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Conserved domains on  [gi|656214657|ref|NP_001280638|]
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antizyme inhibitor 2 [Cricetulus griseus]

Protein Classification

type III PLP-dependent enzyme( domain architecture ID 10089786)

type III PLP-dependent enzyme similar to Selenomonas ruminantium lysine/ornithine decarboxylase, and human ornithine decarboxylase and antizyme inhibitor 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-392 1.81e-173

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


:

Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 490.85  E-value: 1.81e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  40 AFFVADLGAVVRKHFCFLKYLPRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 120 QIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSLNHLSLRFGASLKSCRHLLENAKKSHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 200 GSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLE-GAKVRFEEIASVINSALDLYFPEGcGVDILAELGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 279 YYVTSAFTVAVSIVAKKEALLDQPSREeetssapktivYHLDEGVYGIFNSVLFDNNCPTPTLQKNPSADQPLYSSSLWG 358
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 656214657 359 PAVDGSDRVAEGLWLPQ-LHVGDWLVFDNMGAYTM 392
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTT 345
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-392 1.81e-173

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 490.85  E-value: 1.81e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  40 AFFVADLGAVVRKHFCFLKYLPRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 120 QIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSLNHLSLRFGASLKSCRHLLENAKKSHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 200 GSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLE-GAKVRFEEIASVINSALDLYFPEGcGVDILAELGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 279 YYVTSAFTVAVSIVAKKEALLDQPSREeetssapktivYHLDEGVYGIFNSVLFDNNCPTPTLQKNPSADQPLYSSSLWG 358
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 656214657 359 PAVDGSDRVAEGLWLPQ-LHVGDWLVFDNMGAYTM 392
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTT 345
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 41-388 3.54e-112

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 334.07  E-value: 3.54e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657   41 FFVADLGAVVRKHFCFLKYL-PRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIA 119
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  120 QIKYAAKHGVRLLSFDNEVELAKVVKSHPS--AKMVLCIATQDSHSLNHLSL-----RFGASLKSCRHLLENAKKSHVEV 192
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGTHKISTgglssKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  193 VGVSFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPG--LEGAKVRFEEIASVINSALDLYFPEgcGV 270
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIpyRDEPPPDFEEYAAAIREALDEYFPP--DL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  271 DILAELGRYYVTSAFTVAVSIVAKKEalldqpsreeetsSAPKTIVYhLDEGVYGIFNSVLFDNNCPTPTlqKNPSADQP 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 656214657  351 LYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMG 388
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 41-392 1.86e-47

Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 168.40  E-value: 1.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  41 FFVADLgAVVRKHFCFLKYL---PRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQ 117
Cdd:COG0019   28 LYVYDE-AALRRNLRALREAfpgSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 118 IAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIA----------TQDSHSLNHLSLRFGASLKSCRHLLENAKK 187
Cdd:COG0019  107 EEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGlrvnpgvdagTHEYISTGGKDSKFGIPLEDALEAYRRAAA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 188 S-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFP---GLEGAKVRFEEIASVINSALDLY 263
Cdd:COG0019  187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEEL 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 264 FpeGCGVDILAELGRYYVTSAFTVAVSIVAKKEalldqpsreeetsSAPKTIVYhLDEGVygifnsvlfdNNCPTPTLQK 343
Cdd:COG0019  267 C--GLGPELILEPGRALVGNAGVLLTRVLDVKE-------------NGGRRFVI-VDAGM----------NDLMRPALYG 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 656214657 344 --------NPSADQPLYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTM 392
Cdd:COG0019  321 ayhpivpvGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGF 377
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-284 5.63e-10

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 61.64  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  66 FYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHI--GVPASKIICANPCKQIAQIKYAAKHGVrLLSFDNEVELAKV 143
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNW 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 144 VKSHPSAKMVLCI--ATQDSHslnHLSLR-------FGASLKSCRHLLENAKKSHVEVVGVSFHIGSGCPDPQAYAQsIA 214
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGH---HEKVRtggkeskFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MA 684

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 656214657 215 D--ARLVFQMGaelghTMNILDLGGGFPGLEGAKVR---FEEIASVINSALDLYfPegcGVDILAELGRYYVTSA 284
Cdd:PRK08961 685 DelASFARRFP-----DVRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLVAEA 750
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-392 1.81e-173

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 490.85  E-value: 1.81e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  40 AFFVADLGAVVRKHFCFLKYLPRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 120 QIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSLNHLSLRFGASLKSCRHLLENAKKSHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 200 GSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLE-GAKVRFEEIASVINSALDLYFPEGcGVDILAELGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 279 YYVTSAFTVAVSIVAKKEALLDQPSREeetssapktivYHLDEGVYGIFNSVLFDNNCPTPTLQKNPSADQPLYSSSLWG 358
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 656214657 359 PAVDGSDRVAEGLWLPQ-LHVGDWLVFDNMGAYTM 392
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTT 345
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 32-415 1.43e-140

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor; Antizyme inhibitor (AZI) is homologous to the fold type III PLP-dependent enzyme ODC but does not retain any decarboxylase activity. Like ODC, AZI is presumed to exist as a homodimer. Antizyme is a regulatory protein that binds directly to the ODC monomer to block its active site, leading to its degradation by the 26S proteasome. AZI binds to Antizyme with a higher affinity than ODC, preventing the formation of the Antizyme-ODC complex. Thus, AZI blocks the ability of Antizyme to promote ODC degradation, which leads to increased ODC enzymatic activity and polyamine levels. AZI also prevents the degradation of other proteins regulated by Antizyme, such as cyclin D1.


Pssm-ID: 143504  Cd Length: 394  Bit Score: 408.47  E-value: 1.43e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  32 QATTGKvAAFFVADLGAVVRKHFCFLKYLPRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIC 111
Cdd:cd06831    7 HTLTGK-NAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 112 ANPCKQIAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSLNHLSLRFGASLKSCRHLLENAKKSHVE 191
Cdd:cd06831   86 TNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 192 VVGVSFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFpglEGAKVRFEEIASVINSALDLYFPEGCGVD 271
Cdd:cd06831  166 IVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGF---TGSEIQLEEVNHVIRPLLDVYFPEGSGIQ 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 272 ILAELGRYYVTSAFTVAVSIVAKKEALLDQ--PSREEETSSAPkTIVYHLDEGVYGIFNSVLFDNNCPTPTLQKNPSADQ 349
Cdd:cd06831  243 IIAEPGSYYVSSAFTLAVNVIAKKAVENDKhlSSVEKNGSDEP-AFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDE 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 656214657 350 PLYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTMDTKSLLGGTQAYRITYAMSRLAW 415
Cdd:cd06831  322 PLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDW 387
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 41-388 3.54e-112

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 334.07  E-value: 3.54e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657   41 FFVADLGAVVRKHFCFLKYL-PRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIA 119
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  120 QIKYAAKHGVRLLSFDNEVELAKVVKSHPS--AKMVLCIATQDSHSLNHLSL-----RFGASLKSCRHLLENAKKSHVEV 192
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGTHKISTgglssKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  193 VGVSFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPG--LEGAKVRFEEIASVINSALDLYFPEgcGV 270
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIpyRDEPPPDFEEYAAAIREALDEYFPP--DL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  271 DILAELGRYYVTSAFTVAVSIVAKKEalldqpsreeetsSAPKTIVYhLDEGVYGIFNSVLFDNNCPTPTlqKNPSADQP 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 656214657  351 LYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMG 388
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 46-281 5.47e-96

Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates This domain has a TIM barrel fold.


Pssm-ID: 397077 [Multi-domain]  Cd Length: 241  Bit Score: 288.80  E-value: 5.47e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657   46 LGAVVRKHFCFLKYLPRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIAQIKYAA 125
Cdd:pfam02784   1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  126 KHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSLNHLSLRFGASL-KSCRHLLENAKKSHVEVVGVSFHIGSGCP 204
Cdd:pfam02784  81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  205 DPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFpGLE----GAKVRFEEIASVINSALDLYFPEGCGVDILAELGRYY 280
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDytegEEPLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239


                  .
gi 656214657  281 V 281
Cdd:pfam02784 240 V 240
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 39-394 5.83e-96

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes; This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family.


Pssm-ID: 143485 [Multi-domain]  Cd Length: 368  Bit Score: 293.44  E-value: 5.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  39 AAFFVADLGAVVRKHFCFLKYLP-RVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQ 117
Cdd:cd06810    1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 118 IAQIKYAAKHGVRLLSFDNEVELAKVV----KSHPSAKMVLCIATQDSHSLNHLSL-----RFGASLKSCRHLLENAKKS 188
Cdd:cd06810   81 VSEIEAALASGVDHIVVDSLDELERLNelakKLGPKARILLRVNPDVSAGTHKISTgglksKFGLSLSEARAALERAKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 189 HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPG-LEGAKVRFEEIASVINSALDLYFPEG 267
Cdd:cd06810  161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIpYDEQPLDFEEYAALINPLLKKYFPND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 268 CGVDILAELGRYYVTSAFTVAVSIVAKKEalldqpsreeetssAPKTIVYHLDEGVYGIFNSVLFDNNCPTPTLQKNPSA 347
Cdd:cd06810  241 PGVTLILEPGRYIVAQAGVLVTRVVAVKV--------------NGGRFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGP 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 656214657 348 DQPLYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTMDT 394
Cdd:cd06810  307 DEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSE 353
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 41-392 1.86e-47

Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 168.40  E-value: 1.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  41 FFVADLgAVVRKHFCFLKYL---PRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQ 117
Cdd:COG0019   28 LYVYDE-AALRRNLRALREAfpgSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 118 IAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIA----------TQDSHSLNHLSLRFGASLKSCRHLLENAKK 187
Cdd:COG0019  107 EEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGlrvnpgvdagTHEYISTGGKDSKFGIPLEDALEAYRRAAA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 188 S-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFP---GLEGAKVRFEEIASVINSALDLY 263
Cdd:COG0019  187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEEL 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 264 FpeGCGVDILAELGRYYVTSAFTVAVSIVAKKEalldqpsreeetsSAPKTIVYhLDEGVygifnsvlfdNNCPTPTLQK 343
Cdd:COG0019  267 C--GLGPELILEPGRALVGNAGVLLTRVLDVKE-------------NGGRRFVI-VDAGM----------NDLMRPALYG 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 656214657 344 --------NPSADQPLYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTM 392
Cdd:COG0019  321 ayhpivpvGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGF 377
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 61-243 8.95e-44

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.


Pssm-ID: 143484 [Multi-domain]  Cd Length: 211  Bit Score: 152.86  E-value: 8.95e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  61 PRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIAQIKYAAKHGVRLLSFDNEVEL 140
Cdd:cd06808   14 AGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSLEEL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 141 AKV----VKSHPSAKMVLCIATqdshslNHLSLRFGASLKSCRHLLENAKKS-HVEVVGVSFHIGSGCPDPQAYAQSIAD 215
Cdd:cd06808   94 EKLeeaaLKAGPPARVLLRIDT------GDENGKFGVRPEELKALLERAKELpHLRLVGLHTHFGSADEDYSPFVEALSR 167

                        170       180
                 ....*....|....*....|....*...
gi 656214657 216 ARLVFQMGAELGHTMNILDLGGGFPGLE 243
Cdd:cd06808  168 FVAALDQLGELGIDLEQLSIGGSFAILY 195
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 61-392 1.51e-32

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.


Pssm-ID: 143501 [Multi-domain]  Cd Length: 373  Bit Score: 126.83  E-value: 1.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  61 PRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIAQIKYAAKHGVRLLSFDNEVEL 140
Cdd:cd06828   27 PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSDEELELALELGILRINVDSLSEL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 141 AKVVKSHPSAKMVLCIA----------TQDSHSLNHLSLRFGASLKSCRHLLENAKKS-HVEVVGVSFHIGSGCPDPQAY 209
Cdd:cd06828  107 ERLGEIAPELGKGAPVAlrvnpgvdagTHPYISTGGKDSKFGIPLEQALEAYRRAKELpGLKLVGLHCHIGSQILDLEPF 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 210 AQSiadARLVFQMGAEL---GHTMNILDLGGGFpGL----EGAKVRFEEIASVINSALDLYFPEGCGVDILAELGRYYVT 282
Cdd:cd06828  187 VEA---AEKLLDLAAELrelGIDLEFLDLGGGL-GIpyrdEDEPLDIEEYAEAIAEALKELCEGGPDLKLIIEPGRYIVA 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 283 SAFTVAVSIVAKKEalldqpsreeetsSAPKTIVyHLDEGvygiFNS----VLFDNNCPTPTLqkNPSADQPLYSSSLWG 358
Cdd:cd06828  263 NAGVLLTRVGYVKE-------------TGGKTFV-GVDAG----MNDlirpALYGAYHEIVPV--NKPGEGETEKVDVVG 322

                        330       340       350
                 ....*....|....*....|....*....|....
gi 656214657 359 PAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTM 392
Cdd:cd06828  323 PICESGDVFAKDRELPEVEEGDLLAIHDAGAYGY 356
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 41-395 1.10e-30

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of uncharacterized proteins with similarity to Escherichia coli MccE, a hypothetical protein that is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Most members of this subfamily share the same domain architecture as ODC and DapDC. A few members, including Escherichia coli MccE, contain an additional acetyltransferase domain at the C-terminus.


Pssm-ID: 143508 [Multi-domain]  Cd Length: 379  Bit Score: 121.99  E-value: 1.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  41 FFVADLGAVVRKHFCFL----KYLPRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCK 116
Cdd:cd06841    9 FFVFDEDALRENYRELLgafkKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGPYK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 117 QIAQIKYAAKHGVrLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSL-NHLSLRFGASLKSCRHLLENAKKS----HVE 191
Cdd:cd06841   89 SKEELEKALEEGA-LINIDSFDELERILEIAKELGRVAKVGIRLNMNYgNNVWSRFGFDIEENGEALAALKKIqeskNLS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 192 VVGVSFHIGSGCPDPQAYAQSIADarLVFQMGAELGHTMNILDLGGGFPG---LEGAKVR------FEEIASVINSALDL 262
Cdd:cd06841  168 LVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPAktpLSLAYPQedtvpdPEDYAEAIASTLKE 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 263 YFPEGCGVDILA-ELGRYYVTSAFTVAVSIVAKKEalldQPSREeetssapktiVYHLDEGVygifnsvlfdNNCPTPTL 341
Cdd:cd06841  246 YYANKENKPKLIlEPGRALVDDAGYLLGRVVAVKN----RYGRN----------IAVTDAGI----------NNIPTIFW 301

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 656214657 342 QK------NPSADQPLYSSS-LWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTMDTK 395
Cdd:cd06841  302 YHhpilvlRPGKEDPTSKNYdVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQS 362
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 41-390 1.40e-21

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is composed of Bacillus circulans BtrK decarboxylase and similar proteins. These proteins are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases, eukaryotic ornithine decarboxylases and diaminopimelate decarboxylases. BtrK is presumed to function as a PLP-dependent decarboxylase involved in the biosynthesis of the aminoglycoside antibiotic butirosin. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.


Pssm-ID: 143506 [Multi-domain]  Cd Length: 382  Bit Score: 96.12  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  41 FFVADLgAVVRKHFCFL-KYLPR-VRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQI 118
Cdd:cd06839    9 FYVYDR-DRVRERYAALrAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 119 AQIKYAAKHGVRLLSFDNEVELAKV----VKSHPSAKMVLCIAtqDSHSLNHLSLR-------FG----------ASLKS 177
Cdd:cd06839   88 AELRRAIEAGIGTINVESLEELERIdalaEEHGVVARVALRIN--PDFELKGSGMKmgggpsqFGidveelpavlARIAA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 178 CRHLlenakkshvEVVGVSFHIGSGCPDPQAYAQSIADA-RLVFQMGAELGHTMNILDLGGGF-----PGleGAKVRFEE 251
Cdd:cd06839  166 LPNL---------RFVGLHIYPGTQILDADALIEAFRQTlALALRLAEELGLPLEFLDLGGGFgipyfPG--ETPLDLEA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 252 IASVINSALDLYFPEGCGVDILAELGRYYVTSAFTVAVSIVAKKEalldqpSREEetssapkTIVYhLDEGVY------G 325
Cdd:cd06839  235 LGAALAALLAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV------SRGE-------TFLV-TDGGMHhhlaasG 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 656214657 326 IFNSVLFDNncpTPTLQKNPSADQPLYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAY 390
Cdd:cd06839  301 NFGQVLRRN---YPLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAY 362
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 68-396 7.59e-19

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with similarity to Ornithine and Diaminopimelate Decarboxylases; This subfamily contains uncharacterized proteins with similarity to ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.


Pssm-ID: 143505 [Multi-domain]  Cd Length: 379  Bit Score: 87.83  E-value: 7.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  68 AVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIAQIKYAAKHGVRlLSFDNEVELAKV---V 144
Cdd:cd06836   33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVA-INIDNFQELERIdalV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 145 KSHPSAKMVLCI----------------ATQDShslnhlslRFGASLK-SCRHLLENAKKSHVEVVGVSFHIGS-GCPDP 206
Cdd:cd06836  112 AEFKEASSRIGLrvnpqvgagkigalstATATS--------KFGVALEdGARDEIIDAFARRPWLNGLHVHVGSqGCELS 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 207 QAyAQSIADA-RLVFQMGAELG-HTMNILDLGGGFP---GLEGAKVRFEEIASVINSALDLYFPEGCGVdiLAELGRYYV 281
Cdd:cd06836  184 LL-AEGIRRVvDLAEEINRRVGrRQITRIDIGGGLPvnfESEDITPTFADYAAALKAAVPELFDGRYQL--VTEFGRSLL 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 282 TSAFTVaVSIV--AKK---------EALLDQPSReeeTSSAPKtiVYHLDEGVYgifnsvlfdnncptpTLQKNPSADqP 350
Cdd:cd06836  261 AKCGTI-VSRVeyTKSsggrriaitHAGAQVATR---TAYAPD--DWPLRVTVF---------------DANGEPKTG-P 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 656214657 351 LYSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTMDTKS 396
Cdd:cd06836  319 EVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHS 364
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 43-240 8.75e-17

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.


Pssm-ID: 143509 [Multi-domain]  Cd Length: 423  Bit Score: 81.92  E-value: 8.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  43 VADLGAVVRKHFCflkylpRVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIAQIK 122
Cdd:cd06842   24 IAALRAVLDRHGV------DGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLW 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 123 YAAKHGVrLLSFDNEVELAKVVK--SHPSAKMV-----LCIATQDSHSlnhlslRFGASLKSCRHLLENAKKS--HVEVV 193
Cdd:cd06842   98 LAVRHGA-TIAVDSLDELDRLLAlaRGYTTGPArvllrLSPFPASLPS------RFGMPAAEVRTALERLAQLreRVRLV 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 656214657 194 GVSFHIGSGCPDPQAYAqsIADARLVFQMGAELGHTMNILDLGGGFP 240
Cdd:cd06842  171 GFHFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGGGFP 215
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 64-390 4.62e-13

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase/Diaminopimelate Decarboxylase; Bifunctional aspartate kinase/diaminopimelate decarboxylase (AspK/DapDC, EC 4.1.1.20/EC 2.7.2.4) typically exists in bacteria. These proteins contain an N-terminal AspK region and a C-terminal DapDC region, which contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, characteristic of fold type III PLP-dependent enzymes. Members of this subfamily have not been fully characterized. Based on their sequence, these proteins may catalyze both reactions catalyzed by AspK and DapDC. AspK catalyzes the phosphorylation of L-aspartate to produce 4-phospho-L-aspartate while DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine.


Pssm-ID: 143507 [Multi-domain]  Cd Length: 368  Bit Score: 70.16  E-value: 4.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  64 RPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHI--GVPASKIICANPCKQIAQIKYAAKHGVRLlSFDNEVELA 141
Cdd:cd06840   37 SLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVNV-TVDNLHPLR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 142 KVVKSHPSAKMVLCIATQ--DSHSlNHLSL-----RFGASLKSCRHLLENAKKSHVEVVGVSFHIGSGCPDPQAYAQSIA 214
Cdd:cd06840  116 EWPELFRGREVILRIDPGqgEGHH-KHVRTggpesKFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGD 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 215 D-ARLVFQMGAelghtMNILDLGGGFPGLEGAKVRFEEIASVINS--ALDLYFPegcGVDILAELGRYyvtsaftvavsI 291
Cdd:cd06840  195 YlASLARHFPA-----VRILNVGGGLGIPEAPGGRPIDLDALDAAlaAAKAAHP---QYQLWMEPGRF-----------I 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 292 VAKKEALLdqpSREEETSSAPKTIVYHLDEGVYGIFNSVLFDNNCPTPTLQKNpsADQPLYSSSLWGPAVDGSDRVAEGL 371
Cdd:cd06840  256 VAESGVLL---ARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEIVNLSRL--DEPPAGNADVVGPICESGDVLGRDR 330

                        330
                 ....*....|....*....
gi 656214657 372 WLPQLHVGDWLVFDNMGAY 390
Cdd:cd06840  331 LLPETEEGDVILIANAGAY 349
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-284 5.63e-10

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 61.64  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  66 FYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHI--GVPASKIICANPCKQIAQIKYAAKHGVrLLSFDNEVELAKV 143
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNW 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 144 VKSHPSAKMVLCI--ATQDSHslnHLSLR-------FGASLKSCRHLLENAKKSHVEVVGVSFHIGSGCPDPQAYAQsIA 214
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGH---HEKVRtggkeskFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MA 684

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 656214657 215 D--ARLVFQMGaelghTMNILDLGGGFPGLEGAKVR---FEEIASVINSALDLYfPegcGVDILAELGRYYVTSA 284
Cdd:PRK08961 685 DelASFARRFP-----DVRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLVAEA 750
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 42-239 6.88e-09

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.


Pssm-ID: 143510 [Multi-domain]  Cd Length: 377  Bit Score: 57.29  E-value: 6.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  42 FVADLGAVvRKHFCFLK-YLP-RVRPFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIgVPASKIICANPCKQIA 119
Cdd:cd06843    5 YVYDLAAL-RAHARALRaSLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA-VPDAPLIFGGPGKTDS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 120 QIKYAAKHGVRLLSFDNEVELAK---VVKSHPSAKMVLCIATQDSHSLNHLSLR-------FG---ASLKSCRHLLENAk 186
Cdd:cd06843   83 ELAQALAQGVERIHVESELELRRlnaVARRAGRTAPVLLRVNLALPDLPSSTLTmggqptpFGideADLPDALELLRDL- 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 656214657 187 kSHVEVVGVSFHIGSGCPDPQAYAQSIAD-ARLVFQMGAELGHTMNILDLGGGF 239
Cdd:cd06843  162 -PNIRLRGFHFHLMSHNLDAAAHLALVKAyLETARQWAAEHGLDLDVVNVGGGI 214
PLN02537 PLN02537
diaminopimelate decarboxylase
 65-396 3.99e-06

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 49.02  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  65 PFYAVKCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQIAQIKYAAKHGVrLLSFDNEVELAKVV 144
Cdd:PLN02537  46 IGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 145 ----KSHPSAKMVLCI------------ATQDSHSlnhlslRFGASLKSCRHLLENAKK--SHVEVVGVSFHIGSGCPDP 206
Cdd:PLN02537 125 eaarIAGKKVNVLLRInpdvdpqvhpyvATGNKNS------KFGIRNEKLQWFLDAVKAhpNELKLVGAHCHLGSTITKV 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 207 QAYaqsiADARLVF-----QMGAElGHTMNILDLGGGFpGLE----GAKVrfEEIASVINSALDLYFPEgcGVDILAELG 277
Cdd:PLN02537 199 DIF----RDAAVLMvnyvdEIRAQ-GFELSYLNIGGGL-GIDyyhaGAVL--PTPRDLIDTVRELVLSR--DLTLIIEPG 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 278 RYYV--TSAFTVAVSIV----AKKEALLDQPSREEETSSapktivyhldegVYGIFNSVlfdnncptpTLQKNPSADQPL 351
Cdd:PLN02537 269 RSLIanTCCFVNRVTGVktngTKNFIVIDGSMAELIRPS------------LYDAYQHI---------ELVSPPPPDAEV 327

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 656214657 352 YSSSLWGPAVDGSDRVAEGLWLPQLHVGDWLVFDNMGAYTMDTKS 396
Cdd:PLN02537 328 STFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMAS 372
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
 170-275 6.11e-03

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 38.12  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657  170 RFGASLKSCRHLLENAKKSHVEVVGVSFHIGSGC--PDPQAYAQSIADARLVFQMGAELG-HTMNILdlgGGFPGLEGAK 246
Cdd:pfam01261  21 RPPLSDEEAEELKAALKEHGLEIVVHAPYLGDNLasPDEEEREKAIDRLKRAIELAAALGaKLVVFH---PGSDLGDDPE 97

                          90       100
                  ....*....|....*....|....*....
gi 656214657  247 VRFEEIASVINSALDlyFPEGCGVDILAE 275
Cdd:pfam01261  98 EALARLAESLRELAD--LAEREGVRLALE 124
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
177-275 8.51e-03

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 38.07  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656214657 177 SCRHLLENAKKSHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFQMGAELGHTMNILDLGGGFPGLEGAKVRFEEIASVI 256
Cdd:COG1082   41 DLAELRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDRLAERL 120

                         90
                 ....*....|....*....
gi 656214657 257 NSALDLYfpEGCGVDILAE 275
Cdd:COG1082  121 RELAELA--EEAGVTLALE 137
 
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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