEALKARGYRLALLTNGSAELQEAK--LRR--LGLDDLFDAVVSSEEVGVRKPD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 31982393 163 PQIYNFLLDTLKAKPNEVVFLDD-FGSNLKPARDMGMVTILVH 204
Cdd:COG1011 152 PEIFELALERLGVPPEEALFVGDsPETDVAGARAAGMRTVWVN 194
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 239-550 2.85e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 94.29  E-value: 2.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  239 YVTVKpGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSPPE---IEEYAMELLCkem 315
Cdd:PRK03592  11 RVEVL-GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIdytFADHARYLDA--- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  316 vtFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSipvfnYQLyFQEPGVAEAE- 394
Cdd:PRK03592  86 --WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVREL-----FQA-LRSPGEGEEMv 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  395 LEKNMsrtfksffrasdetgFIavhKATEIGGILvntpedpnlsKITTEEEIEFYIQQFKKTGFRGP-LNWYRN------ 467
Cdd:PRK03592 158 LEENV---------------FI---ERVLPGSIL----------RPLSDEEMAVYRRPFPTPESRRPtLSWPRElpidge 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  468 -------TERNWKWSCKGlgrkiLVPALMVTAEKDIVLR-PEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIK 539
Cdd:PRK03592 210 padvvalVEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAA 284

                        330
                 ....*....|.
gi 31982393  540 WLQTEVQNPSV 550
Cdd:PRK03592 285 WLRRLRLAVSA 295
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-197 8.91e-17

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 78.78  E-value: 8.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393     3 LRVAAFDLDGVLAL--PSIAGAFRRSEEALALPRDFLLGAYQTEFP-EGPTEQLMKGKITFSQWVPLMDESYRKsskaCG 79
Cdd:pfam00702   1 IKAVVFDLDGTLTDgePVVTEAIAELASEHPLAKAIVAAAEDLPIPvEDFTARLLLGKRDWLEELDILRGLVET----LE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393    80 ANLPENFSISQIFSQAMAARSINRPMLQAAI-ALKKKGFTTCIVTNnwlDDGDKRDSLAQMmCELSQHFDFLIESCQVGM 158
Cdd:pfam00702  77 AEGLTVVLVELLGVIALADELKLYPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 31982393   159 IKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMG 197
Cdd:pfam00702 153 GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 142-205 2.45e-07

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 51.19  E-value: 2.45e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982393  142 ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 205
Cdd:PRK09456 123 EVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILVTD 186
 
Name Accession Description Interval E-value
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 3-214 2.44e-59

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 195.26  E-value: 2.44e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   3 LRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLgayQTEFPEGPTEQLMKGKITFSQwvplMDESYRKSSKACganl 82
Cdd:cd02603   1 IRAVLFDFGGVLIDPDPAAAVARFEALTGEPSEFVL---DTEGLAGAFLELERGRITEEE----FWEELREELGRP---- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  83 PENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkrdslAQMMC--ELSQHFDFLIESCQVGMIK 160
Cdd:cd02603  70 LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-----FQLELlpRRGDLFDGVVESCRLGVRK 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 31982393 161 PEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELE 214
Cdd:cd02603 142 PDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 5-203 2.07e-46

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 160.66  E-value: 2.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393     5 VAAFDLDGVLALPSIAGAF-RRSEEALALPRDFLLGAYQtefpegpteqLMKGKITFSQWvplmdESYRKSSKACGANLP 83
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKlINREELGLVPDELGVSAVG----------RLELALRRFKA-----QYGRTISPEDAQLLY 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393    84 ENFSISQIFSQAMAArsINRPMLQAAIALKKKGFTTCIVTNNWlddgdKRDSLAQMMCELSQHFDFLIESCQVGMIKPEP 163
Cdd:TIGR01509  66 KQLFYEQIEEEAKLK--PLPGVRALLEALRARGKKLALLTNSP-----RAHKLVLALLGLRDLFDVVIDSSDVGLGKPDP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 31982393   164 QIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV 203
Cdd:TIGR01509 139 DIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 257-530 2.84e-45

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 159.98  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   257 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 336
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   337 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 416
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   417 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 496
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 31982393   497 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 530
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 236-542 1.32e-39

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 143.60  E-value: 1.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 236 SHGYVTVkPGIRLHFVEMG-SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSSPPEieEYAMELLCKE 314
Cdd:COG0596   3 TPRFVTV-DGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLADD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 315 MVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVaslntpfmppdpdvspmkvirsipvfnyqlyfqepgvaeae 394
Cdd:COG0596  79 LAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGL----------------------------------------- 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 395 leknmsrtfksffrasdetgfiavhkateiggILVNtpedpnlskitteEEIEFYIQQFKKTGfRGPLNWYRNTERNWKW 474
Cdd:COG0596 118 --------------------------------VLVD-------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982393 475 SCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQ 542
Cdd:COG0596 152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 2-218 1.44e-32

epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA.


Pssm-ID: 274054 [Multi-domain]  Cd Length: 211  Bit Score: 124.17  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393     2 ALRVAAFDLDGVLaLPSiAGAFRR--SEEALALPRDFLLGAYQTEFPEGP-TEQLMKGKITFSQWVPLMdesyrksSKAC 78
Cdd:TIGR02247   1 AIKAVIFDFGGVL-LPS-PGVMRRweTERGLPGLKDFIVTVNITGPDFNPwARTFERGELTAEAFDGLF-------RHEY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393    79 GANLPENFSISQIFSQAMAARSINRPMLQAAI-ALKKKGFTTCIVTNNWLDDGDKRDSLAqmMCELSQHFDFLIESCQVG 157
Cdd:TIGR02247  72 GLRLGHDVRIAPVFPLLYGENTKLRPSMMAAIkTLRAKGFKTACITNNFPTDHSAEEALL--PGDIMALFDAVVESCLEG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982393   158 MIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKVTG 218
Cdd:TIGR02247 150 LRKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDLEKATK 210
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-204 1.87e-23

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 98.56  E-value: 1.87e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   8 FDLDGVLAL--PSIAGAFRRSEEALALPRDF--LLGAYQTEFPEGpTEQLMKGKITFSQWVPLMDESYrksskacgaNLP 83
Cdd:COG1011   6 FDLDGTLLDfdPVIAEALRALAERLGLLDEAeeLAEAYRAIEYAL-WRRYERGEITFAELLRRLLEEL---------GLD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  84 ENFSISQIFSQAMAARSINRP-MLQAAIALKKKGFTTCIVTNNWLDDGDKRdsLAQmmCELSQHFDFLIESCQVGMIKPE 162
Cdd:COG1011  76 LAEELAEAFLAALPELVEPYPdALELLEALKARGYRLALLTNGSAELQEAK--LRR--LGLDDLFDAVVSSEEVGVRKPD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 31982393 163 PQIYNFLLDTLKAKPNEVVFLDD-FGSNLKPARDMGMVTILVH 204
Cdd:COG1011 152 PEIFELALERLGVPPEEALFVGDsPETDVAGARAAGMRTVWVN 194
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 239-550 2.85e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 94.29  E-value: 2.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  239 YVTVKpGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSPPE---IEEYAMELLCkem 315
Cdd:PRK03592  11 RVEVL-GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIdytFADHARYLDA--- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  316 vtFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSipvfnYQLyFQEPGVAEAE- 394
Cdd:PRK03592  86 --WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVREL-----FQA-LRSPGEGEEMv 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  395 LEKNMsrtfksffrasdetgFIavhKATEIGGILvntpedpnlsKITTEEEIEFYIQQFKKTGFRGP-LNWYRN------ 467
Cdd:PRK03592 158 LEENV---------------FI---ERVLPGSIL----------RPLSDEEMAVYRRPFPTPESRRPtLSWPRElpidge 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  468 -------TERNWKWSCKGlgrkiLVPALMVTAEKDIVLR-PEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIK 539
Cdd:PRK03592 210 padvvalVEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAA 284

                        330
                 ....*....|.
gi 31982393  540 WLQTEVQNPSV 550
Cdd:PRK03592 285 WLRRLRLAVSA 295
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 239-379 9.42e-19

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 86.95  E-value: 9.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  239 YVTVKPG----IRLHFVEMGSG---PALCLcHGFPeSW-FSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMEL 310
Cdd:PRK00870  23 YVDVDDGdggpLRMHYVDEGPAdgpPVLLL-HGEP-SWsYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYAR 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982393  311 LCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTpfMPPDPDVSPMKV-------IRSIPVF 379
Cdd:PRK00870 101 HVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT--GLPTGDGPMPDAfwawrafSQYSPVL 174
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-197 8.91e-17

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 78.78  E-value: 8.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393     3 LRVAAFDLDGVLAL--PSIAGAFRRSEEALALPRDFLLGAYQTEFP-EGPTEQLMKGKITFSQWVPLMDESYRKsskaCG 79
Cdd:pfam00702   1 IKAVVFDLDGTLTDgePVVTEAIAELASEHPLAKAIVAAAEDLPIPvEDFTARLLLGKRDWLEELDILRGLVET----LE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393    80 ANLPENFSISQIFSQAMAARSINRPMLQAAI-ALKKKGFTTCIVTNnwlDDGDKRDSLAQMmCELSQHFDFLIESCQVGM 158
Cdd:pfam00702  77 AEGLTVVLVELLGVIALADELKLYPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 31982393   159 IKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMG 197
Cdd:pfam00702 153 GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
237-369 1.45e-16

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 78.89  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 237 HGYVTVKPGIRLHFVEM----GSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSP----PEIEEYAM 308
Cdd:COG2267   5 LVTLPTRDGLRLRGRRWrpagSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPrghvDSFDDYVD 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982393 309 ELlcKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVAsLNTPFMPPDPDVSP 369
Cdd:COG2267  85 DL--RAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLV-LLAPAYRADPLLGP 142
PRK05855 PRK05855
SDR family oxidoreductase;
240-530 2.12e-16

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 82.34  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  240 VTVKPGIRLHFVEMG--SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVT 317
Cdd:PRK05855   7 VVSSDGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLA-DRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  318 FLDKLGIPQAV-FIGHDWAGVMVWNmALFYPERVRAVASLnTPFMPPDPD------------VSPMKVIRsipVFN---- 380
Cdd:PRK05855  86 VIDAVSPDRPVhLLAHDWGSIQGWE-AVTRPRAAGRIASF-TSVSGPSLDhvgfwlrsglrrPTPRRLAR---ALGqllr 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  381 --YQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHKATeiggilvnTPEDpnlskitteeeiefyiqqfkktGF 458
Cdd:PRK05855 161 swYIYLFHLPVLPELLWRLGLGRAWPRLLRRVEGTPVDPIPTQT--------TLSD----------------------GA 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31982393  459 RGpLNWYR-NTERNwkwSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIeDCGHWTQIEKP 530
Cdd:PRK05855 211 HG-VKLYRaNMIRS---LSRPRERYTDVPVQLIVPTGDPYVRPALYDDLSRWVPRLWRREI-KAGHWLPMSHP 278
PLN02578 PLN02578
hydrolase
 245-358 1.07e-15

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 78.73  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  245 GIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAgFRVLAIDMKGYGDSSSPpeIEEYAMELLCKEMVTFLDKLGI 324
Cdd:PLN02578  75 GHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKA--LIEYDAMVWRDQVADFVKEVVK 151

                         90       100       110
                 ....*....|....*....|....*....|....
gi 31982393  325 PQAVFIGHDWAGVMVWNMALFYPERVRAVASLNT 358
Cdd:PLN02578 152 EPAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 247-364 1.30e-14

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 74.51  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  247 RLHFVEMGSGPALCLCHGFPESWFSWRYQIPALaQAGFRVLAIDMKGYGDSSSPPEIeEYAMELLCKEMVTFLDKLGIPQ 326
Cdd:PRK03204  25 RIHYIDEGTGPPILLCHGNPTWSFLYRDIIVAL-RDRFRCVAPDYLGFGLSERPSGF-GYQIDEHARVIGEFVDHLGLDR 102

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 31982393  327 AVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPD 364
Cdd:PRK03204 103 YLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPAD 140
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 244-354 1.87e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 71.90  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  244 PGIRLHFVEMG--SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSspPEIEEYAMELLCKEMVTFLDK 321
Cdd:PRK14875 117 GGRTVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASS--KAVGAGSLDELAAAVLAFLDA 193

                         90       100       110
                 ....*....|....*....|....*....|...
gi 31982393  322 LGIPQAVFIGHDWAGVMVWNMALFYPERVRAVA 354
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLT 226
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
237-356 4.13e-13

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 68.89  E-value: 4.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 237 HGYVTVKPGIRLHfvemgsgPALCLCHGFPES-WFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEY-----AMEL 310
Cdd:COG1506  11 PGWLYLPADGKKY-------PVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVddvlaAIDY 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 31982393 311 LCKEMVTFLDKLGIpqavfIGHDWAGVMVWNMALFYPERVRAVASL 356
Cdd:COG1506  84 LAARPYVDPDRIGI-----YGHSYGGYMALLAAARHPDRFKAAVAL 124
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-214 4.89e-12

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 65.34  E-value: 4.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   3 LRVAAFDLDGVLA--LPSIAGAFRRseeALAlprdfllgayQTEFPEGPTEQLMkgkitfsQWV-PLMDESYRKsskACG 79
Cdd:COG0546   1 IKLVLFDLDGTLVdsAPDIAAALNE---ALA----------ELGLPPLDLEELR-------ALIgLGLRELLRR---LLG 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  80 ANLPENFS-ISQIFSQAMAARSIN--------RPMLQAaiaLKKKGFTTCIVTNnwlddgdKRDSLAQMMCE---LSQHF 147
Cdd:COG0546  58 EDPDEELEeLLARFRELYEEELLDetrlfpgvRELLEA---LKARGIKLAVVTN-------KPREFAERLLEalgLDDYF 127

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 148 DFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV---HNTASALRELE 214
Cdd:COG0546 128 DAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVtwgYGSAEELEAAG 197
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 254-357 1.18e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 62.83  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  254 GSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSP-----PEIEEYAMELLCKEMVTFLDKLGIPQAV 328
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAF 105

                         90       100
                 ....*....|....*....|....*....
gi 31982393  329 FIGHDWAGVMVWNMALFYPERVRAVASLN 357
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLIN 134
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 101-203 1.53e-09

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 55.48  E-value: 1.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 101 INRPMLQAaiaLKKKGFTTCIVTNNWLDDGDKRdsLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEV 180
Cdd:cd01427  11 LAVELLKR---LRAAGIKLAIVTNRSREALRAL--LEK--LGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEV 83

                        90       100
                ....*....|....*....|...
gi 31982393 181 VFLDDFGSNLKPARDMGMVTILV 203
Cdd:cd01427  84 LFVGDSENDIEAARAAGGRTVAV 106
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-203 8.90e-09

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 55.28  E-value: 8.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393     8 FDLDGVLA--LPSIAGAFRRSEEAL---ALPRDFLLgayqtEFPEGPTEQLMKgKITFSQWVPLMDESYRKSSKAcgANL 82
Cdd:pfam13419   3 FDFDGTLLdtEELIIKSFNYLLEEFgygELSEEEIL-----KFIGLPLREIFR-YLGVSEDEEEKIEFYLRKYNE--ELH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393    83 PENFS-ISQIFSqamaarsinrpMLQAaiaLKKKGFTTCIVTNNWlddgdkRDSLAQMM--CELSQHFDFLIESCQVGMI 159
Cdd:pfam13419  75 DKLVKpYPGIKE-----------LLEE---LKEQGYKLGIVTSKS------RENVEEFLkqLGLEDYFDVIVGGDDVEGK 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 31982393   160 KPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV 203
Cdd:pfam13419 135 KPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 258-369 3.32e-08

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 54.53  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   258 ALCLCHGFPESwfSWRYQ--IPALAQAGFRVLAIDMKGYGDSSSP----PEIEEYamellCKEMVTFLDKL-----GIPQ 326
Cdd:pfam12146   6 VVVLVHGLGEH--SGRYAhlADALAAQGFAVYAYDHRGHGRSDGKrghvPSFDDY-----VDDLDTFVDKIreehpGLPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 31982393   327 AVFiGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSP 369
Cdd:pfam12146  79 FLL-GHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPP 120
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 261-393 4.43e-08

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 53.63  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   261 LCHGfpesWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPP-EIEEYAmellckEMVTFLDKLGI-PQAVFIGHDWAGVM 338
Cdd:pfam12697   3 LVHG----AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPlDLADLA------DLAALLDELGAaRPVVLVGHSLGGAV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 31982393   339 VWNMALFYPERVRAVASLNTPFMPPDPDVSPMKviRSIPVFNYQLYFQEPGVAEA 393
Cdd:pfam12697  73 ALAAAAAALVVGVLVAPLAAPPGLLAALLALLA--RLGAALAAPAWLAAESLARG 125
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 255-331 7.57e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 54.46  E-value: 7.57e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982393  255 SGPALCLCHGFPESWFSWRYQIPALAQAgFRVLAIDMKGYGDSSSPPEIeEYAMELLCKEMVTFLDKLGIPQAVFIG 331
Cdd:PLN02679  87 SGPPVLLVHGFGASIPHWRRNIGVLAKN-YTVYAIDLLGFGASDKPPGF-SYTMETWAELILDFLEEVVQKPTVLIG 161
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
8-216 7.95e-08

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 52.90  E-value: 7.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   8 FDLDGVLA--LPSIAGAFRRseealalprdfLLGAYQTEFPEGPTEQLMkGKiTFSQWVPLMDESYrksskacGANLP-E 84
Cdd:COG0637   7 FDMDGTLVdsEPLHARAWRE-----------AFAELGIDLTEEEYRRLM-GR-SREDILRYLLEEY-------GLDLPeE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  85 NFS--ISQIFSQAMAARSIN-RPMLQAAI-ALKKKGFTTCIVTNNwlddgdKRDSLAQMM--CELSQHFDFLIESCQVGM 158
Cdd:COG0637  67 ELAarKEELYRELLAEEGLPlIPGVVELLeALKEAGIKIAVATSS------PRENAEAVLeaAGLLDYFDVIVTGDDVAR 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31982393 159 IKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKV 216
Cdd:COG0637 141 GKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGA 198
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 261-360 1.22e-07

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.83  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 261 LCHGFPESWFSWRYQIPALAQAGFRVLAIDmkgYGDSSSPpeIEEYAMELLckemvTFLDKL----GIPQAVFIGHDWAG 336
Cdd:COG1075  10 LVHGLGGSAASWAPLAPRLRAAGYPVYALN---YPSTNGS--IEDSAEQLA-----AFVDAVlaatGAEKVDLVGHSMGG 79

                        90       100
                ....*....|....*....|....*.
gi 31982393 337 VMVWNMA--LFYPERVRAVASLNTPF 360
Cdd:COG1075  80 LVARYYLkrLGGAAKVARVVTLGTPH 105
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 142-205 2.45e-07

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 51.19  E-value: 2.45e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982393  142 ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 205
Cdd:PRK09456 123 EVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILVTD 186
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 101-205 8.16e-07

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 48.06  E-value: 8.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 101 INRPMLQAaiaLKKKGFTTCIVTNNwlddgDKRdsLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPN 178
Cdd:cd16415  11 LAVETLKD---LKEKGLKLAVVSNF-----DRR--LRELLeaLGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPE 80

                        90       100
                ....*....|....*....|....*...
gi 31982393 179 EVVFL-DDFGSNLKPARDMGMVTILVHN 205
Cdd:cd16415  81 EALHVgDDLKNDYLGARAVGWHALLVDR 108
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 114-201 1.15e-06

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 47.15  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 114 KKGFTTCIVTNnwlddGDK---RDSLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFL-DDFGSN 189
Cdd:cd04305  22 KKGYKLGIITN-----GPTevqWEKLEQ--LGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVgDSLESD 94

                        90
                ....*....|..
gi 31982393 190 LKPARDMGMVTI 201
Cdd:cd04305  95 ILGAKNAGIKTV 106
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
250-413 2.46e-06

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 49.17  E-value: 2.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 250 FVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGdsSSPPEIE-----------EYAMELLCKEMvtf 318
Cdd:COG1647   9 FFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHG--TSPEDLLkttwedwledvEEAYEILKAGY--- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 319 lDKLGIpqavfIGHDWAGVMVWNMALFYPErVRAVASLNTPFMPPDPDVSPMKVIRSIP--VFNYQLYFQEPGVAEAELE 396
Cdd:COG1647  84 -DKVIV-----IGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYLArsLRGIGSDIEDPEVAEYAYD 156

                       170
                ....*....|....*..
gi 31982393 397 KNMSRTFKSFFRASDET 413
Cdd:COG1647 157 RTPLRALAELQRLIREV 173
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 240-360 4.11e-06

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 48.37  E-value: 4.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 240 VTVKPGIRLH---FV---EMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCK 313
Cdd:COG1073  15 FKSRDGIKLAgdlYLpagASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERRDAR 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 31982393 314 EMVTFL-DKLGIPQA--VFIGHDWAGVMVWNMALFYPeRVRAVASLnTPF 360
Cdd:COG1073  95 AAVDYLrTLPGVDPEriGLLGISLGGGYALNAAATDP-RVKAVILD-SPF 142
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 111-203 7.15e-06

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 47.26  E-value: 7.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 111 ALKKKGFTTCIVTNnwlddGDkRDSLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGS 188
Cdd:cd02588 102 RLREAGYRLAILSN-----GS-PDLIEDVVanAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAW 175

                        90
                ....*....|....*
gi 31982393 189 NLKPARDMGMVTILV 203
Cdd:cd02588 176 DLAGARALGLRTAWI 190
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
254-378 1.32e-05

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 46.50  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 254 GSGPALCLCHGfpesWFSWRYQIPA----LAQAGFRVLAIDM-KGYGDSSSPPEIEEYAMELLCKEMVT-------FL-- 319
Cdd:COG0412  27 GPRPGVVVLHE----IFGLNPHIRDvarrLAAAGYVVLAPDLyGRGGPGDDPDEARALMGALDPELLAAdlraaldWLka 102

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982393 320 ------DKLGIpqavfIGHDWAGVMVWNMALFYPeRVRAVASLNtPFMPPDPDVSPMKVIRsIPV 378
Cdd:COG0412 103 qpevdaGRVGV-----VGFCFGGGLALLAAARGP-DLAAAVSFY-GGLPADDLLDLAARIK-APV 159
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 103-216 1.96e-05

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 45.73  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 103 RPMLQAaiaLKKKGFTTCIVTNnwlddgdKRDSLAQM---MCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNE 179
Cdd:cd02616  86 YETLAR---LKSQGIKLGVVTT-------KLRETALKglkLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEE 155

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31982393 180 VVFLDDFGSNLKPARDMGMVTILVhntASALRELEKV 216
Cdd:cd02616 156 ALMVGDSPHDILAGKNAGVKTVGV---TWGYKGREYL 189
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 257-374 3.31e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 46.44  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  257 PALCLCHGFPESW-FSWRyQIPALAqAGFRVLAIDMKGYGDSSSPP-------EIEEYamellckemvtFLDKL------ 322
Cdd:PLN02894 106 PTLVMVHGYGASQgFFFR-NFDALA-SRFRVIAIDQLGWGGSSRPDftcksteETEAW-----------FIDSFeewrka 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 31982393  323 -GIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIR 374
Cdd:PLN02894 173 kNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTK 225
PRK10673 PRK10673
esterase;
286-350 4.70e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.11  E-value: 4.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982393  286 VLAIDMKGYGDSSSPPEIEEYAMellCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERV 350
Cdd:PRK10673  45 IIQVDMRNHGLSPRDPVMNYPAM---AQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRI 106
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 247-362 1.03e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 44.87  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393  247 RLHFVEMGS--GPALCLCHGFPESWFSWRYQIPALAQaGFRVLAIDMKGYGDSSSPP-------EIEEY--AMELLCKEM 315
Cdd:PLN03084 116 RWFCVESGSnnNPPVLLIHGFPSQAYSYRKVLPVLSK-NYHAIAFDWLGFGFSDKPQpgygfnyTLDEYvsSLESLIDEL 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 31982393  316 VTflDKLGIpqaVFIGHdWAGVMVwNMALFYPERVRAVASLNTPFMP 362
Cdd:PLN03084 195 KS--DKVSL---VVQGY-FSPPVV-KYASAHPDKIKKLILLNPPLTK 234
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 111-205 4.03e-04

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 40.68  E-value: 4.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 111 ALKKKGFTTCIVTNNWLDDGDKRDSLAQmmcELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNL 190
Cdd:cd07505  52 ALKAAGIPVAVATSSSRRNVELLLLELG---LLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSLAGI 128

                        90
                ....*....|....*
gi 31982393 191 KPARDMGMVTILVHN 205
Cdd:cd07505 129 EAAKAAGMTVVAVPD 143
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 143-205 1.26e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 39.92  E-value: 1.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982393 143 LSQHFDFLIESCQVGMI-KPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 205
Cdd:cd02604 119 LADLFDGIFDIEYAGPDpKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVGP 182
Hydrolase_like pfam13242
HAD-hyrolase-like;
160-203 1.54e-03

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 37.60  E-value: 1.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 31982393   160 KPEPQIYNFLLDTLKAKPNEVVFL-DDFGSNLKPARDMGMVTILV 203
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIgDRLDTDILGAREAGARTILV 48
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
112-203 1.73e-03

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 39.34  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393 112 LKKKGFTTCIVTNNWlddgDKR-DSLAQMMcelsqHFDFLIESCqvgmiKPEPQIYNFLLDTLKAKPNEVVFLDD----- 185
Cdd:COG2179  56 LKEAGFKVCIVSNNS----EKRvKRFAEKL-----GIPYIARAK-----KPLPRGFRKALKLMGLPPEETAVVGDqlftd 121

                        90
                ....*....|....*....
gi 31982393 186 -FGSNLkpardMGMVTILV 203
Cdd:COG2179 122 vLGGNR-----AGLYTILV 135
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-123 3.54e-03

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 39.05  E-value: 3.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982393   1 MALRVAAFDLDGVLalpsIAG------AFRRSEEALALPRDFLlgayqtEFPEGPTEQLMKGKITFsqwvplmDESYRKS 74
Cdd:COG0560   1 RKMRLAVFDLDGTL----IAGesidelARFLGRRGLVDRREVL------EEVAAITERAMAGELDF-------EESLRFR 63

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 31982393  75 SKACgANLPENFsISQIFSQAMAARS-INRPMLQAAIALKKKGFTTCIVT 123
Cdd:COG0560  64 VALL-AGLPEEE-LEELAERLFEEVPrLYPGARELIAEHRAAGHKVAIVS 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH