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Conserved domains on  [gi|406647884|ref|NP_001258350|]
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bifunctional epoxide hydrolase 2 isoform d [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

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 191-464 8.02e-46

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: 8.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  191 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 270
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  271 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 350
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  351 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 430
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 406647884  431 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 464
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-148 3.41e-42

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: 148.65  E-value: 3.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884   1 MDESYRKSSKACganlPENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkrdslAQMMC--ELS 78
Cdd:cd02603   58 FWEELREELGRP----LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-----FQLELlpRRG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  79 QHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELE 148
Cdd:cd02603  126 DLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 191-464 8.02e-46

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: 8.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  191 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 270
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  271 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 350
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  351 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 430
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 406647884  431 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 464
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-148 3.41e-42

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: 148.65  E-value: 3.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884   1 MDESYRKSSKACganlPENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkrdslAQMMC--ELS 78
Cdd:cd02603   58 FWEELREELGRP----LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-----FQLELlpRRG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  79 QHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELE 148
Cdd:cd02603  126 DLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 170-476 5.16e-40

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: 5.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 170 SHGYVTVkPGIRLHFVEMG-SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSSPPEieEYAMELLCKE 248
Cdd:COG0596    3 TPRFVTV-DGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLADD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 249 MVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVaslntpfmppdpdvspmkvirsipvfnyqlyfqepgvaeae 328
Cdd:COG0596   79 LAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGL----------------------------------------- 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 329 leknmsrtfksffrasdetgfiavhkateiggILVNtpedpnlskitteEEIEFYIQQFKKTGfRGPLNWYRNTERNWKW 408
Cdd:COG0596  118 --------------------------------VLVD-------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406647884 409 SCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQ 476
Cdd:COG0596  152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 1-137 7.10e-37

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: 133.70  E-value: 7.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884    1 MDESYRKSSKACGANLPENFSISQIFSQAMAArsINRPMLQAAIALKKKGFTTCIVTNNWlddgdKRDSLAQMMCELSQH 80
Cdd:TIGR01509  49 KAQYGRTISPEDAQLLYKQLFYEQIEEEAKLK--PLPGVRALLEALRARGKKLALLTNSP-----RAHKLVLALLGLRDL 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 406647884   81 FDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV 137
Cdd:TIGR01509 122 FDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 173-484 7.04e-22

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 95.45  E-value: 7.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 173 YVTVKpGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSPPE---IEEYAMELLCkem 249
Cdd:PRK03592  11 RVEVL-GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIdytFADHARYLDA--- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 250 vtFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSipvfnYQLyFQEPGVAEAE- 328
Cdd:PRK03592  86 --WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVREL-----FQA-LRSPGEGEEMv 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 329 LEKNMsrtfksffrasdetgFIavhKATEIGGILvntpedpnlsKITTEEEIEFYIQQFKKTGFRGP-LNWYRN------ 401
Cdd:PRK03592 158 LEENV---------------FI---ERVLPGSIL----------RPLSDEEMAVYRRPFPTPESRRPtLSWPRElpidge 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 402 -------TERNWKWSCKGlgrkiLVPALMVTAEKDIVLR-PEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIK 473
Cdd:PRK03592 210 padvvalVEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAA 284

                        330
                 ....*....|.
gi 406647884 474 WLQTEVQNPSV 484
Cdd:PRK03592 285 WLRRLRLAVSA 295
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 45-138 8.50e-19

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: 85.08  E-value: 8.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  45 ALKKKGFTTCIVTNNWLDDGDKRdsLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDD-FGSN 123
Cdd:COG1011  104 ALKARGYRLALLTNGSAELQEAK--LRR--LGLDDLFDAVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDsPETD 179

                         90
                 ....*....|....*
gi 406647884 124 LKPARDMGMVTILVH 138
Cdd:COG1011  180 VAGARAAGMRTVWVN 194
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 37-131 2.71e-10

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: 59.52  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884   37 RPMLQAAI-ALKKKGFTTCIVTNnwlDDGDKRDSLAQMmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVV 115
Cdd:pfam00702 100 YPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVL 175

                          90
                  ....*....|....*.
gi 406647884  116 FLDDFGSNLKPARDMG 131
Cdd:pfam00702 176 MVGDGVNDIPAAKAAG 191
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 76-139 1.93e-07

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 51.58  E-value: 1.93e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406647884  76 ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 139
Cdd:PRK09456 123 EVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILVTD 186
 
Name Accession Description Interval E-value
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 191-464 8.02e-46

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: 8.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  191 PALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAG 270
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  271 VMVWNMALFYPERVRAVASLNTPFMPPDPDvspmkVIRSIPVFNYQLYFQepGVAEAELEKNMSRTFKSFFRASDetGFI 350
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELD-----EADRFILALFPGFFD--GFVADFAPNPLGRLVAKLLALLL--LRL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  351 AVHKATEigGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRnternwkwsckglgrkilVPALMVTAEKDI 430
Cdd:pfam00561 152 RLLKALP--LLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLD------------------EPTLIIWGDQDP 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 406647884  431 VLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKP 464
Cdd:pfam00561 212 LVPPQALEKLAQLFPNARLVVIPDAGHFAFLEGP 245
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-148 3.41e-42

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: 148.65  E-value: 3.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884   1 MDESYRKSSKACganlPENFSISQIFSQAMaarSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDkrdslAQMMC--ELS 78
Cdd:cd02603   58 FWEELREELGRP----LSAELFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFK-----FQLELlpRRG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  79 QHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELE 148
Cdd:cd02603  126 DLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAEDALRELA 195
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 170-476 5.16e-40

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: 5.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 170 SHGYVTVkPGIRLHFVEMG-SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSSPPEieEYAMELLCKE 248
Cdd:COG0596    3 TPRFVTV-DGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAG--GYTLDDLADD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 249 MVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVaslntpfmppdpdvspmkvirsipvfnyqlyfqepgvaeae 328
Cdd:COG0596   79 LAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGL----------------------------------------- 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 329 leknmsrtfksffrasdetgfiavhkateiggILVNtpedpnlskitteEEIEFYIQQFKKTGfRGPLNWYRNTERNWKW 408
Cdd:COG0596  118 --------------------------------VLVD-------------EVLAALAEPLRRPG-LAPEALAALLRALART 151

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406647884 409 SCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQ 476
Cdd:COG0596  152 DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 1-137 7.10e-37

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: 133.70  E-value: 7.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884    1 MDESYRKSSKACGANLPENFSISQIFSQAMAArsINRPMLQAAIALKKKGFTTCIVTNNWlddgdKRDSLAQMMCELSQH 80
Cdd:TIGR01509  49 KAQYGRTISPEDAQLLYKQLFYEQIEEEAKLK--PLPGVRALLEALRARGKKLALLTNSP-----RAHKLVLALLGLRDL 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 406647884   81 FDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILV 137
Cdd:TIGR01509 122 FDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 12-152 2.99e-30

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: 116.85  E-value: 2.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884   12 CGANLPENFSISQIFSQAMAARSINRPMLQAAI-ALKKKGFTTCIVTNNWLDDGDKRDSLAqmMCELSQHFDFLIESCQV 90
Cdd:TIGR02247  71 YGLRLGHDVRIAPVFPLLYGENTKLRPSMMAAIkTLRAKGFKTACITNNFPTDHSAEEALL--PGDIMALFDAVVESCLE 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406647884   91 GMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKVTG 152
Cdd:TIGR02247 149 GLRKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDLEKATK 210
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 173-484 7.04e-22

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 95.45  E-value: 7.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 173 YVTVKpGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSPPE---IEEYAMELLCkem 249
Cdd:PRK03592  11 RVEVL-GSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIdytFADHARYLDA--- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 250 vtFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSipvfnYQLyFQEPGVAEAE- 328
Cdd:PRK03592  86 --WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVRPMTWDDFPPAVREL-----FQA-LRSPGEGEEMv 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 329 LEKNMsrtfksffrasdetgFIavhKATEIGGILvntpedpnlsKITTEEEIEFYIQQFKKTGFRGP-LNWYRN------ 401
Cdd:PRK03592 158 LEENV---------------FI---ERVLPGSIL----------RPLSDEEMAVYRRPFPTPESRRPtLSWPRElpidge 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 402 -------TERNWKWSCKGlgrkiLVPALMVTAEKDIVLR-PEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIK 473
Cdd:PRK03592 210 padvvalVEEYAQWLATS-----DVPKLLINAEPGAILTtGAIRDWCRSWPNQLEITVFGAGLHFAQEDSPEEIGAAIAA 284

                        330
                 ....*....|.
gi 406647884 474 WLQTEVQNPSV 484
Cdd:PRK03592 285 WLRRLRLAVSA 295
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 173-313 3.96e-19

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 87.72  E-value: 3.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 173 YVTVKPG----IRLHFVEMGSG---PALCLcHGFPeSW-FSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMEL 244
Cdd:PRK00870  23 YVDVDDGdggpLRMHYVDEGPAdgpPVLLL-HGEP-SWsYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYAR 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406647884 245 LCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTpfMPPDPDVSPMKV-------IRSIPVF 313
Cdd:PRK00870 101 HVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT--GLPTGDGPMPDAfwawrafSQYSPVL 174
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 45-138 8.50e-19

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: 85.08  E-value: 8.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  45 ALKKKGFTTCIVTNNWLDDGDKRdsLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDD-FGSN 123
Cdd:COG1011  104 ALKARGYRLALLTNGSAELQEAK--LRR--LGLDDLFDAVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDsPETD 179

                         90
                 ....*....|....*
gi 406647884 124 LKPARDMGMVTILVH 138
Cdd:COG1011  180 VAGARAAGMRTVWVN 194
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
171-303 1.19e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 78.89  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 171 HGYVTVKPGIRLHFVEM----GSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSP----PEIEEYAM 242
Cdd:COG2267    5 LVTLPTRDGLRLRGRRWrpagSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPrghvDSFDDYVD 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 406647884 243 ELlcKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVAsLNTPFMPPDPDVSP 303
Cdd:COG2267   85 DL--RAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLV-LLAPAYRADPLLGP 142
PRK05855 PRK05855
SDR family oxidoreductase;
174-464 1.51e-16

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 82.34  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 174 VTVKPGIRLHFVEMG--SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVT 251
Cdd:PRK05855   7 VVSSDGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLA-DRFRVVAYDVRGAGRSSAPKRTAAYTLARLADDFAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 252 FLDKLGIPQAV-FIGHDWAGVMVWNmALFYPERVRAVASLnTPFMPPDPD------------VSPMKVIRsipVFN---- 314
Cdd:PRK05855  86 VIDAVSPDRPVhLLAHDWGSIQGWE-AVTRPRAAGRIASF-TSVSGPSLDhvgfwlrsglrrPTPRRLAR---ALGqllr 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 315 --YQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHKATeiggilvnTPEDpnlskitteeeiefyiqqfkktGF 392
Cdd:PRK05855 161 swYIYLFHLPVLPELLWRLGLGRAWPRLLRRVEGTPVDPIPTQT--------TLSD----------------------GA 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 406647884 393 RGpLNWYR-NTERNwkwSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIeDCGHWTQIEKP 464
Cdd:PRK05855 211 HG-VKLYRaNMIRS---LSRPRERYTDVPVQLIVPTGDPYVRPALYDDLSRWVPRLWRREI-KAGHWLPMSHP 278
PLN02578 PLN02578
hydrolase
 179-292 6.61e-16

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 79.11  E-value: 6.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 179 GIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAgFRVLAIDMKGYGDSSSPpeIEEYAMELLCKEMVTFLDKLGI 258
Cdd:PLN02578  75 GHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKA--LIEYDAMVWRDQVADFVKEVVK 151

                         90       100       110
                 ....*....|....*....|....*....|....
gi 406647884 259 PQAVFIGHDWAGVMVWNMALFYPERVRAVASLNT 292
Cdd:PLN02578 152 EPAVLVGNSLGGFTALSTAVGYPELVAGVALLNS 185
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 181-298 5.74e-15

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 75.28  E-value: 5.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 181 RLHFVEMGSGPALCLCHGFPESWFSWRYQIPALaQAGFRVLAIDMKGYGDSSSPPEIeEYAMELLCKEMVTFLDKLGIPQ 260
Cdd:PRK03204  25 RIHYIDEGTGPPILLCHGNPTWSFLYRDIIVAL-RDRFRCVAPDYLGFGLSERPSGF-GYQIDEHARVIGEFVDHLGLDR 102

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 406647884 261 AVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPD 298
Cdd:PRK03204 103 YLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPAD 140
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 178-288 1.48e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 71.90  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 178 PGIRLHFVEMG--SGPALCLCHGFPESWFSWRYQIPALAqAGFRVLAIDMKGYGDSSspPEIEEYAMELLCKEMVTFLDK 255
Cdd:PRK14875 117 GGRTVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASS--KAVGAGSLDELAAAVLAFLDA 193

                         90       100       110
                 ....*....|....*....|....*....|...
gi 406647884 256 LGIPQAVFIGHDWAGVMVWNMALFYPERVRAVA 288
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLT 226
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
171-290 3.44e-13

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 68.89  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 171 HGYVTVKPGIRLHfvemgsgPALCLCHGFPES-WFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEY-----AMEL 244
Cdd:COG1506   11 PGWLYLPADGKKY-------PVVVYVHGGPGSrDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVddvlaAIDY 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 406647884 245 LCKEMVTFLDKLGIpqavfIGHDWAGVMVWNMALFYPERVRAVASL 290
Cdd:COG1506   84 LAARPYVDPDRIGI-----YGHSYGGYMALLAAARHPDRFKAAVAL 124
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 188-291 8.21e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 62.83  E-value: 8.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 188 GSGPALCLCHGFPESWFSWRYQIPALAQAGfRVLAIDMKGYGDSSSP-----PEIEEYAMELLCKEMVTFLDKLGIPQAV 262
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAF 105

                         90       100
                 ....*....|....*....|....*....
gi 406647884 263 FIGHDWAGVMVWNMALFYPERVRAVASLN 291
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLIN 134
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 37-131 2.71e-10

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: 59.52  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884   37 RPMLQAAI-ALKKKGFTTCIVTNnwlDDGDKRDSLAQMmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVV 115
Cdd:pfam00702 100 YPGAAEALkALKERGIKVAILTG---DNPEAAEALLRL-LGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVL 175

                          90
                  ....*....|....*.
gi 406647884  116 FLDDFGSNLKPARDMG 131
Cdd:pfam00702 176 MVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 35-137 1.33e-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: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  35 INRPMLQAaiaLKKKGFTTCIVTNNWLDDGDKRdsLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEV 114
Cdd:cd01427   11 LAVELLKR---LRAAGIKLAIVTNRSREALRAL--LEK--LGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEV 83

                         90       100
                 ....*....|....*....|...
gi 406647884 115 VFLDDFGSNLKPARDMGMVTILV 137
Cdd:cd01427   84 LFVGDSENDIEAARAAGGRTVAV 106
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
37-148 1.76e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 54.55  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  37 RPMLQAaiaLKKKGFTTCIVTNnwlddgdKRDSLAQMMCE---LSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNE 113
Cdd:COG0546   90 RELLEA---LKARGIKLAVVTN-------KPREFAERLLEalgLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEE 159

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 406647884 114 VVFLDDFGSNLKPARDMGMVTILV---HNTASALRELE 148
Cdd:COG0546  160 VLMVGDSPHDIEAARAAGVPFIGVtwgYGSAEELEAAG 197
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 192-303 2.79e-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: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  192 ALCLCHGFPESwfSWRYQ--IPALAQAGFRVLAIDMKGYGDSSSP----PEIEEYamellCKEMVTFLDKL-----GIPQ 260
Cdd:pfam12146   6 VVVLVHGLGEH--SGRYAhlADALAAQGFAVYAYDHRGHGRSDGKrghvPSFDDY-----VDDLDTFVDKIreehpGLPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 406647884  261 AVFiGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSP 303
Cdd:pfam12146  79 FLL-GHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPP 120
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 195-327 3.74e-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: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  195 LCHGfpesWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPP-EIEEYAmellckEMVTFLDKLGI-PQAVFIGHDWAGVM 272
Cdd:pfam12697   3 LVHG----AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPlDLADLA------DLAALLDELGAaRPVVLVGHSLGGAV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 406647884  273 VWNMALFYPERVRAVASLNTPFMPPDPDVSPMKviRSIPVFNYQLYFQEPGVAEA 327
Cdd:pfam12697  73 ALAAAAAALVVGVLVAPLAAPPGLLAALLALLA--RLGAALAAPAWLAAESLARG 125
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
46-137 3.82e-08

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 52.97  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884   46 LKKKGFTTCIVTNNWlddgdkRDSLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSN 123
Cdd:pfam13419  91 LKEQGYKLGIVTSKS------RENVEEFLkqLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRD 164

                          90
                  ....*....|....
gi 406647884  124 LKPARDMGMVTILV 137
Cdd:pfam13419 165 IEAAKNAGIKVIAV 178
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 189-265 5.53e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 54.85  E-value: 5.53e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406647884 189 SGPALCLCHGFPESWFSWRYQIPALAQAgFRVLAIDMKGYGDSSSPPEIeEYAMELLCKEMVTFLDKLGIPQAVFIG 265
Cdd:PLN02679  87 SGPPVLLVHGFGASIPHWRRNIGVLAKN-YTVYAIDLLGFGASDKPPGF-SYTMETWAELILDFLEEVVQKPTVLIG 161
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 195-294 1.06e-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: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 195 LCHGFPESWFSWRYQIPALAQAGFRVLAIDmkgYGDSSSPpeIEEYAMELLckemvTFLDKL----GIPQAVFIGHDWAG 270
Cdd:COG1075   10 LVHGLGGSAASWAPLAPRLRAAGYPVYALN---YPSTNGS--IEDSAEQLA-----AFVDAVlaatGAEKVDLVGHSMGG 79

                         90       100
                 ....*....|....*....|....*.
gi 406647884 271 VMVWNMA--LFYPERVRAVASLNTPF 294
Cdd:COG1075   80 LVARYYLkrLGGAAKVARVVTLGTPH 105
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 76-139 1.93e-07

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 51.58  E-value: 1.93e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406647884  76 ELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 139
Cdd:PRK09456 123 EVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILVTD 186
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 35-139 7.05e-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: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  35 INRPMLQAaiaLKKKGFTTCIVTNNwlddgDKRdsLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPN 112
Cdd:cd16415   11 LAVETLKD---LKEKGLKLAVVSNF-----DRR--LRELLeaLGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPE 80

                         90       100
                 ....*....|....*....|....*...
gi 406647884 113 EVVFL-DDFGSNLKPARDMGMVTILVHN 139
Cdd:cd16415   81 EALHVgDDLKNDYLGARAVGWHALLVDR 108
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 48-135 1.06e-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: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  48 KKGFTTCIVTNnwlddGDK---RDSLAQmmCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFL-DDFGSN 123
Cdd:cd04305   22 KKGYKLGIITN-----GPTevqWEKLEQ--LGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVgDSLESD 94

                         90
                 ....*....|..
gi 406647884 124 LKPARDMGMVTI 135
Cdd:cd04305   95 ILGAKNAGIKTV 106
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
24-150 1.14e-06

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 49.44  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  24 QIFSQAMAARSIN-RPMLQAAI-ALKKKGFTTCIVTNNwlddgdKRDSLAQMM--CELSQHFDFLIESCQVGMIKPEPQI 99
Cdd:COG0637   74 ELYRELLAEEGLPlIPGVVELLeALKEAGIKIAVATSS------PRENAEAVLeaAGLLDYFDVIVTGDDVARGKPDPDI 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 406647884 100 YNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKV 150
Cdd:COG0637  148 YLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGA 198
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
184-347 1.71e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 49.17  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 184 FVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGdsSSPPEIE-----------EYAMELLCKEMvtf 252
Cdd:COG1647    9 FFLEGGRKGVLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHG--TSPEDLLkttwedwledvEEAYEILKAGY--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 253 lDKLGIpqavfIGHDWAGVMVWNMALFYPErVRAVASLNTPFMPPDPDVSPMKVIRSIP--VFNYQLYFQEPGVAEAELE 330
Cdd:COG1647   84 -DKVIV-----IGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYLArsLRGIGSDIEDPEVAEYAYD 156

                        170
                 ....*....|....*..
gi 406647884 331 KNMSRTFKSFFRASDET 347
Cdd:COG1647  157 RTPLRALAELQRLIREV 173
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 174-294 3.46e-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: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 174 VTVKPGIRLH---FV---EMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCK 247
Cdd:COG1073   15 FKSRDGIKLAgdlYLpagASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERRDAR 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 406647884 248 EMVTFL-DKLGIPQA--VFIGHDWAGVMVWNMALFYPeRVRAVASLnTPF 294
Cdd:COG1073   95 AAVDYLrTLPGVDPEriGLLGISLGGGYALNAAATDP-RVKAVILD-SPF 142
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 45-137 6.05e-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: 6.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  45 ALKKKGFTTCIVTNnwlddGDkRDSLAQMM--CELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGS 122
Cdd:cd02588  102 RLREAGYRLAILSN-----GS-PDLIEDVVanAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAW 175

                         90
                 ....*....|....*
gi 406647884 123 NLKPARDMGMVTILV 137
Cdd:cd02588  176 DLAGARALGLRTAWI 190
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
188-312 1.11e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 46.50  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 188 GSGPALCLCHGfpesWFSWRYQIPA----LAQAGFRVLAIDM-KGYGDSSSPPEIEEYAMELLCKEMVT-------FL-- 253
Cdd:COG0412   27 GPRPGVVVLHE----IFGLNPHIRDvarrLAAAGYVVLAPDLyGRGGPGDDPDEARALMGALDPELLAAdlraaldWLka 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406647884 254 ------DKLGIpqavfIGHDWAGVMVWNMALFYPeRVRAVASLNtPFMPPDPDVSPMKVIRsIPV 312
Cdd:COG0412  103 qpevdaGRVGV-----VGFCFGGGLALLAAARGP-DLAAAVSFY-GGLPADDLLDLAARIK-APV 159
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 37-150 1.66e-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: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  37 RPMLQAaiaLKKKGFTTCIVTNnwlddgdKRDSLAQM---MCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNE 113
Cdd:cd02616   86 YETLAR---LKSQGIKLGVVTT-------KLRETALKglkLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEE 155

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 406647884 114 VVFLDDFGSNLKPARDMGMVTILVhntASALRELEKV 150
Cdd:cd02616  156 ALMVGDSPHDILAGKNAGVKTVGV---TWGYKGREYL 189
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 191-308 2.00e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 46.83  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 191 PALCLCHGFPESW-FSWRyQIPALAqAGFRVLAIDMKGYGDSSSPP-------EIEEYamellckemvtFLDKL------ 256
Cdd:PLN02894 106 PTLVMVHGYGASQgFFFR-NFDALA-SRFRVIAIDQLGWGGSSRPDftcksteETEAW-----------FIDSFeewrka 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 406647884 257 -GIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIR 308
Cdd:PLN02894 173 kNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDKSEWLTK 225
PRK10673 PRK10673
esterase;
220-284 3.96e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.11  E-value: 3.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406647884 220 VLAIDMKGYGDSSSPPEIEEYAMellCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERV 284
Cdd:PRK10673  45 IIQVDMRNHGLSPRDPVMNYPAM---AQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRI 106
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 181-296 8.60e-05

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 44.87  E-value: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884 181 RLHFVEMGS--GPALCLCHGFPESWFSWRYQIPALAQaGFRVLAIDMKGYGDSSSPP-------EIEEY--AMELLCKEM 249
Cdd:PLN03084 116 RWFCVESGSnnNPPVLLIHGFPSQAYSYRKVLPVLSK-NYHAIAFDWLGFGFSDKPQpgygfnyTLDEYvsSLESLIDEL 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 406647884 250 VTflDKLGIpqaVFIGHdWAGVMVwNMALFYPERVRAVASLNTPFMP 296
Cdd:PLN03084 195 KS--DKVSL---VVQGY-FSPPVV-KYASAHPDKIKKLILLNPPLTK 234
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 45-139 3.35e-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: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  45 ALKKKGFTTCIVTNNWLDDGDKRDSLAQmmcELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNL 124
Cdd:cd07505   52 ALKAAGIPVAVATSSSRRNVELLLLELG---LLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSLAGI 128

                         90
                 ....*....|....*
gi 406647884 125 KPARDMGMVTILVHN 139
Cdd:cd07505  129 EAAKAAGMTVVAVPD 143
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 77-139 1.08e-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: 1.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406647884  77 LSQHFDFLIESCQVGMI-KPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHN 139
Cdd:cd02604  119 LADLFDGIFDIEYAGPDpKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVGP 182
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
46-137 1.32e-03

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 39.34  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  46 LKKKGFTTCIVTNNWlddgDKR-DSLAQMMcelsqHFDFLIESCqvgmiKPEPQIYNFLLDTLKAKPNEVVFLDD----- 119
Cdd:COG2179   56 LKEAGFKVCIVSNNS----EKRvKRFAEKL-----GIPYIARAK-----KPLPRGFRKALKLMGLPPEETAVVGDqlftd 121

                         90
                 ....*....|....*....
gi 406647884 120 -FGSNLkpardMGMVTILV 137
Cdd:COG2179  122 vLGGNR-----AGLYTILV 135
Hydrolase_like pfam13242
HAD-hyrolase-like;
94-137 1.35e-03

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 37.60  E-value: 1.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 406647884   94 KPEPQIYNFLLDTLKAKPNEVVFL-DDFGSNLKPARDMGMVTILV 137
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIgDRLDTDILGAREAGARTILV 48
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 38-137 9.15e-03

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong 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 (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. 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 35.90  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406647884  38 PMLQAaiaLKKKGFTTCIVTNnwlddgdKRDSLAQMMCE--LSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVV 115
Cdd:cd16421   14 ELLKA---LRQKGIKLAVLSN-------KPNEAVQVLVEelFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVL 83

                         90       100
                 ....*....|....*....|..
gi 406647884 116 FLDDFGSNLKPARDMGMVTILV 137
Cdd:cd16421   84 YVGDSGVDMQTARNAGMDEIGV 105
 
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.
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