|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
23-411 |
6.74e-113 |
|
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: 336.38 E-value: 6.74e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 23 WGTPVYLHDRAFIEQSCDQLLNMPNAFGLHVRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTTQ 102
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 103 EVPlgqeREELEGMIRNG-LKYNVCSLTQYRLIADFAKQAGI--DLSIRVHPGAsGGGESQTRDTGSEYSCFGVHLNDIP 179
Cdd:cd06828 81 GKS----DEELELALELGiLRINVDSLSELERLGEIAPELGKgaPVALRVNPGV-DAGTHPYISTGGKDSKFGIPLEQAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 180 TVVEMARD-KGLRFTQVHVHIGSG-GDPEKWRENIDRELGFV---RSYFPDAGTVSFGGGLKVARMPGEKQADINELGTY 254
Cdd:cd06828 156 EAYRRAKElPGLKLVGLHCHIGSQiLDLEPFVEAAEKLLDLAaelRELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 255 AAARLKEFKEqTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPISIVGQDGTLR 334
Cdd:cd06828 236 IAEALKELCE-GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGE 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500055952 335 SSEYDsysvgtatpygIVGRCCESGDSVRLDNEGtivpvqvAEAEIGDYVVIGGTGAYSESMSPeNYNSHRKAPAVM 411
Cdd:cd06828 315 TEKVD-----------VVGPICESGDVFAKDREL-------PEVEEGDLLAIHDAGAYGYSMSS-NYNSRPRPAEVL 372
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
10-435 |
2.86e-104 |
|
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: 315.55 E-value: 2.86e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 10 RLDAALVPL--IAQKWGTPVYLHDRAFIEQSCDQLLNMPNAFGLHVRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARA 87
Cdd:COG0019 9 ELTIEGVDLaeLAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 88 HSAGIPYDRMMLTTQEVPlgqeREELEGMIRNGLKY-NVCSLTQYRLIADFAKQAG--IDLSIRVHPGASGGGeSQTRDT 164
Cdd:COG0019 89 LAAGFPPERIVFSGNGKS----EEELEEALELGVGHiNVDSLSELERLAELAAELGkrAPVGLRVNPGVDAGT-HEYIST 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 165 GSEYSCFGVHLNDIPTVVEMARD-KGLRFTQVHVHIGSG-GDPEKWRENIDRELGFVRSyFPDAG----TVSFGGGLKVA 238
Cdd:COG0019 164 GGKDSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQiLDLEPFEEALERLLELAEE-LRELGidleWLDLGGGLGIP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 239 RMPGEKQADINELgtyaAARLKEFKEQ-TGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLL 317
Cdd:COG0019 243 YTEGDEPPDLEEL----AAAIKEALEElCGLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRPAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 318 YGSEHPISIVGQDGTlrsseydsysvGTATPYGIVGRCCESGDSVRLDnegtivpVQVAEAEIGDYVVIGGTGAYSESMS 397
Cdd:COG0019 319 YGAYHPIVPVGRPSG-----------AEAETYDVVGPLCESGDVLGKD-------RSLPPLEPGDLLAFLDAGAYGFSMA 380
|
410 420 430
....*....|....*....|....*....|....*...
gi 500055952 398 PeNYNSHRKAPAVMKmKDAELVLIRKRQVREQLVQNEL 435
Cdd:COG0019 381 S-NYNGRPRPAEVLV-DDGEARLIRRRETYEDLLASEV 416
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
2-435 |
6.52e-75 |
|
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: 239.88 E-value: 6.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 2 TQNHFGPTRLDAALVPLIAQKWGTPVYLHDRAFIEQscdQLLNMPNAFGLH--VRYAMKANSDRTVLRVVTGKGLDLDCS 79
Cdd:TIGR01048 2 VENEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRR---RFRAYKEAFGGRslVCYAVKANSNLAVLRLLAELGSGFDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 80 SVDEAARAHSAGIPYDRMMLTTQevplGQEREELEGMIRNGLKYNVCSLTQYRLIADFAKQAGI--DLSIRVHPGAsGGG 157
Cdd:TIGR01048 79 SGGELYRALAAGFPPEKIVFSGN----GKSRAELERALELGICINVDSFSELERLNEIAPELGKkaRISLRVNPGV-DAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 158 ESQTRDTGSEYSCFGVHLNDIPTVVEMA-RDKGLRFTQVHVHIGSG-GDPEKWRENIDRELGFVRSYFPDAG--TVSFGG 233
Cdd:TIGR01048 154 THPYISTGLKDSKFGIDVEEALEAYLYAlQLPHLELVGIHCHIGSQiTDLSPFVEAAEKVVKLAESLAEGIDleFLDLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 234 GLKVARMPGEKQADINELGTYAAARLKEFKEQtGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLS 313
Cdd:TIGR01048 234 GLGIPYTPEEEPPDLSEYAQAILNALEGYADL-GLDPKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 314 RPLLYGSEHPISIVGQDGTLRSSEYDsysvgtatpygIVGRCCESGDSVRLDnegtivpVQVAEAEIGDYVVIGGTGAYS 393
Cdd:TIGR01048 313 RPALYGAYHHIIVLNRTNDAPTEVAD-----------VVGPVCESGDVLAKD-------RELPEVEPGDLLAVFDAGAYG 374
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 500055952 394 ESMSpENYNShRKAPAVMKMKDAELVLIRKRQVREQLVQNEL 435
Cdd:TIGR01048 375 FSMS-SNYNS-RPRPAEVLVDGGQARLIRRRETYEDLWALEV 414
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
27-390 |
2.28e-63 |
|
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: 207.72 E-value: 2.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 27 VYLHDRAFIEQSCDQLLNmpnAFGLHVR--YAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTtqev 104
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKA---ALPPRVKifYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 105 PLGQEREELEGMIRNGLKY-NVCSLTQYRLIADFAKQAGIDLSIRVHPGASGGGESQTrdTGSEYSCFGVHLNDIPTVVE 183
Cdd:pfam00278 74 GPGKTDSEIRYALEAGVLCfNVDSEDELEKIAKLAPELVARVALRINPDVDAGTHKIS--TGGLSSKFGIDLEDAPELLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 184 MARDKGLRFTQVHVHIGSG-GDPEKWRENIDRELGFVRsYFPDAG----TVSFGGGLKVARMPGEkqadINELGTYAAAR 258
Cdd:pfam00278 152 LAKELGLNVVGVHFHIGSQiTDLEPFVEALQRARELFD-RLRELGidlkLLDIGGGFGIPYRDEP----PPDFEEYAAAI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 259 LKEFKEQTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPISIVGQDGTLRSSEY 338
Cdd:pfam00278 227 REALDEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETY 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 500055952 339 DsysvgtatpygIVGRCCESGDSVRLDnegtivpVQVAEAEIGDYVVIGGTG 390
Cdd:pfam00278 307 D-----------VVGPTCESGDVLAKD-------RELPELEVGDLLAFEDAG 340
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
55-409 |
2.10e-41 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 156.78 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 55 YAMKANSDRTVLRVVTGKGLDLDCSSVDE--AARAHSAGIPYDRMMLTTQEVPlgqeREELEGMIRNGLKYNVCSLTQYR 132
Cdd:PRK08961 531 YAIKANPHPAILRTLEEEGFGFECVSIGElrRVFELFPELSPERVLFTPNFAP----RAEYEAAFALGVTVTLDNVEPLR 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 133 LIADFAKqaGIDLSIRVHPGaSGGGESQTRDTGSEYSCFGVHLNDIPTVVEMARDKGLRFTQVHVHIGSG-GDPEKWREN 211
Cdd:PRK08961 607 NWPELFR--GREVWLRIDPG-HGDGHHEKVRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGiETGEHWRRM 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 212 IDRELGFVRSyFPDAGTVSFGGGLKVARMPGEKQADINELgtyaAARLKEFKEQTGRaLRMEIEPGTFVVANSGYIITRV 291
Cdd:PRK08961 684 ADELASFARR-FPDVRTIDLGGGLGIPESAGDEPFDLDAL----DAGLAEVKAQHPG-YQLWIEPGRYLVAEAGVLLARV 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 292 MDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPIsivgqdgtLRSSEYDSYSVGTATpygIVGRCCESGDSVRLDNegtiv 371
Cdd:PRK08961 758 TQVKEKDGVRRVGLETGMNSLIRPALYGAYHEI--------VNLSRLDEPAAGTAD---VVGPICESSDVLGKRR----- 821
|
330 340 350
....*....|....*....|....*....|....*...
gi 500055952 372 pvQVAEAEIGDYVVIGGTGAYSESMSpENYNshRKAPA 409
Cdd:PRK08961 822 --RLPATAEGDVILIANAGAYGYSMS-STYN--LREPA 854
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
23-411 |
6.74e-113 |
|
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: 336.38 E-value: 6.74e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 23 WGTPVYLHDRAFIEQSCDQLLNMPNAFGLHVRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTTQ 102
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 103 EVPlgqeREELEGMIRNG-LKYNVCSLTQYRLIADFAKQAGI--DLSIRVHPGAsGGGESQTRDTGSEYSCFGVHLNDIP 179
Cdd:cd06828 81 GKS----DEELELALELGiLRINVDSLSELERLGEIAPELGKgaPVALRVNPGV-DAGTHPYISTGGKDSKFGIPLEQAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 180 TVVEMARD-KGLRFTQVHVHIGSG-GDPEKWRENIDRELGFV---RSYFPDAGTVSFGGGLKVARMPGEKQADINELGTY 254
Cdd:cd06828 156 EAYRRAKElPGLKLVGLHCHIGSQiLDLEPFVEAAEKLLDLAaelRELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 255 AAARLKEFKEqTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPISIVGQDGTLR 334
Cdd:cd06828 236 IAEALKELCE-GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGE 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500055952 335 SSEYDsysvgtatpygIVGRCCESGDSVRLDNEGtivpvqvAEAEIGDYVVIGGTGAYSESMSPeNYNSHRKAPAVM 411
Cdd:cd06828 315 TEKVD-----------VVGPICESGDVFAKDREL-------PEVEEGDLLAIHDAGAYGYSMSS-NYNSRPRPAEVL 372
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
10-435 |
2.86e-104 |
|
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: 315.55 E-value: 2.86e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 10 RLDAALVPL--IAQKWGTPVYLHDRAFIEQSCDQLLNMPNAFGLHVRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARA 87
Cdd:COG0019 9 ELTIEGVDLaeLAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 88 HSAGIPYDRMMLTTQEVPlgqeREELEGMIRNGLKY-NVCSLTQYRLIADFAKQAG--IDLSIRVHPGASGGGeSQTRDT 164
Cdd:COG0019 89 LAAGFPPERIVFSGNGKS----EEELEEALELGVGHiNVDSLSELERLAELAAELGkrAPVGLRVNPGVDAGT-HEYIST 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 165 GSEYSCFGVHLNDIPTVVEMARD-KGLRFTQVHVHIGSG-GDPEKWRENIDRELGFVRSyFPDAG----TVSFGGGLKVA 238
Cdd:COG0019 164 GGKDSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQiLDLEPFEEALERLLELAEE-LRELGidleWLDLGGGLGIP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 239 RMPGEKQADINELgtyaAARLKEFKEQ-TGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLL 317
Cdd:COG0019 243 YTEGDEPPDLEEL----AAAIKEALEElCGLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRPAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 318 YGSEHPISIVGQDGTlrsseydsysvGTATPYGIVGRCCESGDSVRLDnegtivpVQVAEAEIGDYVVIGGTGAYSESMS 397
Cdd:COG0019 319 YGAYHPIVPVGRPSG-----------AEAETYDVVGPLCESGDVLGKD-------RSLPPLEPGDLLAFLDAGAYGFSMA 380
|
410 420 430
....*....|....*....|....*....|....*...
gi 500055952 398 PeNYNSHRKAPAVMKmKDAELVLIRKRQVREQLVQNEL 435
Cdd:COG0019 381 S-NYNGRPRPAEVLV-DDGEARLIRRRETYEDLLASEV 416
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
2-435 |
6.52e-75 |
|
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: 239.88 E-value: 6.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 2 TQNHFGPTRLDAALVPLIAQKWGTPVYLHDRAFIEQscdQLLNMPNAFGLH--VRYAMKANSDRTVLRVVTGKGLDLDCS 79
Cdd:TIGR01048 2 VENEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRR---RFRAYKEAFGGRslVCYAVKANSNLAVLRLLAELGSGFDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 80 SVDEAARAHSAGIPYDRMMLTTQevplGQEREELEGMIRNGLKYNVCSLTQYRLIADFAKQAGI--DLSIRVHPGAsGGG 157
Cdd:TIGR01048 79 SGGELYRALAAGFPPEKIVFSGN----GKSRAELERALELGICINVDSFSELERLNEIAPELGKkaRISLRVNPGV-DAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 158 ESQTRDTGSEYSCFGVHLNDIPTVVEMA-RDKGLRFTQVHVHIGSG-GDPEKWRENIDRELGFVRSYFPDAG--TVSFGG 233
Cdd:TIGR01048 154 THPYISTGLKDSKFGIDVEEALEAYLYAlQLPHLELVGIHCHIGSQiTDLSPFVEAAEKVVKLAESLAEGIDleFLDLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 234 GLKVARMPGEKQADINELGTYAAARLKEFKEQtGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLS 313
Cdd:TIGR01048 234 GLGIPYTPEEEPPDLSEYAQAILNALEGYADL-GLDPKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 314 RPLLYGSEHPISIVGQDGTLRSSEYDsysvgtatpygIVGRCCESGDSVRLDnegtivpVQVAEAEIGDYVVIGGTGAYS 393
Cdd:TIGR01048 313 RPALYGAYHHIIVLNRTNDAPTEVAD-----------VVGPVCESGDVLAKD-------RELPEVEPGDLLAVFDAGAYG 374
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 500055952 394 ESMSpENYNShRKAPAVMKMKDAELVLIRKRQVREQLVQNEL 435
Cdd:TIGR01048 375 FSMS-SNYNS-RPRPAEVLVDGGQARLIRRRETYEDLWALEV 414
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
27-390 |
2.28e-63 |
|
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: 207.72 E-value: 2.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 27 VYLHDRAFIEQSCDQLLNmpnAFGLHVR--YAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTtqev 104
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKA---ALPPRVKifYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 105 PLGQEREELEGMIRNGLKY-NVCSLTQYRLIADFAKQAGIDLSIRVHPGASGGGESQTrdTGSEYSCFGVHLNDIPTVVE 183
Cdd:pfam00278 74 GPGKTDSEIRYALEAGVLCfNVDSEDELEKIAKLAPELVARVALRINPDVDAGTHKIS--TGGLSSKFGIDLEDAPELLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 184 MARDKGLRFTQVHVHIGSG-GDPEKWRENIDRELGFVRsYFPDAG----TVSFGGGLKVARMPGEkqadINELGTYAAAR 258
Cdd:pfam00278 152 LAKELGLNVVGVHFHIGSQiTDLEPFVEALQRARELFD-RLRELGidlkLLDIGGGFGIPYRDEP----PPDFEEYAAAI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 259 LKEFKEQTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPISIVGQDGTLRSSEY 338
Cdd:pfam00278 227 REALDEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETY 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 500055952 339 DsysvgtatpygIVGRCCESGDSVRLDnegtivpVQVAEAEIGDYVVIGGTG 390
Cdd:pfam00278 307 D-----------VVGPTCESGDVLAKD-------RELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
25-410 |
6.74e-60 |
|
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: 199.45 E-value: 6.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 25 TPVYLHDRAFIEQSCDQLLNmpnAFGLHVR--YAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTtq 102
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKE---ALPSGVKlfYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFT-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 103 evPLGQEREELEGMIRNGLK-YNVCSLTQYRLIADFAKQAGIDLSI--RVHPGASGGGESQtrDTGSEYSCFGVHLNDIP 179
Cdd:cd06810 76 --GPAKSVSEIEAALASGVDhIVVDSLDELERLNELAKKLGPKARIllRVNPDVSAGTHKI--STGGLKSKFGLSLSEAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 180 TVVEMARDKGLRFTQVHVHIGSGG-DPEKWRENIDRELGFVRSYF---PDAGTVSFGGGLKVARMpgEKQADINELgtya 255
Cdd:cd06810 152 AALERAKELDLRLVGLHFHVGSQIlDLETIVQALSDARELIEELVemgFPLEMLDLGGGLGIPYD--EQPLDFEEY---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 256 AARLKEFKEQTGRA---LRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLL-YGSEHPISIVGQDG 331
Cdd:cd06810 226 AALINPLLKKYFPNdpgVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHSFRPALaYDAYHPITPLKAPG 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500055952 332 TLRSSEydsysvgtatPYGIVGRCCESGDSVRLDNEgtivpvqVAEAEIGDYVVIGGTGAYSESMSPeNYNSHRKAPAV 410
Cdd:cd06810 306 PDEPLV----------PATLAGPLCDSGDVIGRDRL-------LPELEVGDLLVFEDMGAYGFSESS-NFNSHPRPAEY 366
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
26-402 |
2.07e-41 |
|
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: 150.66 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 26 PVYLHDRAFIEQSCDQLLNMPNAFGLHvrYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSA--GIPYDRMMLTTQE 103
Cdd:cd06840 13 PCYVYDLETVRARARQVSALKAVDSLF--YAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 104 VPlgqeREELEGMIRNGLKYNVCSLTQYRLIADFAKqaGIDLSIRVHPGASGGGESQTRDTGSEySCFGVHLNDIPTVVE 183
Cdd:cd06840 91 AA----RSEYEQALELGVNVTVDNLHPLREWPELFR--GREVILRIDPGQGEGHHKHVRTGGPE-SKFGLDVDELDEARD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 184 MARDKGLRFTQVHVHIGSG-GDPEKWRENIDrELGFVRSYFPDAGTVSFGGGLKVARMPGEKQADINELGtyaaARLKEF 262
Cdd:cd06840 164 LAKKAGIIVIGLHAHSGSGvEDTDHWARHGD-YLASLARHFPAVRILNVGGGLGIPEAPGGRPIDLDALD----AALAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 263 KEQTGRaLRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPIsivgqdgtLRSSEYDSYS 342
Cdd:cd06840 239 KAAHPQ-YQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEI--------VNLSRLDEPP 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 343 VGTATpygIVGRCCESGDSVRLDNegtIVPvqvaEAEIGDYVVIGGTGAYSESMSpENYN 402
Cdd:cd06840 310 AGNAD---VVGPICESGDVLGRDR---LLP----ETEEGDVILIANAGAYGFCMA-STYN 358
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
55-409 |
2.10e-41 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 156.78 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 55 YAMKANSDRTVLRVVTGKGLDLDCSSVDE--AARAHSAGIPYDRMMLTTQEVPlgqeREELEGMIRNGLKYNVCSLTQYR 132
Cdd:PRK08961 531 YAIKANPHPAILRTLEEEGFGFECVSIGElrRVFELFPELSPERVLFTPNFAP----RAEYEAAFALGVTVTLDNVEPLR 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 133 LIADFAKqaGIDLSIRVHPGaSGGGESQTRDTGSEYSCFGVHLNDIPTVVEMARDKGLRFTQVHVHIGSG-GDPEKWREN 211
Cdd:PRK08961 607 NWPELFR--GREVWLRIDPG-HGDGHHEKVRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGiETGEHWRRM 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 212 IDRELGFVRSyFPDAGTVSFGGGLKVARMPGEKQADINELgtyaAARLKEFKEQTGRaLRMEIEPGTFVVANSGYIITRV 291
Cdd:PRK08961 684 ADELASFARR-FPDVRTIDLGGGLGIPESAGDEPFDLDAL----DAGLAEVKAQHPG-YQLWIEPGRYLVAEAGVLLARV 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 292 MDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPIsivgqdgtLRSSEYDSYSVGTATpygIVGRCCESGDSVRLDNegtiv 371
Cdd:PRK08961 758 TQVKEKDGVRRVGLETGMNSLIRPALYGAYHEI--------VNLSRLDEPAAGTAD---VVGPICESSDVLGKRR----- 821
|
330 340 350
....*....|....*....|....*....|....*...
gi 500055952 372 pvQVAEAEIGDYVVIGGTGAYSESMSpENYNshRKAPA 409
Cdd:PRK08961 822 --RLPATAEGDVILIANAGAYGYSMS-STYN--LREPA 854
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
19-404 |
3.49e-41 |
|
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: 150.44 E-value: 3.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 19 IAQKWGTPVYLHDRAFIEQSCDQLLN-MPNAFGLHvrYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRM 97
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAaLPPAIEIY--YSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 98 MLTTqevPlGQEREELEGMIRNGLK-YNVCSLTQYRLIADFAKQAGI--DLSIRVHPGAS--------GGGESQtrdtgs 166
Cdd:cd06839 79 LFAG---P-GKSDAELRRAIEAGIGtINVESLEELERIDALAEEHGVvaRVALRINPDFElkgsgmkmGGGPSQ------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 167 eyscFGVHLNDIPTVV-EMARDKGLRFTQVHVHIGSGG-DPEKWRENIDRELGFVRSYFPDAG----TVSFGGGLKVARM 240
Cdd:cd06839 149 ----FGIDVEELPAVLaRIAALPNLRFVGLHIYPGTQIlDADALIEAFRQTLALALRLAEELGlpleFLDLGGGFGIPYF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 241 PGEKQADINELGTYAAARLKEFkEQTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGM----------- 309
Cdd:cd06839 225 PGETPLDLEALGAALAALLAEL-GDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVTDGGMhhhlaasgnfg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 310 ELLSRPLlygsehPISIVGQDGTlrsseydsysvGTATPYGIVGRCCESGDsvRL-DNegtivpVQVAEAEIGDYVVIGG 388
Cdd:cd06839 304 QVLRRNY------PLAILNRMGG-----------EERETVTVVGPLCTPLD--LLgRN------VELPPLEPGDLVAVLQ 358
|
410
....*....|....*.
gi 500055952 389 TGAYSESMSPENYNSH 404
Cdd:cd06839 359 SGAYGLSASPLAFLSH 374
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
55-404 |
1.33e-32 |
|
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: 127.01 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 55 YAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGipydrmmlttQEVPL-----GQEREELEGMIRNGLK-YNVCSL 128
Cdd:cd06843 31 YAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAV----------PDAPLifggpGKTDSELAQALAQGVErIHVESE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 129 TQYRLIADFAKQAGIDLSI--RVHPgASGGGESQTRDTGSEYSCFGVHLNDIPTVVEMARD-KGLRFTQVHVHIGSGG-D 204
Cdd:cd06843 101 LELRRLNAVARRAGRTAPVllRVNL-ALPDLPSSTLTMGGQPTPFGIDEADLPDALELLRDlPNIRLRGFHFHLMSHNlD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 205 PEKWRENIDRELGFVRS----YFPDAGTVSFGGGLKVARMPGEKQADINELGTYaaarLKEFKEQTGRALRMEIEPGTFV 280
Cdd:cd06843 180 AAAHLALVKAYLETARQwaaeHGLDLDVVNVGGGIGVNYADPEEQFDWAGFCEG----LDQLLAEYEPGLTLRFECGRYI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 281 VANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPISIVGQDGTLRSSEYDSysvGTATPYGIVGRCCESGD 360
Cdd:cd06843 256 SAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPAAWGHNHPFSVLPVEEWPYPWPRPS---VRDTPVTLVGQLCTPKD 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 500055952 361 SVRLDnegtivpVQVAEAEIGDYVVIGGTGAYSESMSPENYNSH 404
Cdd:cd06843 333 VLARD-------VPVDRLRAGDLVVFPLAGAYGWNISHHDFLMH 369
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
24-397 |
3.30e-28 |
|
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: 114.51 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 24 GTPVYLHDRAFIEQSCDQLL-NMPNAfglHVRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTtq 102
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKkALPRV---RPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 103 eVPLGQEREelegmIRNGLKYNVcsltqyRL-----------IADFAKqaGIDLSIRVhpgasgggesQTRDTGSEYSC- 170
Cdd:cd00622 76 -NPCKSISD-----IRYAAELGV------RLftfdsedelekIAKHAP--GAKLLLRI----------ATDDSGALCPLs 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 171 --FGVHLNDIPTVVEMARDKGLRFTQVHVHIGSG-GDPEKWRENIDRelgfVRSYFPDAGTVSF-------GGGLkvarm 240
Cdd:cd00622 132 rkFGADPEEARELLRRAKELGLNVVGVSFHVGSQcTDPSAYVDAIAD----AREVFDEAAELGFklklldiGGGF----- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 241 PGEKQADINELGTYAAARLKEFKE-QTGRALRMEIEPGTFVVANSGYIITRVMDKK----LTNEMNFLLVDGgmellsrp 315
Cdd:cd00622 203 PGSYDGVVPSFEEIAAVINRALDEyFPDEGVRIIAEPGRYLVASAFTLAVNVIAKRkrgdDDRERWYYLNDG-------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 316 lLYGS------EHPISIVgqdgtlrSSEYDSYSVGTATPYGIVGRCCESGDSVRLDnegtivpVQVAEA-EIGDYVVIGG 388
Cdd:cd00622 275 -VYGSfneilfDHIRYPP-------RVLKDGGRDGELYPSSLWGPTCDSLDVIYED-------VLLPEDlAVGDWLLFEN 339
|
....*....
gi 500055952 389 TGAYSESMS 397
Cdd:cd00622 340 MGAYTTAYA 348
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
19-399 |
1.40e-26 |
|
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: 110.04 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 19 IAQKWGTPVYLHDRAFIEQSCDQLLNMPNAFGLHVR--YAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDR 96
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRYPNVViaYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 97 MMLTTqevPLgQEREELEGMIRNGLKYNVCSLTQYRLIADFAKQAGIDLS--IRVHpgasgggeSQTRDTGseYSCFGVH 174
Cdd:cd06841 81 IIFNG---PY-KSKEELEKALEEGALINIDSFDELERILEIAKELGRVAKvgIRLN--------MNYGNNV--WSRFGFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 175 LNDIPTVVE----MARDKGLRFTQVHVHIGS-GGDPEKWRENIDRELGFVRSYF-PDAGTVSFGGGL--KVARMPGEKQA 246
Cdd:cd06841 147 IEENGEALAalkkIQESKNLSLVGLHCHVGSnILNPEAYSAAAKKLIELLDRLFgLELEYLDLGGGFpaKTPLSLAYPQE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 247 DIN-ELGTYAAA---RLKEFKEQTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYgsEH 322
Cdd:cd06841 227 DTVpDPEDYAEAiasTLKEYYANKENKPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINNIPTIFWY--HH 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500055952 323 PISIVGQDGtlrsseydsySVGTATPYGIVGRCCESGDSVRldnEGTIVPvqvaEAEIGDYVVIGGTGAYSESMSPE 399
Cdd:cd06841 305 PILVLRPGK----------EDPTSKNYDVYGFNCMESDVLF---PNVPLP----PLNVGDILAIRNVGAYNMTQSNQ 364
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
27-410 |
4.15e-21 |
|
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: 94.38 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 27 VYLHDRAFIEQSCDQLLNMPNAFGLHVrYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTTqevPL 106
Cdd:cd06836 5 VGLYDLDGFRALVARLTAAFPAPVLHT-FAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDS---PA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 107 gQEREELEGMIRNGLKYNVCSLTQYR----LIADFAKQAGIdLSIRVHPgASGGGESQTRDTGSEYSCFGVHLNDiptvv 182
Cdd:cd06836 81 -KTRAELREALELGVAINIDNFQELEridaLVAEFKEASSR-IGLRVNP-QVGAGKIGALSTATATSKFGVALED----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 183 eMARDKGLR-------FTQVHVHIGSGGDP-----------EKWRENIDRELGFVRsyfpdAGTVSFGGGLKVARmpgEK 244
Cdd:cd06836 153 -GARDEIIDafarrpwLNGLHVHVGSQGCElsllaegirrvVDLAEEINRRVGRRQ-----ITRIDIGGGLPVNF---ES 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 245 QADINELGTYAAARLKEFKEQTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLygseHPi 324
Cdd:cd06836 224 EDITPTFADYAAALKAAVPELFDGRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIAITHAGAQVATRTAY----AP- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 325 sivgQDGTLRSSEYDS---YSVGTATPYGIVGRCCESGDSVRLDNEgtivpvqVAEAEIGDYVVIGGTGAYSESMsPENY 401
Cdd:cd06836 299 ----DDWPLRVTVFDAngePKTGPEVVTDVAGPCCFAGDVLAKERA-------LPPLEPGDYVAVHDTGAYYFSS-HSSY 366
|
....*....
gi 500055952 402 NShRKAPAV 410
Cdd:cd06836 367 NS-LPRPAV 374
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
41-282 |
5.54e-21 |
|
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: 91.57 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 41 QLLNMPNAFGLH-VRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTTQEVPLGQEREELEGMIRN 119
Cdd:pfam02784 7 RHRRWKKALPRIkPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVGVGC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 120 GlkyNVCSLTQYRLIADFAkqAGIDLSIRVHPGASGGgesqtrdTGSEYSCFGVHLN-DIPTVVEMARDKGLRFTQVHVH 198
Cdd:pfam02784 87 V---TVDNVDELEKLARLA--PEARVLLRIKPDDSAA-------TCPLSSKFGADLDeDVEALLEAAKLLNLQVVGVSFH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 199 IGSG-GDPEKWRENIDRELGFV---RSYFPDAGTVSFGGGLKVARMPGEKQADINELGTYAAARLKEFKEQtGRALRMEI 274
Cdd:pfam02784 155 VGSGcTDAEAFVLALEDARGVFdqgAELGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINEALEEYFPG-DPGVTIIA 233
|
....*...
gi 500055952 275 EPGTFVVA 282
Cdd:pfam02784 234 EPGRYFVA 241
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
55-422 |
3.83e-15 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 76.75 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 55 YAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTTQevplGQEREELEGMIRNGLKYNVCSLTQYRLI 134
Cdd:PLN02537 48 YAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGN----GKLLEDLVLAAQEGVFVNVDSEFDLENI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 135 ADFAKQAGI----------DLSIRVHPGASgggesqtrdTGSEYSCFGVHLNDIPTVVEMARD--KGLRFTQVHVHIGSG 202
Cdd:PLN02537 124 VEAARIAGKkvnvllrinpDVDPQVHPYVA---------TGNKNSKFGIRNEKLQWFLDAVKAhpNELKLVGAHCHLGST 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 203 -GDPEKWR-------ENID--RELGFVRSYfpdagtVSFGGGL--------KVARMPGEKQADINELgtyaaarlkefke 264
Cdd:PLN02537 195 iTKVDIFRdaavlmvNYVDeiRAQGFELSY------LNIGGGLgidyyhagAVLPTPRDLIDTVREL------------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 265 QTGRALRMEIEPGTFVVANSGYIITRVMDKKLTNEMNFLLVDGGMELLSRPLLYGSEHPISIVgqdgtlrSSEYDSYSVG 344
Cdd:PLN02537 256 VLSRDLTLIIEPGRSLIANTCCFVNRVTGVKTNGTKNFIVIDGSMAELIRPSLYDAYQHIELV-------SPPPPDAEVS 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500055952 345 TatpYGIVGRCCESGDSVRLDNEgtivpvqVAEAEIGDYVVIGGTGAYSESMSpENYNSHRKAPAVMKMKDAELVLIR 422
Cdd:PLN02537 329 T---FDVVGPVCESADFLGKDRE-------LPTPPKGAGLVVHDAGAYCMSMA-STYNLKMRPPEYWVEEDGSITKIR 395
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
50-253 |
3.85e-14 |
|
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: 71.20 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 50 GLHVRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGIPYDRMMLTtqeVPLGQEREelegmIRNGLKY-----N 124
Cdd:cd06808 15 GITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFL---GPCKQVSE-----LEDAAEQgvivvT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 125 VCSLTQYRLIADFAKQAG--IDLSIRVhpgasgggesqtrDTGSEYSCFGVHLNDIPTVVEMARD-KGLRFTQVHVHIGS 201
Cdd:cd06808 87 VDSLEELEKLEEAALKAGppARVLLRI-------------DTGDENGKFGVRPEELKALLERAKElPHLRLVGLHTHFGS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500055952 202 G-GDPEKWRENIDRELGFVRS---YFPDAGTVSFGGGLKVARMPGEKQA--DINELGT 253
Cdd:cd06808 154 AdEDYSPFVEALSRFVAALDQlgeLGIDLEQLSIGGSFAILYLQELPLGtfIIVEPGR 211
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
127-306 |
6.16e-11 |
|
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: 63.34 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 127 SLTQYRLIADFAKQAGIDLSIRVHPGASgggESQTR--DTGSEYSCFGVHLNDIPTVVeMARDKGLRFtqvHVHIGSGGD 204
Cdd:cd06829 97 SLSQLERFKDRAKAAGISVGLRINPEYS---EVETDlyDPCAPGSRLGVTLDELEEED-LDGIEGLHF---HTLCEQDFD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 205 P-EKWRENIDRELGfvrSYFPDAGTVSFGGGLKVARmpgeKQADINELgtyaAARLKEFKEQTGraLRMEIEPGTFVVAN 283
Cdd:cd06829 170 AlERTLEAVEERFG---EYLPQLKWLNLGGGHHITR----PDYDVDRL----IALIKRFKEKYG--VEVYLEPGEAVALN 236
|
170 180
....*....|....*....|...
gi 500055952 284 SGYIITRVMDkKLTNEMNFLLVD 306
Cdd:cd06829 237 TGYLVATVLD-IVENGMPIAILD 258
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
15-286 |
3.30e-07 |
|
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: 52.26 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 15 LVPLIAQkWGTPVYLHDRAFIEQSCDQLLNMPNAFGL--HVRYAMKANSDRTVLRVVTGKGLDLDCSSVDEAARAHSAGI 92
Cdd:cd06842 1 LVALVEA-YGSPLNVLFPQTFRENIAALRAVLDRHGVdgRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 93 PYDRMMLTTQEVPlgqeREELEGMIRNGLKYNVCSLTQYRLIADFAKQAG---IDLSIRVhpgasgGGESQTRdtgseYS 169
Cdd:cd06842 80 RGDRIVATGPAKT----DEFLWLAVRHGATIAVDSLDELDRLLALARGYTtgpARVLLRL------SPFPASL-----PS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 170 CFGVHLNDIPTVVEM--ARDKGLRFTQVHVHIGSGGDPEKWREnIDRELGFV---RSYFPDAGTVSFGGGLKVARMPGEK 244
Cdd:cd06842 145 RFGMPAAEVRTALERlaQLRERVRLVGFHFHLDGYSAAQRVAA-LQECLPLIdraRALGLAPRFIDIGGGFPVSYLADAA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 500055952 245 QADinelgTYAAArLKEFKEQTGRALRMEIEPGTFVVANSGY 286
Cdd:cd06842 224 EWE-----AFLAA-LTEALYGYGRPLTWRNEGGTLRGPDDFY 259
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
55-303 |
1.15e-05 |
|
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: 47.18 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 55 YAMKANSDRTVLRVVTGKG----LDLDCSSVDEAARAHSagipydrmMLTTQEVPL---GQEREElegMIRNGLK----- 122
Cdd:cd06830 43 YPIKVNQQREVVEEIVKAGkrynIGLEAGSKPELLAALA--------LLKTPDALIicnGYKDDE---YIELALLarklg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 123 YNVC----SLTQYRLIADFAKQAGID--LSIRVHPGASGGGESQtrDTGSEYSCFGVHLNDIPTVVEMARDKGL--RFTQ 194
Cdd:cd06830 112 HNVIivieKLSELDLILELAKKLGVKplLGVRIKLASKGSGKWQ--ESGGDRSKFGLTASEILEVVEKLKEAGMldRLKL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500055952 195 VHVHIGSG-GDPEKWRENIdRElgFVRSY------FPDAGTVSFGGGLKVA------RMPGEKQADINElgtYAAARLKE 261
Cdd:cd06830 190 LHFHIGSQiTDIRRIKSAL-RE--AARIYaelrklGANLRYLDIGGGLGVDydgsrsSSDSSFNYSLEE---YANDIVKT 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 500055952 262 FKEqtgRALRMEI-------EPGTFVVANSGYIITRVMDKKLTNEMNFL 303
Cdd:cd06830 264 VKE---ICDEAGVphptivtESGRAIVAHHSVLIFEVLGVKRLADWYFC 309
|
|
| |
