|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
9-419 |
1.74e-174 |
|
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: 493.90 E-value: 1.74e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 9 GELTMGGTSLKTVAQSFGTPTIVYDEDQIRNQMRRYHSAFEKSGLKynISYASKAFTCIQMVKLVQEEDLQLDVVSEGEL 88
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAK--VLYAVKANSNLAVLRLLAEEGLGADVVSGGEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 89 YTALEAGFDANRIHFHGNNKTKREIQYALENNIGYFVIDALEEIDLIDKYASDE---VNIVLRVNPGVEAHTHEFIQTGQ 165
Cdd:COG0019 86 RLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELgkrAPVGLRVNPGVDAGTHEYISTGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 166 EDSKFGLSIKHglALEAINKVKASKHLQLKGVHFHVGSQIEGTEAMIETAKLVLHW---LSENEIKVELLNLGGGFGIKY 242
Cdd:COG0019 166 KDSKFGIPLED--ALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELaeeLRELGIDLEWLDLGGGLGIPY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 243 VEGDESFPIEegiaEIADAIKETAHSLNYEVPEIGIEPGRSIVGEAGITLYEVGTIKEIPEVNkYVSVDGGMSDHIRTAL 322
Cdd:COG0019 244 TEGDEPPDLE----ELAAAIKEALEELCGLGPELILEPGRALVGNAGVLLTRVLDVKENGGRR-FVIVDAGMNDLMRPAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 323 YDAKYQALLVNRNEEADD-TVTIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFLKDG 401
Cdd:COG0019 319 YGAYHPIVPVGRPSGAEAeTYDVVGPLCESGDVLGKDRSLP-PLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDG 397
|
410
....*....|....*...
gi 488383836 402 KAREVIKRQSLRQLIIND 419
Cdd:COG0019 398 EARLIRRRETYEDLLASE 415
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
25-398 |
1.87e-165 |
|
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: 469.27 E-value: 1.87e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 25 FGTPTIVYDEDQIRNQMRRYHSAFEKSGLKynISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFH 104
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFK--ICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 105 GNNKTKREIQYALENNIGYFVIDALEEIDLIDKYASDE---VNIVLRVNPGVEAHTHEFIQTGQEDSKFGLSIKHglALE 181
Cdd:cd06828 79 GNGKSDEELELALELGILRINVDSLSELERLGEIAPELgkgAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQ--ALE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 182 AINKVKASKHLQLKGVHFHVGSQIEGTEAMIETAKLVLHWLSENE---IKVELLNLGGGFGIKYVEGDESFPIEEGIAEI 258
Cdd:cd06828 157 AYRRAKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRelgIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 259 ADAIKETAHSLNyeVPEIGIEPGRSIVGEAGITLYEVGTIKEIPEvNKYVSVDGGMSDHIRTALYDAKYQALLVNRNEEA 338
Cdd:cd06828 237 AEALKELCEGGP--DLKLIIEPGRYIVANAGVLLTRVGYVKETGG-KTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEG 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488383836 339 DD-TVTIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:cd06828 314 ETeKVDVVGPICESGDVFAKDRELP-EVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
5-416 |
8.69e-144 |
|
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: 415.92 E-value: 8.69e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 5 YNEYGELTMGGTSLKTVAQSFGTPTIVYDEDQIRNQMRRYHSAFEKSGLkynISYASKAFTCIQMVKLVQEEDLQLDVVS 84
Cdd:TIGR01048 3 ENEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRSL---VCYAVKANSNLAVLRLLAELGSGFDVVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 85 EGELYTALEAGFDANRIHFHGNNKTKREIQYALENNIgYFVIDALEEIDLIDKYASD---EVNIVLRVNPGVEAHTHEFI 161
Cdd:TIGR01048 80 GGELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPElgkKARISLRVNPGVDAKTHPYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 162 QTGQEDSKFGLSIKHglALEAINKVKASKHLQLKGVHFHVGSQIEGTEAMIETAKLVLHWLSENEIKVEL--LNLGGGFG 239
Cdd:TIGR01048 159 STGLKDSKFGIDVEE--ALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAEGIDLefLDLGGGLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 240 IKYVEGDESFPIEEGIAEIADAIKETAHSLNYevPEIGIEPGRSIVGEAGITLYEVGTIKEIPeVNKYVSVDGGMSDHIR 319
Cdd:TIGR01048 237 IPYTPEEEPPDLSEYAQAILNALEGYADLGLD--PKLILEPGRSIVANAGVLLTRVGFVKETG-SRNFVIVDAGMNDLIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 320 TALYDAKYQALLVNR-NEEADDTVTIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:TIGR01048 314 PALYGAYHHIIVLNRtNDAPTEVADVVGPVCESGDVLAKDRELP-EVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLV 392
|
410
....*....|....*...
gi 488383836 399 KDGKAREVIKRQSLRQLI 416
Cdd:TIGR01048 393 DGGQARLIRRRETYEDLW 410
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
31-377 |
2.73e-101 |
|
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: 304.79 E-value: 2.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 31 VYDEDQIRNQMRRYHSAFEKsglKYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFHGNNKTK 110
Cdd:pfam00278 3 VYDLATLRRNYRRWKAALPP---RVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 111 REIQYALENNIGYFVIDALEEIDLIDKYASDEV-NIVLRVNPGVEAHTHeFIQTGQEDSKFGLSIKHglALEAINKVKAS 189
Cdd:pfam00278 80 SEIRYALEAGVLCFNVDSEDELEKIAKLAPELVaRVALRINPDVDAGTH-KISTGGLSSKFGIDLED--APELLALAKEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 190 kHLQLKGVHFHVGSQIEGTEAMIETAKLVLH---WLSENEIKVELLNLGGGFGIKYvEGDESFPIEegiaEIADAIKETA 266
Cdd:pfam00278 157 -GLNVVGVHFHIGSQITDLEPFVEALQRARElfdRLRELGIDLKLLDIGGGFGIPY-RDEPPPDFE----EYAAAIREAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 267 HSLNYEVPEIGIEPGRSIVGEAGITLYEVGTIKEIPEVNkYVSVDGGMSDHIRTALYDAKYQALLVNRNEEADD-TVTIA 345
Cdd:pfam00278 231 DEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKT-FVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLeTYDVV 309
|
330 340 350
....*....|....*....|....*....|..
gi 488383836 346 GKLCESGDIIIKKAKLPsSIKRGDYLAILSTG 377
Cdd:pfam00278 310 GPTCESGDVLAKDRELP-ELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
27-398 |
5.73e-98 |
|
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: 297.29 E-value: 5.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 27 TPTIVYDEDQIRNQMRRYHSAFEKsglKYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFHGN 106
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPS---GVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 107 NKTKREIQYALENNIGYFVIDALEEIDLIDKYASDE---VNIVLRVNPGVEAHTHeFIQTGQEDSKFGLSIKHglALEAI 183
Cdd:cd06810 78 AKSVSEIEAALASGVDHIVVDSLDELERLNELAKKLgpkARILLRVNPDVSAGTH-KISTGGLKSKFGLSLSE--ARAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 184 NKVKASkHLQLKGVHFHVGSQI---EGTEAMIETAKLVLHWLSENEIKVELLNLGGGFGIKYVEgdESFPIEEGIAEIAD 260
Cdd:cd06810 155 ERAKEL-DLRLVGLHFHVGSQIldlETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE--QPLDFEEYAALINP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 261 AIKEtaHSLNYEVPEIGIEPGRSIVGEAGITLYEVGTIKEIpEVNKYVSVDGGMSDHIRTALYDAKYQALLVNRNEEADD 340
Cdd:cd06810 232 LLKK--YFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVN-GGRFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGPDE 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488383836 341 ---TVTIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:cd06810 309 plvPATLAGPLCDSGDVIGRDRLLP-ELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
22-402 |
8.96e-58 |
|
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: 193.63 E-value: 8.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 22 AQSFGTPTIVYDEDQIRNQMRRYHSAFEKSGLKYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRI 101
Cdd:cd06841 2 LESYGSPFFVFDEDALRENYRELLGAFKKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 102 HFHGNNKTKREIQYALENNiGYFVIDALEEIDLIDKYASD---EVNIVLRVNpgveahtheFIQTGQEDSKFGLSIKH-G 177
Cdd:cd06841 82 IFNGPYKSKEELEKALEEG-ALINIDSFDELERILEIAKElgrVAKVGIRLN---------MNYGNNVWSRFGFDIEEnG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 178 LALEAINKVKASKHLQLKGVHFHVGSQIEGTEAMIETAKLVLHWLSEN-EIKVELLNLGGGFG------IKYVEGDESFP 250
Cdd:cd06841 152 EALAALKKIQESKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRLfGLELEYLDLGGGFPaktplsLAYPQEDTVPD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 251 IEEGIAEIADAIKEtaHSLNYEV-PEIGIEPGRSIVGEAGITLYEVGTIKEIPEVNKYVsVDGGMsDHIRTALYdaKYQA 329
Cdd:cd06841 232 PEDYAEAIASTLKE--YYANKENkPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAV-TDAGI-NNIPTIFW--YHHP 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488383836 330 LLVNR---NEEADDTVTIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYSMASNYNQMQkPSVFFLKDGK 402
Cdd:cd06841 306 ILVLRpgkEDPTSKNYDVYGFNCMESDVLFPNVPLP-PLNVGDILAIRNVGAYNMTQSNQFIRPR-PAVYLIDNNG 379
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
34-286 |
1.10e-57 |
|
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: 189.03 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 34 EDQIRNQMRRYHSAFEKsglkYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFHGNNKTKREI 113
Cdd:pfam02784 1 LGSIERRHRRWKKALPR----IKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 114 QYALENNIGYFVIDALEEIDLIDKYASdEVNIVLRVNPGVEAHTHEFiqtgqeDSKFGLSIKHglALEAINKVKASKHLQ 193
Cdd:pfam02784 77 RYALEVGVGCVTVDNVDELEKLARLAP-EARVLLRIKPDDSAATCPL------SSKFGADLDE--DVEALLEAAKLLNLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 194 LKGVHFHVGSQIEGTEAM---IETAKLVLHWLSENEIKVELLNLGGGFGIKYVEGDESFPIEEGIAEIADAIKETAHSLn 270
Cdd:pfam02784 148 VVGVSFHVGSGCTDAEAFvlaLEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINEALEEYFPGD- 226
|
250
....*....|....*.
gi 488383836 271 yEVPEIGIEPGRSIVG 286
Cdd:pfam02784 227 -PGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
22-385 |
3.85e-57 |
|
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: 192.42 E-value: 3.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 22 AQSFGTPTIVYDEDQIRNQMRRYHSAFeksGLKYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRI 101
Cdd:cd06839 2 ADAYGTPFYVYDRDRVRERYAALRAAL---PPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 102 HFHGNNKTKREIQYALENNIGYFVIDALEEIDLIDKYASDE---VNIVLRVNPGVEAhTHEFIQTGQEDSKFGLSIKHgl 178
Cdd:cd06839 79 LFAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHgvvARVALRINPDFEL-KGSGMKMGGGPSQFGIDVEE-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 179 ALEAINKVKASKHLQLKGVHFHVGSQIEGTEAMIE----TAKLVLHWLSENEIKVELLNLGGGFGIKYVEGDESFPIEeg 254
Cdd:cd06839 156 LPAVLARIAALPNLRFVGLHIYPGTQILDADALIEafrqTLALALRLAEELGLPLEFLDLGGGFGIPYFPGETPLDLE-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 255 iaEIADAIKETAHSLNYEVPE--IGIEPGRSIVGEAGITLYEVGTIKeIPEVNKYVSVDGGMSDH----------IRTal 322
Cdd:cd06839 234 --ALGAALAALLAELGDRLPGtrVVLELGRYLVGEAGVYVTRVLDRK-VSRGETFLVTDGGMHHHlaasgnfgqvLRR-- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488383836 323 ydaKYQALLVNRNE-EADDTVTIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYSmAS 385
Cdd:cd06839 309 ---NYPLAILNRMGgEERETVTVVGPLCTPLDLLGRNVELP-PLEPGDLVAVLQSGAYGLS-AS 367
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
26-394 |
3.14e-54 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 192.99 E-value: 3.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 26 GTPTIVYDEDQIRNQMRryhsafEKSGLKY--NISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEA--GFDANRI 101
Cdd:PRK08961 502 GSPCYVYHLPTVRARAR------ALAALAAvdQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERV 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 102 HFHGNNKTKREIQYALEnnIGYFV-IDALEEIDLIDKYASDEvNIVLRVNPGVEAHTHEFIQTGQEDSKFGLSIKHglaL 180
Cdd:PRK08961 576 LFTPNFAPRAEYEAAFA--LGVTVtLDNVEPLRNWPELFRGR-EVWLRIDPGHGDGHHEKVRTGGKESKFGLSQTR---I 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 181 EAINKVKASKHLQLKGVHFHVGSQIEGTEAMIETAKLvLHWLSENEIKVELLNLGGGFGIKYVEGDESFPIEEGIAEIAD 260
Cdd:PRK08961 650 DEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRMADE-LASFARRFPDVRTIDLGGGLGIPESAGDEPFDLDALDAGLAE 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 261 AikETAHslnyevP--EIGIEPGRSIVGEAGITLYEVGTIKEIPEVnKYVSVDGGMSDHIRTALYDAKYQALLVNR-NEE 337
Cdd:PRK08961 729 V--KAQH------PgyQLWIEPGRYLVAEAGVLLARVTQVKEKDGV-RRVGLETGMNSLIRPALYGAYHEIVNLSRlDEP 799
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488383836 338 ADDTVTIAGKLCESGDIIIKKAKLPSSiKRGDYLAILSTGAYHYSMASNYNQMQKPS 394
Cdd:PRK08961 800 AAGTADVVGPICESSDVLGKRRRLPAT-AEGDVILIANAGAYGYSMSSTYNLREPAR 855
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
26-398 |
8.59e-54 |
|
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: 182.69 E-value: 8.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 26 GTPTIVYDEDQIRNQMRRYHSAFEKSglkyNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFHG 105
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRV----RPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 106 NNKTKREIQYALENNIGYFVIDALEEIDLIDKYAsDEVNIVLRvnpgveahthefIQTGQEDSKFGLSIKHG----LALE 181
Cdd:cd00622 77 PCKSISDIRYAAELGVRLFTFDSEDELEKIAKHA-PGAKLLLR------------IATDDSGALCPLSRKFGadpeEARE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 182 AINKVKAsKHLQLKGVHFHVGSQIEGTEAM---IETAKLVLHWLSENEIKVELLNLGGGFGIKYVEGDESFpieegiAEI 258
Cdd:cd00622 144 LLRRAKE-LGLNVVGVSFHVGSQCTDPSAYvdaIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSF------EEI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 259 ADAIKET-AHSLNYEVPEIGIEPGRSIVGEAGITLYEVGTIKEIPEVNKYVSV---DG---GMSDhirtALYD-AKYQAL 330
Cdd:cd00622 217 AAVINRAlDEYFPDEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERWYylnDGvygSFNE----ILFDhIRYPPR 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 331 LVNRNEEADDT--VTIAGKLCESGDIIIKKAKLPSSIKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:cd00622 293 VLKDGGRDGELypSSLWGPTCDSLDVIYEDVLLPEDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
27-406 |
5.24e-53 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 182.30 E-value: 5.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 27 TPTIVYDEDQIRNQMRRYHSAFEksGLKYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFHGN 106
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALE--GLRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 107 NKTKREIQYALENniGYFV-IDA---LEEIDLIDKYASDEVNIVLRVNPGVEAHTHEFIQTGQEDSKFGLSIKH-GLALE 181
Cdd:PLN02537 96 GKLLEDLVLAAQE--GVFVnVDSefdLENIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNSKFGIRNEKlQWFLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 182 AINkvKASKHLQLKGVHFHVGSQIEGTEAMIETAKLVLHWLSE---NEIKVELLNLGGGFGIKYVEGDESFPIEEgiaEI 258
Cdd:PLN02537 174 AVK--AHPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEiraQGFELSYLNIGGGLGIDYYHAGAVLPTPR---DL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 259 ADAIKETAHSLNYEVPeigIEPGRSIVGEAGITLYEVGTIKEIPEVNkYVSVDGGMSDHIRTALYDAkYQ--ALLVNRNE 336
Cdd:PLN02537 249 IDTVRELVLSRDLTLI---IEPGRSLIANTCCFVNRVTGVKTNGTKN-FIVIDGSMAELIRPSLYDA-YQhiELVSPPPP 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488383836 337 EAD-DTVTIAGKLCESGDIIIKKAKLPSSiKRGDYLAILSTGAYHYSMASNYN-QMQKPSVFFLKDGKAREV 406
Cdd:PLN02537 324 DAEvSTFDVVGPVCESADFLGKDRELPTP-PKGAGLVVHDAGAYCMSMASTYNlKMRPPEYWVEEDGSITKI 394
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
28-388 |
2.62e-50 |
|
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: 173.78 E-value: 2.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 28 PTIVYDEDQIRNQMRryhsafEKSGLKYNIS--YASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEA--GFDANRIHF 103
Cdd:cd06840 13 PCYVYDLETVRARAR------QVSALKAVDSlfYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 104 HGNNKTKREIQYALENNIgYFVIDALEEIDLIDKYASDEvNIVLRVNPGVEAHTHEFIQTGQEDSKFGLSIKHglaLEAI 183
Cdd:cd06840 87 TPNFAARSEYEQALELGV-NVTVDNLHPLREWPELFRGR-EVILRIDPGQGEGHHKHVRTGGPESKFGLDVDE---LDEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 184 NKVKASKHLQLKGVHFHVGSQIEGTEAMIETAkLVLHWLSENEIKVELLNLGGGFGIKYVEGDESFPIEEGIAEIADAik 263
Cdd:cd06840 162 RDLAKKAGIIVIGLHAHSGSGVEDTDHWARHG-DYLASLARHFPAVRILNVGGGLGIPEAPGGRPIDLDALDAALAAA-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 264 ETAHslnyevP--EIGIEPGRSIVGEAGITLYEVGTIKEIPEVnKYVSVDGGMSDHIRTALYDAKYQALLVNR-NEEADD 340
Cdd:cd06840 239 KAAH------PqyQLWMEPGRFIVAESGVLLARVTQIKHKDGV-RFVGLETGMNSLIRPALYGAYHEIVNLSRlDEPPAG 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 488383836 341 TVTIAGKLCESGDIIIKKAKLPSSiKRGDYLAILSTGAYHYSMASNYN 388
Cdd:cd06840 312 NADVVGPICESGDVLGRDRLLPET-EEGDVILIANAGAYGFCMASTYN 358
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
26-396 |
1.72e-42 |
|
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: 153.32 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 26 GTPTI-VYDEDQIRNQMRRYHSAFEKSGLKyniSYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFH 104
Cdd:cd06836 1 VHPAVgLYDLDGFRALVARLTAAFPAPVLH---TFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 105 GNNKTKREIQYALENNIgYFVIDALEEIDLID------KYASDEVNIvlRVNPGVEAHTHEFIQTGQEDSKFGLSIKHGL 178
Cdd:cd06836 78 SPAKTRAELREALELGV-AINIDNFQELERIDalvaefKEASSRIGL--RVNPQVGAGKIGALSTATATSKFGVALEDGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 179 ALEAINKVKASKhlQLKGVHFHVGSQIEGTEAMIETAKLVLHwLSEnEI-------KVELLNLGGGFGIKYvEGDESFPI 251
Cdd:cd06836 155 RDEIIDAFARRP--WLNGLHVHVGSQGCELSLLAEGIRRVVD-LAE-EInrrvgrrQITRIDIGGGLPVNF-ESEDITPT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 252 eegIAEIADAIKETAHSLNYEVPEIGIEPGRSIVGEAGITLYEVgtikeipevnKYVSVDG---------GMSDHIRTA- 321
Cdd:cd06836 230 ---FADYAAALKAAVPELFDGRYQLVTEFGRSLLAKCGTIVSRV----------EYTKSSGgrriaithaGAQVATRTAy 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 322 ---LYDAKYQALLVNRNEEADDTV--TIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYSMASNYNQMQKPSVF 396
Cdd:cd06836 297 apdDWPLRVTVFDANGEPKTGPEVvtDVAGPCCFAGDVLAKERALP-PLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
37-242 |
1.31e-35 |
|
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: 130.52 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 37 IRNQMRRYHSAFeksGLKYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFDANRIHFHGNNKTKREIQYA 116
Cdd:cd06808 1 IRHNYRRLREAA---PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 117 LENNIGYFVIDALEEIDLIDKYASDE---VNIVLRVNPGVeahthefiqtgqEDSKFGLSIKHglALEAINKVKASKHLQ 193
Cdd:cd06808 78 AEQGVIVVTVDSLEELEKLEEAALKAgppARVLLRIDTGD------------ENGKFGVRPEE--LKALLERAKELPHLR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488383836 194 LKGVHFHVGSQIEGTEAMIETAKLVLHWLS---ENEIKVELLNLGGGFGIKY 242
Cdd:cd06808 144 LVGLHTHFGSADEDYSPFVEALSRFVAALDqlgELGIDLEQLSIGGSFAILY 195
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
18-380 |
1.36e-32 |
|
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: 127.38 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 18 LKTVAQSFGTPTIVYDEDQIRNQMRRYHSAFEKSGLKYNISYASKAFTCIQMVKLVQEEDLQLDVVSEGELYTALEAGFD 97
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 98 ANRIHFHGNNKTKREIQYALENNIgYFVIDALEEIDLIDK----YASDEVNIVLRVNPgvEAHTHEfiqtgqedSKFGLS 173
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLAlargYTTGPARVLLRLSP--FPASLP--------SRFGMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 174 IKH-GLALEAINkvKASKHLQLKGVHFHV-GSQIEGTEAMIETAKLVLHWLSENEIKVELLNLGGGFGIKYVEGDE---- 247
Cdd:cd06842 150 AAEvRTALERLA--QLRERVRLVGFHFHLdGYSAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAAewea 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 248 ----------------SFPIEEGIAEI-------------ADAIKETAHSLNYEVPEIG-----------IEPGRSIVGE 287
Cdd:cd06842 228 flaaltealygygrplTWRNEGGTLRGpddfypygqplvaADWLRAILSAPLPQGRTIAerlrdngitlaLEPGRALLDQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 288 AGITLYEVGTIKEIPEVNKYVSVDGGMSDhIRTALYDAKYQALLVNRNEEADDT----VTIAGKLCESGDIIIK-KAKLP 362
Cdd:cd06842 308 CGLTVARVAFVKQLGDGNHLIGLEGNSFS-ACEFSSEFLVDPLLIPAPEPTTDGapieAYLAGASCLESDLITRrKIPFP 386
|
410
....*....|....*...
gi 488383836 363 SSIKRGDYLAILSTGAYH 380
Cdd:cd06842 387 RLPKPGDLLVFPNTAGYQ 404
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
26-388 |
1.34e-27 |
|
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: 113.05 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 26 GTPTIVYDEDQIRNQMRRYHSAFEKSGLKYNisYASKaFTCIQMVKLVQEEDLQLDVVSEGELYTA-LEAG--FDANRIH 102
Cdd:cd06830 4 GLPLLLRFPDILRHRIERLNAAFAKAIEEYG--YKGK-YQGVYPIKVNQQREVVEEIVKAGKRYNIgLEAGskPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 103 FHGNNKT--------KRE--IQYAL-ENNIGY---FVIDALEEIDLIDKyASDEVNIVLRVnpGV-----EAHTHEFIQT 163
Cdd:cd06830 81 ALLKTPDaliicngyKDDeyIELALlARKLGHnviIVIEKLSELDLILE-LAKKLGVKPLL--GVriklaSKGSGKWQES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 164 GQEDSKFGLSIKHglALEAINKVKASKHLQ-LKGVHFHVGSQIEGT----EAMIETAKLV--LHWLSENeikVELLNLGG 236
Cdd:cd06830 158 GGDRSKFGLTASE--ILEVVEKLKEAGMLDrLKLLHFHIGSQITDIrrikSALREAARIYaeLRKLGAN---LRYLDIGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 237 GFGIKYvEGDES-------FPIEEGIAEIADAIKETAHSLNYEVPEIGIEPGRSIVGEAGITLYEVGTIKEIPEvnKYV- 308
Cdd:cd06830 233 GLGVDY-DGSRSssdssfnYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGVKRLAD--WYFc 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 309 --SVDGGMSDHIrtALyDAKYQALLVNR-NEEADDTVTIAGKLCESGDIIIK-------KAKLPSSIKRGD---YLAILS 375
Cdd:cd06830 310 nfSLFQSLPDSW--AI-DQLFPIMPLHRlNEKPTRRAVLGDITCDSDGKIDSfidppdiLPTLPLHPLRKDepyYLGFFL 386
|
410
....*....|...
gi 488383836 376 TGAYHYSMASNYN 388
Cdd:cd06830 387 VGAYQEILGDLHN 399
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
80-384 |
2.69e-25 |
|
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: 106.21 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 80 LDVVSEGELyTALEAGFDANRIHFHGNNKTKREIQYALENNIGYFVIDALEEIDLIDKYASDE---VNIVLRVNPGVEAH 156
Cdd:cd06843 52 FEVASGGEI-AHVRAAVPDAPLIFGGPGKTDSELAQALAQGVERIHVESELELRRLNAVARRAgrtAPVLLRVNLALPDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 157 THEFIQTGQEDSKFGLSIKHGLAleAINKVKASKHLQLKGVHFHVGS-QIEGTE--AMIET-AKLVLHWLSENEIKVELL 232
Cdd:cd06843 131 PSSTLTMGGQPTPFGIDEADLPD--ALELLRDLPNIRLRGFHFHLMShNLDAAAhlALVKAyLETARQWAAEHGLDLDVV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 233 NLGGGFGIKYVEGDESFPIEEGIAEIADAIKETAhslnyEVPEIGIEPGRSIVGEAGITLYEVGTIKEIPevNKYVSVDG 312
Cdd:cd06843 209 NVGGGIGVNYADPEEQFDWAGFCEGLDQLLAEYE-----PGLTLRFECGRYISAYCGYYVTEVLDLKRSH--GEWFAVLR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 313 GMSDHIRTALYDAKYQALLVNRNEEADD----------TVTIAGKLCESGDIIIKKAKLPsSIKRGDYLAILSTGAYHYS 382
Cdd:cd06843 282 GGTHHFRLPAAWGHNHPFSVLPVEEWPYpwprpsvrdtPVTLVGQLCTPKDVLARDVPVD-RLRAGDLVVFPLAGAYGWN 360
|
..
gi 488383836 383 MA 384
Cdd:cd06843 361 IS 362
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
35-295 |
9.60e-12 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 66.63 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 35 DQIRNQMRRYHSAFEKSGLKYniSYASKaFTCIQMVKLVQEEDLQLDVVSEGELYT-ALEAGFDANRI-----HFHGNN- 107
Cdd:PLN02439 7 DVLKNRLESLQSAFDYAIQSQ--GYNSH-YQGVFPVKCNQDRFLVEDIVKFGSPFRfGLEAGSKPELLlamscLCKGSPd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 108 --------KTKREIQYALE------NNIgyFVIDALEEIDLIDKYASDevnivLRVNP--GVEA-----HTHEFIQTGQE 166
Cdd:PLN02439 84 aflicngyKDAEYVSLALLarklglNTV--IVLEQEEELDLVIEASQR-----LGVRPviGVRAklrtkHSGHFGSTSGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 167 DSKFGLSIKHglALEAINKVKASKHLQ-LKGVHFHVGSQIEGT----EAMIETA----KLVLhwLSENeikVELLNLGGG 237
Cdd:PLN02439 157 KGKFGLTATE--IVRVVRKLRKEGMLDcLQLLHFHIGSQIPSTsllkDGVSEAAqiycELVR--LGAP---MRVIDIGGG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488383836 238 FGIKY-----VEGDES--FPIEEGIAEIADAIKETAHSLNYEVPEIGIEPGRSIVGEAGITLYEV 295
Cdd:PLN02439 230 LGIDYdgsksGSSDMSvaYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEA 294
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
123-285 |
7.23e-09 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 57.82 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 123 YFVIDALEEIDLIDKyASDEVNIVLRVnpGVEA--HTH---EFIQTGQEDSKFGLSIKHglALEAINKVKASKHLQ-LKG 196
Cdd:PRK05354 174 FIVIEKLSELELILE-EAKELGVKPRL--GVRArlASQgsgKWQSSGGEKSKFGLSATE--VLEAVERLREAGLLDcLQL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 197 VHFHVGSQIegTE------AMIETAKlvlhwlseneIKVEL---------LNLGGGFGIKYvEGDES-------FPIEEG 254
Cdd:PRK05354 249 LHFHLGSQI--ANirdiktAVREAAR----------FYVELrklgapiqyLDVGGGLGVDY-DGTRSqsdssvnYSLQEY 315
|
170 180 190
....*....|....*....|....*....|.
gi 488383836 255 IAEIADAIKETAHSLNYEVPEIGIEPGRSIV 285
Cdd:PRK05354 316 ANDVVYTLKEICEEHGVPHPTIISESGRALT 346
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
27-395 |
8.52e-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: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 27 TPTIVYDEDQIRNQMRRYHSAFEKSGLKynISYASKAFTCIQMVKLVQEedlQLDVVSEGELYTALEAgfdanRIHFHGN 106
Cdd:cd06829 1 TPCYVLDEAKLRRNLEILKRVQERSGAK--ILLALKAFSMWSVFPLIRE---YLDGTTASSLFEARLG-----REEFGGE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 107 NKT------KREIQYALENNiGYFVIDALEEIDLI-DKYASDEVNIVLRVNPGVEAHTHEFIQTGQEDSKFG--LSIKHG 177
Cdd:cd06829 71 VHTyspayrDDEIDEILRLA-DHIIFNSLSQLERFkDRAKAAGISVGLRINPEYSEVETDLYDPCAPGSRLGvtLDELEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 178 LALEAINkvkaskhlqlkGVHFHVGSQiEGTEAMIETAKLVL----HWLSeneiKVELLNLGGGFGIKyvegDESFPIEE 253
Cdd:cd06829 150 EDLDGIE-----------GLHFHTLCE-QDFDALERTLEAVEerfgEYLP----QLKWLNLGGGHHIT----RPDYDVDR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 254 GIAEIADaIKETahslnYEVpEIGIEPGRSIVGEAGitlYEVGTIKEIpevnkyvsVDGGMsdhiRTALYDAK------- 326
Cdd:cd06829 210 LIALIKR-FKEK-----YGV-EVYLEPGEAVALNTG---YLVATVLDI--------VENGM----PIAILDASatahmpd 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488383836 327 -----YQ--ALLVNRNEEADDTVTIAGKLCESGDiIIKKAKLPSSIKRGDYLAILSTGayHYSMASN--YNQMQKPSV 395
Cdd:cd06829 268 vlempYRppIRGAGEPGEGAHTYRLGGNSCLAGD-VIGDYSFDEPLQVGDRLVFEDMA--HYTMVKTntFNGVRLPSI 342
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
123-285 |
6.35e-08 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 54.71 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 123 YFVIDALEEIDLIDKYAsDEVNIV----LRVNPGVEAHTHefIQ-TGQEDSKFGLSIKHglALEAINKVKASKHLQ-LKG 196
Cdd:COG1166 170 IIVIEKLSELELILEEA-KELGVKpligVRVKLASKGSGK--WQnSGGERSKFGLSASE--ILEVVERLKEAGMLDcLQL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488383836 197 VHFHVGSQIegT------EAMIETAKlvlhwlseneIKVEL---------LNLGGGFGIKYvEGDES-FP------IEEG 254
Cdd:COG1166 245 LHFHLGSQI--PnirdikRAVREAAR----------FYAELrklgapieyLDVGGGLGVDY-DGSRSnSDssmnysLQEY 311
|
170 180 190
....*....|....*....|....*....|.
gi 488383836 255 IAEIADAIKETAHSLNYEVPEIGIEPGRSIV 285
Cdd:COG1166 312 ANDVVYAIKEVCDEAGVPHPTIISESGRALT 342
|
|
| |
