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Conserved domains on  [gi|1524699473|ref|WP_124225685|]
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alanine racemase [Staphylococcus pettenkoferi]

Protein Classification

type III PLP-dependent enzyme domain-containing protein( domain architecture ID 469)

type III PLP (pyridoxal 5-phosphate)-dependent enzyme domain-containing protein, similar to alanine racemase which catalyzes the interconversion of L-alanine and D-alanine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III super family cl00261
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 16-374 8.43e-138

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.


The actual alignment was detected with superfamily member cd06843:

Pssm-ID: 469695 [Multi-domain]  Cd Length: 377  Bit Score: 397.42  E-value: 8.43e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSA--TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAPMIYGGPVKTRGNL 93
Cdd:cd06843     5 YVYDLAALRAHARALRASlpPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDAPLIFGGPGKTDSEL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  94 AYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINL-SNIESSAKLKMAGVPTQFGLPYEDLEEAFEICEATPEL 172
Cdd:cd06843    85 AQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLaLPDLPSSTLTMGGQPTPFGIDEADLPDALELLRDLPNI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 173 QLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSS--RLPADYaINVGGGIGINYE-GETQFDFETFASQI-------ED 242
Cdd:cd06843   165 RLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAehGLDLDV-VNVGGGIGVNYAdPEEQFDWAGFCEGLdqllaeyEP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 243 FPQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILPTETTS---SRVkSIENQQVT 319
Cdd:cd06843   244 GLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPAAWGHNHPFSVLPVEEWPypwPRP-SVRDTPVT 322

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1524699473 320 LAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDISHLQFLSHNLPKIKFI 374
Cdd:cd06843   323 LVGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYGWNISHHDFLMHPHPERIYL 377
 
Name Accession Description Interval E-value
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 16-374 8.43e-138

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: 397.42  E-value: 8.43e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSA--TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAPMIYGGPVKTRGNL 93
Cdd:cd06843     5 YVYDLAALRAHARALRASlpPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDAPLIFGGPGKTDSEL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  94 AYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINL-SNIESSAKLKMAGVPTQFGLPYEDLEEAFEICEATPEL 172
Cdd:cd06843    85 AQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLaLPDLPSSTLTMGGQPTPFGIDEADLPDALELLRDLPNI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 173 QLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSS--RLPADYaINVGGGIGINYE-GETQFDFETFASQI-------ED 242
Cdd:cd06843   165 RLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAehGLDLDV-VNVGGGIGVNYAdPEEQFDWAGFCEGLdqllaeyEP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 243 FPQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILPTETTS---SRVkSIENQQVT 319
Cdd:cd06843   244 GLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPAAWGHNHPFSVLPVEEWPypwPRP-SVRDTPVT 322

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1524699473 320 LAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDISHLQFLSHNLPKIKFI 374
Cdd:cd06843   323 LVGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYGWNISHHDFLMHPHPERIYL 377
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 16-352 1.03e-87

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: 268.20  E-value: 1.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSA--TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATA-PMIYGGPVKTRGN 92
Cdd:pfam00278   2 YVYDLATLRRNYRRWKAAlpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPeRIVFAGPGKTDSE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  93 LAYALEHQVKSIQVESLYELDALQSLLAdsERSVEVMLRINLSNIESSAKLKMAGVPTQFGLPYEDLEEAFEICEATpEL 172
Cdd:pfam00278  82 IRYALEAGVLCFNVDSEDELEKIAKLAP--ELVARVALRINPDVDAGTHKISTGGLSSKFGIDLEDAPELLALAKEL-GL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 173 QLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSR-LPADYaINVGGGIGINYEGETQFDFETFASQI-----EDFP-- 244
Cdd:pfam00278 159 NVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELgIDLKL-LDIGGGFGIPYRDEPPPDFEEYAAAIrealdEYFPpd 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 245 -QLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILPTETTSSRVKsienqqVTLAGK 323
Cdd:pfam00278 238 lEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLET------YDVVGP 311

                         330       340
                  ....*....|....*....|....*....
gi 1524699473 324 LCTPNDVFGPPYSIKSLKTGDWVIFKRAG 352
Cdd:pfam00278 312 TCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 15-371 3.32e-83

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: 259.31  E-value: 3.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  15 YYIYDLTTLEQRIHWLTSA---TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATA-PMIYGGPVKTR 90
Cdd:COG0019    28 LYVYDEAALRRNLRALREAfpgSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPeRIVFSGNGKSE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  91 GNLAYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINlSNIES--SAKLKMAGVPTQFGLPYEDLEEAFEICEA 168
Cdd:COG0019   108 EELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVN-PGVDAgtHEYISTGGKDSKFGIPLEDALEAYRRAAA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 169 TPELQLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSR-LPADYaINVGGGIGINY-EGETQFDFETFASQIEDF--- 243
Cdd:COG0019   187 LPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELgIDLEW-LDLGGGLGIPYtEGDEPPDLEELAAAIKEAlee 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 244 -----PQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPkAWYH-NHPLDILptettsSRVKSIENQQ 317
Cdd:COG0019   266 lcglgPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRP-ALYGaYHPIVPV------GRPSGAEAET 338

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1524699473 318 VTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDISHlQFLSHNLPKI 371
Cdd:COG0019   339 YDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMAS-NYNGRPRPAE 391
lysA TIGR01048
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ...
 16-359 1.27e-52

diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273415 [Multi-domain]  Cd Length: 414  Bit Score: 179.79  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSATK--HSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEkvRAVSATAP---MIYGGPVKTR 90
Cdd:TIGR01048  28 YVYDEDTIRRRFRAYKEAFGgrSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELY--RALAAGFPpekIVFSGNGKSR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  91 GNLAYALEHQVKsIQVESLYELDALQSLLADSERSVEVMLRINlSNIE--SSAKLKMAGVPTQFGLPYEDLEEAFEICEA 168
Cdd:TIGR01048 106 AELERALELGIC-INVDSFSELERLNEIAPELGKKARISLRVN-PGVDakTHPYISTGLKDSKFGIDVEEALEAYLYALQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 169 TPELQLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSRLPADYaINVGGGIGINYEGETQ-FDFETFASQIED----- 242
Cdd:TIGR01048 184 LPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAEGIDLEF-LDLGGGLGIPYTPEEEpPDLSEYAQAILNalegy 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 243 -----FPQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFP---KAWYHNHPLdilptettsSRVKSIE 314
Cdd:TIGR01048 263 adlglDPKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLIRPalyGAYHHIIVL---------NRTNDAP 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1524699473 315 NQQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDIS 359
Cdd:TIGR01048 334 TEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMS 378
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
6-359 4.37e-34

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 133.67  E-value: 4.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473   6 HLLT--DPEQDYYIYDLTTLEQRIHWLTS-ATKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVR-AVSATAP- 80
Cdd:PRK08961  494 RLLTlsDAGSPCYVYHLPTVRARARALAAlAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFeLFPELSPe 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  81 -MIYGGPVKTRGNLAYALEHQVkSIQVESLYELDALQSLLADSersvEVMLRINLSNIES-SAKLKMAGVPTQFGLPYED 158
Cdd:PRK08961  574 rVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNWPELFRGR----EVWLRIDPGHGDGhHEKVRTGGKESKFGLSQTR 648

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 159 LEEAFEICEaTPELQLTGFHFHSMSNNLDE---QAHVDFIknaIAFAqkysSRLPADYAINVGGGIGINYE-GETQFDFE 234
Cdd:PRK08961  649 IDEFVDLAK-TLGITVVGLHAHLGSGIETGehwRRMADEL---ASFA----RRFPDVRTIDLGGGLGIPESaGDEPFDLD 720

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 235 TFASQIEDFP------QLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILptettsS 308
Cdd:PRK08961  721 ALDAGLAEVKaqhpgyQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNSLIRPALYGAYHEIVNL------S 794

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1524699473 309 RVKSIENQQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDIS 359
Cdd:PRK08961  795 RLDEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMS 845
 
Name Accession Description Interval E-value
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 16-374 8.43e-138

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: 397.42  E-value: 8.43e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSA--TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAPMIYGGPVKTRGNL 93
Cdd:cd06843     5 YVYDLAALRAHARALRASlpPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDAPLIFGGPGKTDSEL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  94 AYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINL-SNIESSAKLKMAGVPTQFGLPYEDLEEAFEICEATPEL 172
Cdd:cd06843    85 AQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLaLPDLPSSTLTMGGQPTPFGIDEADLPDALELLRDLPNI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 173 QLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSS--RLPADYaINVGGGIGINYE-GETQFDFETFASQI-------ED 242
Cdd:cd06843   165 RLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAehGLDLDV-VNVGGGIGVNYAdPEEQFDWAGFCEGLdqllaeyEP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 243 FPQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILPTETTS---SRVkSIENQQVT 319
Cdd:cd06843   244 GLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPAAWGHNHPFSVLPVEEWPypwPRP-SVRDTPVT 322

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1524699473 320 LAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDISHLQFLSHNLPKIKFI 374
Cdd:cd06843   323 LVGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYGWNISHHDFLMHPHPERIYL 377
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 16-352 1.03e-87

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: 268.20  E-value: 1.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSA--TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATA-PMIYGGPVKTRGN 92
Cdd:pfam00278   2 YVYDLATLRRNYRRWKAAlpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPeRIVFAGPGKTDSE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  93 LAYALEHQVKSIQVESLYELDALQSLLAdsERSVEVMLRINLSNIESSAKLKMAGVPTQFGLPYEDLEEAFEICEATpEL 172
Cdd:pfam00278  82 IRYALEAGVLCFNVDSEDELEKIAKLAP--ELVARVALRINPDVDAGTHKISTGGLSSKFGIDLEDAPELLALAKEL-GL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 173 QLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSR-LPADYaINVGGGIGINYEGETQFDFETFASQI-----EDFP-- 244
Cdd:pfam00278 159 NVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELgIDLKL-LDIGGGFGIPYRDEPPPDFEEYAAAIrealdEYFPpd 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 245 -QLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILPTETTSSRVKsienqqVTLAGK 323
Cdd:pfam00278 238 lEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLET------YDVVGP 311

                         330       340
                  ....*....|....*....|....*....
gi 1524699473 324 LCTPNDVFGPPYSIKSLKTGDWVIFKRAG 352
Cdd:pfam00278 312 TCESGDVLAKDRELPELEVGDLLAFEDAG 340
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 15-371 3.29e-84

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: 260.31  E-value: 3.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  15 YYIYDLTTLEQRIHWLTSATK--HSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATA-PMIYGGPVKTRG 91
Cdd:cd06810     3 FYVYDLDIIRAHYAALKEALPsgVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPeRIIFTGPAKSVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  92 NLAYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINLSNIESSAKLKMAGVPTQFGLPYEDLEEAFEICEATpE 171
Cdd:cd06810    83 EIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLKSKFGLSLSEARAALERAKEL-D 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 172 LQLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSRLPADYAINVGGGIGINYEGETqFDFETFASQIEDF-------- 243
Cdd:cd06810   162 LRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQP-LDFEEYAALINPLlkkyfpnd 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 244 --PQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFrFPKAWY--HNHPLDILPTETTssrvkSIENQQVT 319
Cdd:cd06810   241 pgVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHS-FRPALAydAYHPITPLKAPGP-----DEPLVPAT 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1524699473 320 LAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDISHlQFLSHNLPKI 371
Cdd:cd06810   315 LAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESS-NFNSHPRPAE 365
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 15-371 3.32e-83

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: 259.31  E-value: 3.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  15 YYIYDLTTLEQRIHWLTSA---TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATA-PMIYGGPVKTR 90
Cdd:COG0019    28 LYVYDEAALRRNLRALREAfpgSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPeRIVFSGNGKSE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  91 GNLAYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINlSNIES--SAKLKMAGVPTQFGLPYEDLEEAFEICEA 168
Cdd:COG0019   108 EELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVN-PGVDAgtHEYISTGGKDSKFGIPLEDALEAYRRAAA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 169 TPELQLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSR-LPADYaINVGGGIGINY-EGETQFDFETFASQIEDF--- 243
Cdd:COG0019   187 LPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELgIDLEW-LDLGGGLGIPYtEGDEPPDLEELAAAIKEAlee 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 244 -----PQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPkAWYH-NHPLDILptettsSRVKSIENQQ 317
Cdd:COG0019   266 lcglgPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRP-ALYGaYHPIVPV------GRPSGAEAET 338

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1524699473 318 VTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDISHlQFLSHNLPKI 371
Cdd:COG0019   339 YDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMAS-NYNGRPRPAE 391
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 16-369 4.94e-81

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: 252.51  E-value: 4.94e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSA--TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAPMI-YGGPVKTRGN 92
Cdd:cd06839    10 YVYDRDRVRERYAALRAAlpPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKIlFAGPGKSDAE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  93 LAYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINLSNIESSAKLKMAGVPTQFGLPYEDLEEAFEICEATPEL 172
Cdd:cd06839    90 LRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRINPDFELKGSGMKMGGGPSQFGIDVEELPAVLARIAALPNL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 173 QLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSRLPADYA-INVGGGIGINY-EGETQFDFETFASQIEDF------- 243
Cdd:cd06839   170 RFVGLHIYPGTQILDADALIEAFRQTLALALRLAEELGLPLEfLDLGGGFGIPYfPGETPLDLEALGAALAALlaelgdr 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 244 ---PQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNH-----FRFPKAWYHNHPLDILPtettssRVKSIEN 315
Cdd:cd06839   250 lpgTRVVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVTDGGMHHhlaasGNFGQVLRRNYPLAILN------RMGGEER 323

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1524699473 316 QQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDISHLQFLSHNLP 369
Cdd:cd06839   324 ETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLSASPLAFLSHPAP 377
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 16-356 2.68e-65

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: 211.57  E-value: 2.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSATK---HSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEkvRAVSATAPM---IYGGPVKT 89
Cdd:cd06828     6 YVYDEATIRENYRRLKEAFSgpgFKICYAVKANSNLAILKLLAEEGLGADVVSGGELY--RALKAGFPPeriVFTGNGKS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  90 RGNLAYALEHQVKSIQVESLYELDALQSLLADSERSVEVMLRINlSNIES--SAKLKMAGVPTQFGLPYEDLEEAFEICE 167
Cdd:cd06828    84 DEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVN-PGVDAgtHPYISTGGKDSKFGIPLEQALEAYRRAK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 168 ATPELQLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSRLPADYAINVGGGIGINY-EGETQFDFETFASQIEDF--- 243
Cdd:cd06828   163 ELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYrDEDEPLDIEEYAEAIAEAlke 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 244 -------PQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFP---KAWYHnhpldILPTettsSRVKSI 313
Cdd:cd06828   243 lceggpdLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLIRPalyGAYHE-----IVPV----NKPGEG 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1524699473 314 ENQQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAY 356
Cdd:cd06828   314 ETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGY 356
lysA TIGR01048
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ...
 16-359 1.27e-52

diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273415 [Multi-domain]  Cd Length: 414  Bit Score: 179.79  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  16 YIYDLTTLEQRIHWLTSATK--HSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEkvRAVSATAP---MIYGGPVKTR 90
Cdd:TIGR01048  28 YVYDEDTIRRRFRAYKEAFGgrSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELY--RALAAGFPpekIVFSGNGKSR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  91 GNLAYALEHQVKsIQVESLYELDALQSLLADSERSVEVMLRINlSNIE--SSAKLKMAGVPTQFGLPYEDLEEAFEICEA 168
Cdd:TIGR01048 106 AELERALELGIC-INVDSFSELERLNEIAPELGKKARISLRVN-PGVDakTHPYISTGLKDSKFGIDVEEALEAYLYALQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 169 TPELQLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSRLPADYaINVGGGIGINYEGETQ-FDFETFASQIED----- 242
Cdd:TIGR01048 184 LPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAEGIDLEF-LDLGGGLGIPYTPEEEpPDLSEYAQAILNalegy 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 243 -----FPQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFP---KAWYHNHPLdilptettsSRVKSIE 314
Cdd:TIGR01048 263 adlglDPKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLIRPalyGAYHHIIVL---------NRTNDAP 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1524699473 315 NQQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDIS 359
Cdd:TIGR01048 334 TEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMS 378
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 15-354 7.54e-42

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: 150.49  E-value: 7.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  15 YYIYDLTTLEQRIHWLTSA-----TKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKvrAVSATAP---MIYGGP 86
Cdd:cd06841     9 FFVFDEDALRENYRELLGAfkkryPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYEL--ALKLGVPgkrIIFNGP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  87 VKTRGNLAYALEHQVKsIQVESLYELDALQSLLADSERSVEVMLRINL--SNIESSaklkmagvptQFGLPYEDLEEAFE 164
Cdd:cd06841    87 YKSKEELEKALEEGAL-INIDSFDELERILEIAKELGRVAKVGIRLNMnyGNNVWS----------RFGFDIEENGEALA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 165 ICEATPE---LQLTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSrLPADYaINVGGGIGIN------YEGE-TQFDFE 234
Cdd:cd06841   156 ALKKIQEsknLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRLFG-LELEY-LDLGGGFPAKtplslaYPQEdTVPDPE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 235 TFASQI-----------EDFPQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHfrFPKAWYHNHPLDILPT 303
Cdd:cd06841   234 DYAEAIastlkeyyankENKPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINN--IPTIFWYHHPILVLRP 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1524699473 304 ETTSSRVKSienqqVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSY 354
Cdd:cd06841   312 GKEDPTSKN-----YDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAY 357
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 12-354 6.67e-40

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: 144.94  E-value: 6.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  12 EQDYYIYDLTTLEQRIHWLTSATKHS-IYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRA--VSAtAPMIYGGPVK 88
Cdd:cd00622     1 ETPFLVVDLGDVVRKYRRWKKALPRVrPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGlgVSP-ERIIFANPCK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  89 TRGNLAYALEHQVKSIQVESLYELDALQSLLADSersvEVMLRINLSNieSSAKLKMAgvpTQFGLpyeDLEEAFEICEA 168
Cdd:cd00622    80 SISDIRYAAELGVRLFTFDSEDELEKIAKHAPGA----KLLLRIATDD--SGALCPLS---RKFGA---DPEEARELLRR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 169 TPE--LQLTGFHFHSMSNNLDEQAHVDFIKNA---IAFAQKYSSRLpadYAINVGGGIGINYEGETqFDFETFASQI--- 240
Cdd:cd00622   148 AKElgLNVVGVSFHVGSQCTDPSAYVDAIADArevFDEAAELGFKL---KLLDIGGGFPGSYDGVV-PSFEEIAAVInra 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 241 --EDFP----QLTFELGRFITAPIGYYAANVYDIKTMHG---ETFVLLN----GGTNHFRFPKAWYHNHPL-DILPTETT 306
Cdd:cd00622   224 ldEYFPdegvRIIAEPGRYLVASAFTLAVNVIAKRKRGDddrERWYYLNdgvyGSFNEILFDHIRYPPRVLkDGGRDGEL 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1524699473 307 SSrvksienqqVTLAGKLCTPNDVFGPPYSI-KSLKTGDWVIFKRAGSY 354
Cdd:cd00622   304 YP---------SSLWGPTCDSLDVIYEDVLLpEDLAVGDWLLFENMGAY 343
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 24-256 2.28e-37

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: 134.72  E-value: 2.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  24 EQRIHWLTSATKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAP-MIYGGPVKTRGNLAYALEHQVK 102
Cdd:pfam02784   6 RRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPErIIFANPCKQRSFLRYALEVGVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 103 SIQVESLYELDALQSLLADSersvEVMLRINLSNIESSAKLKMagvptQFGLPYEDLEEAFEICEATPELQLTGFHFHSM 182
Cdd:pfam02784  86 CVTVDNVDELEKLARLAPEA----RVLLRIKPDDSAATCPLSS-----KFGADLDEDVEALLEAAKLLNLQVVGVSFHVG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 183 SNNLDEQAHVDFIKNAIAF---AQKYSSRLPadyAINVGGGIGINYEGET-QFDFETFASQI-----EDFPQLT-----F 248
Cdd:pfam02784 157 SGCTDAEAFVLALEDARGVfdqGAELGFNLK---ILDLGGGFGVDYTEGEePLDFEEYANVInealeEYFPGDPgvtiiA 233


                  ....*...
gi 1524699473 249 ELGRFITA 256
Cdd:pfam02784 234 EPGRYFVA 241
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 7-359 2.21e-34

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: 130.25  E-value: 2.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473   7 LLTDPEQD--YYIYDLTTLEQRIHWLTS-ATKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAP--- 80
Cdd:cd06840     4 LLRLAPDVgpCYVYDLETVRARARQVSAlKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLFPDLDprr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  81 MIYGGPVKTRGNLAYALEHQVkSIQVESLYELDALQSLLADsersVEVMLRINLSNIES-SAKLKMAGVPTQFGLPYEDL 159
Cdd:cd06840    84 VLFTPNFAARSEYEQALELGV-NVTVDNLHPLREWPELFRG----REVILRIDPGQGEGhHKHVRTGGPESKFGLDVDEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 160 EEAFEICeATPELQLTGFHFHSMSNNLDEqahvDFIKNAIAFAQKYSSRLPADYAINVGGGIGINYE-GETQFDFETFAS 238
Cdd:cd06840   159 DEARDLA-KKAGIIVIGLHAHSGSGVEDT----DHWARHGDYLASLARHFPAVRILNVGGGLGIPEApGGRPIDLDALDA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 239 QIED----FP--QLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILptettsSRVKS 312
Cdd:cd06840   234 ALAAakaaHPqyQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEIVNL------SRLDE 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1524699473 313 IENQQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDIS 359
Cdd:cd06840   308 PPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMA 354
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
6-359 4.37e-34

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 133.67  E-value: 4.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473   6 HLLT--DPEQDYYIYDLTTLEQRIHWLTS-ATKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVR-AVSATAP- 80
Cdd:PRK08961  494 RLLTlsDAGSPCYVYHLPTVRARARALAAlAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFeLFPELSPe 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  81 -MIYGGPVKTRGNLAYALEHQVkSIQVESLYELDALQSLLADSersvEVMLRINLSNIES-SAKLKMAGVPTQFGLPYED 158
Cdd:PRK08961  574 rVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNWPELFRGR----EVWLRIDPGHGDGhHEKVRTGGKESKFGLSQTR 648

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 159 LEEAFEICEaTPELQLTGFHFHSMSNNLDE---QAHVDFIknaIAFAqkysSRLPADYAINVGGGIGINYE-GETQFDFE 234
Cdd:PRK08961  649 IDEFVDLAK-TLGITVVGLHAHLGSGIETGehwRRMADEL---ASFA----RRFPDVRTIDLGGGLGIPESaGDEPFDLD 720

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 235 TFASQIEDFP------QLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGGTNHFRFPKAWYHNHPLDILptettsS 308
Cdd:PRK08961  721 ALDAGLAEVKaqhpgyQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNSLIRPALYGAYHEIVNL------S 794

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1524699473 309 RVKSIENQQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGSYAYDIS 359
Cdd:PRK08961  795 RLDEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMS 845
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 38-228 8.19e-29

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: 111.26  E-value: 8.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  38 IYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVS-ATAPMIYGGPVKTRGNLAYALEHQVKSIQVESLYELDALQ 116
Cdd:cd06808    18 LFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGiPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSLEELEKLE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 117 SLLADSERSVEVMLRINLSNIESsaklkmagvptQFGLPYEDLEEAFEICEATPELQLTGFHFHSMSNNLDEQAHVDFIK 196
Cdd:cd06808    98 EAALKAGPPARVLLRIDTGDENG-----------KFGVRPEELKALLERAKELPHLRLVGLHTHFGSADEDYSPFVEALS 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1524699473 197 NAIAFAQKYSSRLPADYAINVGGGIGINYEGE 228
Cdd:cd06808   167 RFVAALDQLGELGIDLEQLSIGGSFAILYLQE 198
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 17-368 8.87e-29

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: 115.18  E-value: 8.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  17 IYDLTTLEQRIHWLTSATK----HSIyyAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAP-MIYGGPVKTRG 91
Cdd:cd06836     7 LYDLDGFRALVARLTAAFPapvlHTF--AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPErIVFDSPAKTRA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  92 NLAYALEHQVkSIQVESLYELDALQSLLADSERSVEVM-LRINLSNIESSAKLKMAGVPT-QFGLPYEDlEEAFEICEAT 169
Cdd:cd06836    85 ELREALELGV-AINIDNFQELERIDALVAEFKEASSRIgLRVNPQVGAGKIGALSTATATsKFGVALED-GARDEIIDAF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 170 PELQ-LTGFHFHSMSNNLDEQAHVDFIKNAIAFAQKYSSRLPADYA--INVGGGIGINYEGE-TQFDFETFASQI----- 240
Cdd:cd06836   163 ARRPwLNGLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRVGRRQItrIDIGGGLPVNFESEdITPTFADYAAALkaavp 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 241 ---EDFPQLTFELGRFITAPIGYYAANVYDIKTMHGETFVLLNGG----TNHFRFPKAWyhnhPLDILPTeTTSSRVKSI 313
Cdd:cd06836   243 elfDGRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIAITHAGaqvaTRTAYAPDDW----PLRVTVF-DANGEPKTG 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1524699473 314 ENQQVTLAGKLCTPNDVFGPPYSIKSLKTGDWVIFKRAGsyAYDISHlqFLSHNL 368
Cdd:cd06836   318 PEVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTG--AYYFSS--HSSYNS 368
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 38-236 3.33e-19

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: 88.47  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  38 IYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSAT-APMIYGGPVKTRGNLAYALEHQVkSIQVESLYELDALQ 116
Cdd:cd06842    40 VYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRgDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 117 SLL-ADSERSVEVMLRINlsniESSAKLkmagvPTQFGLPYEDLEEAFE-ICEATPELQLTGFHFHsmsnnLDEQA---H 191
Cdd:cd06842   119 ALArGYTTGPARVLLRLS----PFPASL-----PSRFGMPAAEVRTALErLAQLRERVRLVGFHFH-----LDGYSaaqR 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1524699473 192 VDFIKNAIAFAQKYSSRLPADYAINVGGGIGINYEGETQfDFETF 236
Cdd:cd06842   185 VAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAA-EWEAF 228
PLPDE_III_ADC cd06830
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ...
 23-271 2.34e-13

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which 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. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family.


Pssm-ID: 143503 [Multi-domain]  Cd Length: 409  Bit Score: 70.68  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  23 LEQRIHWLTSATKHSI----Y-------YAVKANSHPRILETLA----PYVAGFEVASPGEIEKVRAV--SATAPMIYGG 85
Cdd:cd06830    15 LRHRIERLNAAFAKAIeeygYkgkyqgvYPIKVNQQREVVEEIVkagkRYNIGLEAGSKPELLAALALlkTPDALIICNG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  86 pVKTRGNLAYALE-----HQVkSIQVESLYELDalqsLLADSERSVEVM----LRINLSNIESSAKLKMAGVPTQFGLPY 156
Cdd:cd06830    95 -YKDDEYIELALLarklgHNV-IIVIEKLSELD----LILELAKKLGVKpllgVRIKLASKGSGKWQESGGDRSKFGLTA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 157 EDLEEAFEICEAT---PELQLTGFHFHSMSNNldeqahVDFIKNAIAFAQKYSSRLPADYA----INVGGGIGINYEGET 229
Cdd:cd06830   169 SEILEVVEKLKEAgmlDRLKLLHFHIGSQITD------IRRIKSALREAARIYAELRKLGAnlryLDIGGGLGVDYDGSR 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524699473 230 Q-------FDFETFASQI------------EDFPQLTFELGRFITAPIGYYAANVYDIKTM 271
Cdd:cd06830   243 SssdssfnYSLEEYANDIvktvkeicdeagVPHPTIVTESGRAIVAHHSVLIFEVLGVKRL 303
PLN02537 PLN02537
diaminopimelate decarboxylase
 38-354 2.19e-10

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 61.73  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  38 IYYAVKANSHPRILETLAPYVAGFEVASPGEIE-KVRAVSATAPMIYGGPVKTRGNLAYALEHQVkSIQVESLYELDALQ 116
Cdd:PLN02537   46 IGYAIKANNNLKILEHLRELGCGAVLVSGNELRlALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 117 SLLADSERSVEVMLRINlSNIESSAKLKMA--GVPTQFGLPYEDLEEAFEICEATP-ELQLTGFHFHSMSNnldeQAHVD 193
Cdd:PLN02537  125 EAARIAGKKVNVLLRIN-PDVDPQVHPYVAtgNKNSKFGIRNEKLQWFLDAVKAHPnELKLVGAHCHLGST----ITKVD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 194 FIKNAIAFAQKYSSRLPA-----DYaINVGGGIGINYEGE-----TQFDFETFASQIEDFPQLTF--ELGRFITAPIGYY 261
Cdd:PLN02537  200 IFRDAAVLMVNYVDEIRAqgfelSY-LNIGGGLGIDYYHAgavlpTPRDLIDTVRELVLSRDLTLiiEPGRSLIANTCCF 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 262 AANVYDIKTMHGETFVLLNGGTNHFRFPK---AWYHnhpldilpTETTSSRVKSIENQQVTLAGKLCTPNDVFGPPYSIK 338
Cdd:PLN02537  279 VNRVTGVKTNGTKNFIVIDGSMAELIRPSlydAYQH--------IELVSPPPPDAEVSTFDVVGPVCESADFLGKDRELP 350

                         330
                  ....*....|....*.
gi 1524699473 339 SLKTGDWVIFKRAGSY 354
Cdd:PLN02537  351 TPPKGAGLVVHDAGAY 366
PLPDE_III_CANSDC cd06829
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ...
 15-354 6.81e-09

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which 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. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.


Pssm-ID: 143502 [Multi-domain]  Cd Length: 346  Bit Score: 56.79  E-value: 6.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  15 YYIYDLTTLEQRIHWLTSATKHS---IYYAVKANSHPRILETLAPYVAGFEVASPGEiekvravSATAPMIYGGPVKT-- 89
Cdd:cd06829     3 CYVLDEAKLRRNLEILKRVQERSgakILLALKAFSMWSVFPLIREYLDGTTASSLFE-------ARLGREEFGGEVHTys 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  90 ----RGNLAYALEHqVKSIQVESLYELDALQSLLADSErsVEVMLRIN--LSNiessaklkmAGVP--------TQFGLP 155
Cdd:cd06829    76 payrDDEIDEILRL-ADHIIFNSLSQLERFKDRAKAAG--ISVGLRINpeYSE---------VETDlydpcapgSRLGVT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 156 YEDLEEAfeiceaTPELqLTGFHFHsmsnNLDEQAHVDFIKNAIAFAQKYSSRLPADYAINVGGGIGINYEGetqFDFET 235
Cdd:cd06829   144 LDELEEE------DLDG-IEGLHFH----TLCEQDFDALERTLEAVEERFGEYLPQLKWLNLGGGHHITRPD---YDVDR 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473 236 FASQIEDFP-----QLTFELGRFITAPIGYYAANVYDIkTMHGETFVLLNGGTNHfrfpkawyhnHPLDILPTETTSSRV 310
Cdd:cd06829   210 LIALIKRFKekygvEVYLEPGEAVALNTGYLVATVLDI-VENGMPIAILDASATA----------HMPDVLEMPYRPPIR 278

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1524699473 311 KSIENQQ----VTLAGKLCTPNDVFGpPYSI-KSLKTGDWVIFKRAGSY 354
Cdd:cd06829   279 GAGEPGEgahtYRLGGNSCLAGDVIG-DYSFdEPLQVGDRLVFEDMAHY 326
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
19-179 1.54e-07

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 51.46  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  19 DLTTLEQRIHWLTSATKH--SIYYAVKANSHP----RILETLAPYVA-GFEVASPGEIEKVRAVSATAP-MIYGGPvkTR 90
Cdd:pfam01168   2 DLDALRHNLRRLRRRAGPgaKLMAVVKANAYGhgavEVARALLEGGAdGFAVATLDEALELREAGITAPiLVLGGF--PP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  91 GNLAYALEHQVkSIQVESLYELDALQSLLADSERSVEVMLRINLSniessaklkMagvpTQFGLPYEDLEEAFEICEATP 170
Cdd:pfam01168  80 EELALAAEYDL-TPTVDSLEQLEALAAAARRLGKPLRVHLKIDTG---------M----GRLGFRPEEALALLARLAALP 145

                         170
                  ....*....|.
gi 1524699473 171 ELQLTGF--HF 179
Cdd:pfam01168 146 GLRLEGLmtHF 156
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 15-198 1.89e-04

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: 43.30  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  15 YYIYDLTTL-EQRIHWLTSATKHSIYYAVKANSHPRILETLAPYVAGFEVASPGEIEKVRAVSATAP-MIYGGPVKTRGN 92
Cdd:cd06831    15 FFVGDLGKIvKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPEnIIYTNPCKQASQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524699473  93 LAYALEHQVKSIQVESLYELDAlqslLADSERSVEVMLRINLSNIESSAKLKMagvptQFGLPYEDLEEAFEiCEATPEL 172
Cdd:cd06831    95 IKYAAKVGVNIMTCDNEIELKK----IARNHPNAKLLLHIATEDNIGGEEMNM-----KFGTTLKNCRHLLE-CAKELDV 164

                         170       180
                  ....*....|....*....|....*.
gi 1524699473 173 QLTGFHFHSMSNNLDEQAHVDFIKNA 198
Cdd:cd06831   165 QIVGVKFHVSSSCKEYQTYVHALSDA 190
 
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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