|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
1-419 |
0e+00 |
|
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: 513.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 1 MTvKYNQNGELTMDGISLKTIAQSFGTPTIVYDELQIREQMRRYHRAFKDSGLKynISYASKAFTCIQMVKLVAEEDLQL 80
Cdd:COG0019 1 MT-HFARDGELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAK--VLYAVKANSNLAVLRLLAEEGLGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 81 DVVSEGELYTALEAGFEPSRIHFHGNNKTKHEIRYALENNIGYFVIDSLEEIELIDRYAND---TVQVVLRVNPGVEAHT 157
Cdd:COG0019 78 DVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAElgkRAPVGLRVNPGVDAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 158 HEFIQTGQEDSKFGLSIQygLAKKAIDKVQQSKHLKLKGVHCHIGSQIEGTEAFIETAKIVLRW---LKEQGIQVELLNL 234
Cdd:COG0019 158 HEYISTGGKDSKFGIPLE--DALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELaeeLRELGIDLEWLDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 235 GGGFGIKYVEGDESFPIEsgikDITDAIKSEIKVLGIDAPEIGIEPGRSIVGEAGVTLYEVGTIKEIPEINkYVSIDGGM 314
Cdd:COG0019 236 GGGLGIPYTEGDEPPDLE----ELAAAIKEALEELCGLGPELILEPGRALVGNAGVLLTRVLDVKENGGRR-FVIVDAGM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 315 SDHIRTALYDAKYQALLVNRNEEADD-SVTIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSMASNYNQMQKP 393
Cdd:COG0019 311 NDLMRPALYGAYHPIVPVGRPSGAEAeTYDVVGPLCESGDVLGKDRSLP-PLEPGDLLAFLDAGAYGFSMASNYNGRPRP 389
|
410 420
....*....|....*....|....*.
gi 1332406779 394 SVFFLKDGKAREVIKRQSLRQLIIND 419
Cdd:COG0019 390 AEVLVDDGEARLIRRRETYEDLLASE 415
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
25-398 |
6.74e-174 |
|
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: 490.46 E-value: 6.74e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 25 FGTPTIVYDELQIREQMRRYHRAFKDSGLKynISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFH 104
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFK--ICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 105 GNNKTKHEIRYALENNIGYFVIDSLEEIELIDRYA---NDTVQVVLRVNPGVEAHTHEFIQTGQEDSKFGlsIQYGLAKK 181
Cdd:cd06828 79 GNGKSDEELELALELGILRINVDSLSELERLGEIApelGKGAPVALRVNPGVDAGTHPYISTGGKDSKFG--IPLEQALE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 182 AIDKVQQSKHLKLKGVHCHIGSQIEGTEAFIETAKIVLRW---LKEQGIQVELLNLGGGFGIKYVEGDESFPIESGIKDI 258
Cdd:cd06828 157 AYRRAKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLaaeLRELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 259 TDAIKSEIKvlGIDAPEIGIEPGRSIVGEAGVTLYEVGTIKEIPeINKYVSIDGGMSDHIRTALYDAKYQALLVNRNEEA 338
Cdd:cd06828 237 AEALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETG-GKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEG 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332406779 339 DD-SVTIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:cd06828 314 ETeKVDVVGPICESGDVFAKDRELP-EVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
5-416 |
8.03e-153 |
|
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: 438.65 E-value: 8.03e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 5 YNQNGELTMDGISLKTIAQSFGTPTIVYDELQIREQMRRYHRAFKDSGLkynISYASKAFTCIQMVKLVAEEDLQLDVVS 84
Cdd:TIGR01048 3 ENEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRSL---VCYAVKANSNLAVLRLLAELGSGFDVVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 85 EGELYTALEAGFEPSRIHFHGNNKTKHEIRYALENNIgYFVIDSLEEIELIDRYA---NDTVQVVLRVNPGVEAHTHEFI 161
Cdd:TIGR01048 80 GGELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIApelGKKARISLRVNPGVDAKTHPYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 162 QTGQEDSKFGLSIQygLAKKAIDKVQQSKHLKLKGVHCHIGSQIEGTEAFIETAKIVLRWLKE--QGIQVELLNLGGGFG 239
Cdd:TIGR01048 159 STGLKDSKFGIDVE--EALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESlaEGIDLEFLDLGGGLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 240 IKYVEGDESFPIESGIKDITDAIKsEIKVLGIDaPEIGIEPGRSIVGEAGVTLYEVGTIKEIPEINkYVSIDGGMSDHIR 319
Cdd:TIGR01048 237 IPYTPEEEPPDLSEYAQAILNALE-GYADLGLD-PKLILEPGRSIVANAGVLLTRVGFVKETGSRN-FVIVDAGMNDLIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 320 TALYDAKYQALLVNR-NEEADDSVTIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:TIGR01048 314 PALYGAYHHIIVLNRtNDAPTEVADVVGPVCESGDVLAKDRELP-EVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLV 392
|
410
....*....|....*...
gi 1332406779 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 |
7.84e-107 |
|
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: 319.05 E-value: 7.84e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 31 VYDELQIREQMRRYHRAFKDsglKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFHGNNKTK 110
Cdd:pfam00278 3 VYDLATLRRNYRRWKAALPP---RVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 111 HEIRYALENNIGYFVIDSLEEIELIDRYA-NDTVQVVLRVNPGVEAHTHeFIQTGQEDSKFGLSIQygLAKKAIDKVQQS 189
Cdd:pfam00278 80 SEIRYALEAGVLCFNVDSEDELEKIAKLApELVARVALRINPDVDAGTH-KISTGGLSSKFGIDLE--DAPELLALAKEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 190 kHLKLKGVHCHIGSQIEGTEAFIETAKIVLR---WLKEQGIQVELLNLGGGFGIKYvEGDESFPIEsgikDITDAIKSEI 266
Cdd:pfam00278 157 -GLNVVGVHFHIGSQITDLEPFVEALQRARElfdRLRELGIDLKLLDIGGGFGIPY-RDEPPPDFE----EYAAAIREAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 267 KVLGIDAPEIGIEPGRSIVGEAGVTLYEVGTIKEIPEINkYVSIDGGMSDHIRTALYDAKYQALLVNRNEEADD-SVTIA 345
Cdd:pfam00278 231 DEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKT-FVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLeTYDVV 309
|
330 340 350
....*....|....*....|....*....|..
gi 1332406779 346 GKLCESGDIIIKDAKLPsSVKRGDYLAILSTG 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 |
2.05e-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: 298.45 E-value: 2.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 27 TPTIVYDELQIREQMRRYHRAFKdsgLKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFHGN 106
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALP---SGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 107 NKTKHEIRYALENNIGYFVIDSLEEIELIDRYA---NDTVQVVLRVNPGVEAHTHeFIQTGQEDSKFGLSiqYGLAKKAI 183
Cdd:cd06810 78 AKSVSEIEAALASGVDHIVVDSLDELERLNELAkklGPKARILLRVNPDVSAGTH-KISTGGLKSKFGLS--LSEARAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 184 DKVQQSkHLKLKGVHCHIGSQI---EGTEAFIETAKIVLRWLKEQGIQVELLNLGGGFGIKYVEgdESFPIESGIKDITD 260
Cdd:cd06810 155 ERAKEL-DLRLVGLHFHVGSQIldlETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE--QPLDFEEYAALINP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 261 AIKSEIKVLGidAPEIGIEPGRSIVGEAGVTLYEVGTIKEIPEInKYVSIDGGMSDHIRTALYDAKYQALLVNRNEEADD 340
Cdd:cd06810 232 LLKKYFPNDP--GVTLILEPGRYIVAQAGVLVTRVVAVKVNGGR-FFAVVDGGMNHSFRPALAYDAYHPITPLKAPGPDE 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332406779 341 S---VTIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:cd06810 309 PlvpATLAGPLCDSGDVIGRDRLLP-ELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
36-286 |
2.15e-64 |
|
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: 206.75 E-value: 2.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 36 QIREQMRRYHRAFKDsglkYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFHGNNKTKHEIRY 115
Cdd:pfam02784 3 SIERRHRRWKKALPR----IKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 116 ALENNIGYFVIDSLEEIELIDRYANDTvQVVLRVNPGVEAHTHEFiqtgqeDSKFGLSIQYGLAkkAIDKVQQSKHLKLK 195
Cdd:pfam02784 79 ALEVGVGCVTVDNVDELEKLARLAPEA-RVLLRIKPDDSAATCPL------SSKFGADLDEDVE--ALLEAAKLLNLQVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 196 GVHCHIGSQIEGTEAF---IETAKIVLRWLKEQGIQVELLNLGGGFGIKYVEGDESFPIESGIKDITDAIksEIKVLGID 272
Cdd:pfam02784 150 GVSFHVGSGCTDAEAFvlaLEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINEAL--EEYFPGDP 227
|
250
....*....|....
gi 1332406779 273 APEIGIEPGRSIVG 286
Cdd:pfam02784 228 GVTIIAEPGRYFVA 241
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
21-402 |
1.16e-63 |
|
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: 209.04 E-value: 1.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 21 IAQSFGTPTIVYDELQIREQMRRYHRAFKDSGLKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSR 100
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 101 IHFHGNNKTKHEIRYALENNiGYFVIDSLEEIELIDRYAND---TVQVVLRVNpgveahtheFIQTGQEDSKFGLSIQY- 176
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEG-ALINIDSFDELERILEIAKElgrVAKVGIRLN---------MNYGNNVWSRFGFDIEEn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 177 GLAKKAIDKVQQSKHLKLKGVHCHIGSQIEGTEAFIETAKIVLRWLKE-QGIQVELLNLGGGFG------IKYVEGDESF 249
Cdd:cd06841 151 GEALAALKKIQESKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRlFGLELEYLDLGGGFPaktplsLAYPQEDTVP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 250 PIESGIKDITDAIKSEIKvLGIDAPEIGIEPGRSIVGEAGVTLYEVGTIKEIPEINKYVsIDGGMsDHIRTALYdaKYQA 329
Cdd:cd06841 231 DPEDYAEAIASTLKEYYA-NKENKPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAV-TDAGI-NNIPTIFW--YHHP 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332406779 330 LLVNR---NEEADDSVTIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSMASNYNQMQkPSVFFLKDGK 402
Cdd:cd06841 306 ILVLRpgkEDPTSKNYDVYGFNCMESDVLFPNVPLP-PLNVGDILAIRNVGAYNMTQSNQFIRPR-PAVYLIDNNG 379
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
27-406 |
6.13e-63 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 208.11 E-value: 6.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 27 TPTIVYDELQIREQMRRYHRAFKdsGLKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFHGN 106
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALE--GLRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 107 NKTKHEIRYALENniGYFV-IDS---LEEIELIDRYANDTVQVVLRVNPGVEAHTHEFIQTGQEDSKFGL---SIQYGLa 179
Cdd:PLN02537 96 GKLLEDLVLAAQE--GVFVnVDSefdLENIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNSKFGIrneKLQWFL- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 180 kkaiDKVQQ-SKHLKLKGVHCHIGSQIEGTEAFIETAKIVLRWLKE---QGIQVELLNLGGGFGIKYVEGDESFPIEsgi 255
Cdd:PLN02537 173 ----DAVKAhPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEiraQGFELSYLNIGGGLGIDYYHAGAVLPTP--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 256 KDITDAIKSEIKVLGIDapeIGIEPGRSIVGEAGVTLYEVGTIKEIPEINkYVSIDGGMSDHIRTALYDAkYQALLVNRN 335
Cdd:PLN02537 246 RDLIDTVRELVLSRDLT---LIIEPGRSLIANTCCFVNRVTGVKTNGTKN-FIVIDGSMAELIRPSLYDA-YQHIELVSP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1332406779 336 EEADDSVT---IAGKLCESGDIIIKDAKLPSSvKRGDYLAILSTGAYHYSMASNYN-QMQKPSVFFLKDGKAREV 406
Cdd:PLN02537 321 PPPDAEVStfdVVGPVCESADFLGKDRELPTP-PKGAGLVVHDAGAYCMSMASTYNlKMRPPEYWVEEDGSITKI 394
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
21-385 |
8.25e-61 |
|
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: 201.67 E-value: 8.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 21 IAQSFGTPTIVYDELQIREQMRRYHRAFKDsglKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSR 100
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAALPP---AIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 101 IHFHGNNKTKHEIRYALENNIGYFVIDSLEEIELIDRYA---NDTVQVVLRVNPGVEAhTHEFIQTGQEDSKFGLSIQYG 177
Cdd:cd06839 78 ILFAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAeehGVVARVALRINPDFEL-KGSGMKMGGGPSQFGIDVEEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 178 LAkkAIDKVQQSKHLKLKGVHCHIGSQIEGTEAFIE----TAKIVLRWLKEQGIQVELLNLGGGFGIKYVEGDESFPIES 253
Cdd:cd06839 157 PA--VLARIAALPNLRFVGLHIYPGTQILDADALIEafrqTLALALRLAEELGLPLEFLDLGGGFGIPYFPGETPLDLEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 254 gikdITDAIKSEIKVLG--IDAPEIGIEPGRSIVGEAGVTLYEVGTIKeIPEINKYVSIDGGMSDH----------IRTa 321
Cdd:cd06839 235 ----LGAALAALLAELGdrLPGTRVVLELGRYLVGEAGVYVTRVLDRK-VSRGETFLVTDGGMHHHlaasgnfgqvLRR- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1332406779 322 lydaKYQALLVNRNE-EADDSVTIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSmAS 385
Cdd:cd06839 309 ----NYPLAILNRMGgEERETVTVVGPLCTPLDLLGRNVELP-PLEPGDLVAVLQSGAYGLS-AS 367
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
26-398 |
5.77e-58 |
|
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: 193.86 E-value: 5.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 26 GTPTIVYDELQIREQMRRYHRAFKDSglkyNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFHG 105
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRV----RPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 106 NNKTKHEIRYALENNIGYFVIDSLEEIELIDRYAnDTVQVVLRvnpgveahthefIQTGQEDSKFGLSIQYGLA-KKAID 184
Cdd:cd00622 77 PCKSISDIRYAAELGVRLFTFDSEDELEKIAKHA-PGAKLLLR------------IATDDSGALCPLSRKFGADpEEARE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 185 KVQQSK--HLKLKGVHCHIGSQIEGTEAF---IETAKIVLRWLKEQGIQVELLNLGGGFGIKYVEGDESFpiesgiKDIT 259
Cdd:cd00622 144 LLRRAKelGLNVVGVSFHVGSQCTDPSAYvdaIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSF------EEIA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 260 DAIKSEI-KVLGIDAPEIGIEPGRSIVGEAGVTLYEVGTIKEIPEINKYVS--ID----GGMSDhirtALYD-AKYQALL 331
Cdd:cd00622 218 AVINRALdEYFPDEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERWyyLNdgvyGSFNE----ILFDhIRYPPRV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1332406779 332 VNRNEEADD--SVTIAGKLCESGDIIIKDAKLPSSVKRGDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:cd00622 294 LKDGGRDGElyPSSLWGPTCDSLDVIYEDVLLPEDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
26-394 |
1.71e-56 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 199.54 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 26 GTPTIVYDELQIREQMRRYhrafkdSGLKY--NISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEA--GFEPSRI 101
Cdd:PRK08961 502 GSPCYVYHLPTVRARARAL------AALAAvdQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERV 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 102 HFHGNNKTKHEIRYALEnnIGYFV-IDSLEEIEL-IDRYANDTVqvVLRVNPGVEAHTHEFIQTGQEDSKFGLSIQYglA 179
Cdd:PRK08961 576 LFTPNFAPRAEYEAAFA--LGVTVtLDNVEPLRNwPELFRGREV--WLRIDPGHGDGHHEKVRTGGKESKFGLSQTR--I 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 180 KKAIDKVQQSkHLKLKGVHCHIGSQIEGTEAFIETAKIvLRWLKEQGIQVELLNLGGGFGIKYVEGDESFPIESgikdiT 259
Cdd:PRK08961 650 DEFVDLAKTL-GITVVGLHAHLGSGIETGEHWRRMADE-LASFARRFPDVRTIDLGGGLGIPESAGDEPFDLDA-----L 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 260 DAIKSEIKVLGIDApEIGIEPGRSIVGEAGVTLYEVGTIKEIPEInKYVSIDGGMSDHIRTALYDAKYQALLVNR-NEEA 338
Cdd:PRK08961 723 DAGLAEVKAQHPGY-QLWIEPGRYLVAEAGVLLARVTQVKEKDGV-RRVGLETGMNSLIRPALYGAYHEIVNLSRlDEPA 800
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1332406779 339 DDSVTIAGKLCESGDIIIKDAKLPSSvKRGDYLAILSTGAYHYSMASNYNQMQKPS 394
Cdd:PRK08961 801 AGTADVVGPICESSDVLGKRRRLPAT-AEGDVILIANAGAYGYSMSSTYNLREPAR 855
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
28-388 |
1.19e-53 |
|
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: 182.63 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 28 PTIVYDELQIREqmrryhRAFKDSGLKYNIS--YASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEA--GFEPSRIHF 103
Cdd:cd06840 13 PCYVYDLETVRA------RARQVSALKAVDSlfYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 104 HGNNKTKHEIRYALENNIgYFVIDSLEEIELI-DRYANdtVQVVLRVNPGVEAHTHEFIQTGQEDSKFGLSiQYGLAkKA 182
Cdd:cd06840 87 TPNFAARSEYEQALELGV-NVTVDNLHPLREWpELFRG--REVILRIDPGQGEGHHKHVRTGGPESKFGLD-VDELD-EA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 183 IDKVQQSkHLKLKGVHCHIGSQIEGTEAFIETAKIVLRwLKEQGIQVELLNLGGGFGIKYVEGDESFPIESgIKDITDAI 262
Cdd:cd06840 162 RDLAKKA-GIIVIGLHAHSGSGVEDTDHWARHGDYLAS-LARHFPAVRILNVGGGLGIPEAPGGRPIDLDA-LDAALAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 263 KSEIKVLgidapEIGIEPGRSIVGEAGVTLYEVGTIKEIPEInKYVSIDGGMSDHIRTALYDAKYQALLVNR-NEEADDS 341
Cdd:cd06840 239 KAAHPQY-----QLWMEPGRFIVAESGVLLARVTQIKHKDGV-RFVGLETGMNSLIRPALYGAYHEIVNLSRlDEPPAGN 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1332406779 342 VTIAGKLCESGDIIIKDAKLPSSvKRGDYLAILSTGAYHYSMASNYN 388
Cdd:cd06840 313 ADVVGPICESGDVLGRDRLLPET-EEGDVILIANAGAYGFCMASTYN 358
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
26-396 |
1.80e-45 |
|
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: 161.41 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 26 GTPTI-VYDELQIREQMRRYHRAFKDSGLKyniSYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFH 104
Cdd:cd06836 1 VHPAVgLYDLDGFRALVARLTAAFPAPVLH---TFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 105 GNNKTKHEIRYALENNIgYFVIDSLEEIELID----RYANDTVQVVLRVNPGVEAHTHEFIQTGQEDSKFGlsiqYGLAK 180
Cdd:cd06836 78 SPAKTRAELREALELGV-AINIDNFQELERIDalvaEFKEASSRIGLRVNPQVGAGKIGALSTATATSKFG----VALED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 181 KAIDKVQQS--KHLKLKGVHCHIGSQ-------IEGTEAFIETAKIVLRWLKEQgiQVELLNLGGGFGIKYvEGDESFPI 251
Cdd:cd06836 153 GARDEIIDAfaRRPWLNGLHVHVGSQgcelsllAEGIRRVVDLAEEINRRVGRR--QITRIDIGGGLPVNF-ESEDITPT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 252 esgIKDITDAIKSEIKVLGIDAPEIGIEPGRSIVGEAGVTLYEVgtikeipeinKYVSIDG---------GMSDHIRTA- 321
Cdd:cd06836 230 ---FADYAAALKAAVPELFDGRYQLVTEFGRSLLAKCGTIVSRV----------EYTKSSGgrriaithaGAQVATRTAy 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 322 ---LYDAKYQALLVNRNEEADDSV--TIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSMASNYNQMQKPSVF 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 ... |
37-255 |
1.23e-44 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 154.01 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 37 IREQMRRYHRAFkdsGLKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGFEPSRIHFHGNNKTKHEIRYA 116
Cdd:cd06808 1 IRHNYRRLREAA---PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 117 LENNIGYFVIDSLEEIELIDRYA---NDTVQVVLRVNPGVeahthefiqtgqEDSKFGlsIQYGLAKKAIDKVQQSKHLK 193
Cdd:cd06808 78 AEQGVIVVTVDSLEELEKLEEAAlkaGPPARVLLRIDTGD------------ENGKFG--VRPEELKALLERAKELPHLR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1332406779 194 LKGVHCHIGSQIEGTEAFIETAKIV---LRWLKEQGIQVELLNLGGGFGIKYVEGDESFP---IESGI 255
Cdd:cd06808 144 LVGLHTHFGSADEDYSPFVEALSRFvaaLDQLGELGIDLEQLSIGGSFAILYLQELPLGTfiiVEPGR 211
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
18-380 |
1.15e-29 |
|
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: 119.29 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 18 LKTIAQSFGTP-TIVYDElQIREQMRRYHRAFKDSGLKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELYTALEAGF 96
Cdd:cd06842 1 LVALVEAYGSPlNVLFPQ-TFRENIAALRAVLDRHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 97 EPSRIHFHGNNKTKHEIRYALENNIgYFVIDSLEEIELID----RYANDTVQVVLRVNPgvEAHTHEfiqtgqedSKFGL 172
Cdd:cd06842 80 RGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLalarGYTTGPARVLLRLSP--FPASLP--------SRFGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 173 SIQyGLAkKAIDKVQQS-KHLKLKGVHCHIG--SQIEGTEAFIETAKIVLRwLKEQGIQVELLNLGGGFGIKYVEGDE-- 247
Cdd:cd06842 149 PAA-EVR-TALERLAQLrERVRLVGFHFHLDgySAAQRVAALQECLPLIDR-ARALGLAPRFIDIGGGFPVSYLADAAew 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 248 ------------------SFPIESGIKDITDA---------------------------IKSEIKVLGIDapeIGIEPGR 282
Cdd:cd06842 226 eaflaaltealygygrplTWRNEGGTLRGPDDfypygqplvaadwlrailsaplpqgrtIAERLRDNGIT---LALEPGR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 283 SIVGEAGVTLYEVGTIKEIPEINKYVSIDGGMSDhIRTALYDAKYQALLVNRNEEADDS----VTIAGKLCESGDIIIKD 358
Cdd:cd06842 303 ALLDQCGLTVARVAFVKQLGDGNHLIGLEGNSFS-ACEFSSEFLVDPLLIPAPEPTTDGapieAYLAGASCLESDLITRR 381
|
410 420
....*....|....*....|...
gi 1332406779 359 -AKLPSSVKRGDYLAILSTGAYH 380
Cdd:cd06842 382 kIPFPRLPKPGDLLVFPNTAGYQ 404
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
31-384 |
1.75e-26 |
|
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: 109.68 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 31 VYDELQIREQMRRYHRAFKDsglKYNISYASKAFTCIQMVKLVAEEDLQLDVVSEGELyTALEAGFEPSRIHFHGNNKTK 110
Cdd:cd06843 6 VYDLAALRAHARALRASLPP---GCELFYAIKANSDPPILRALAPHVDGFEVASGGEI-AHVRAAVPDAPLIFGGPGKTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 111 HEIRYALENNIGYFVIDSLEEIELID---RYANDTVQVVLRVNPGVEAHTHEFIQTGQEDSKFGLSIQYGLAkkAIDKVQ 187
Cdd:cd06843 82 SELAQALAQGVERIHVESELELRRLNavaRRAGRTAPVLLRVNLALPDLPSSTLTMGGQPTPFGIDEADLPD--ALELLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 188 QSKHLKLKGVHCHIGS-QIEGTE--AFIET-AKIVLRWLKEQGIQVELLNLGGGFGIKYVEGDESFPIESGIKDITDAIK 263
Cdd:cd06843 160 DLPNIRLRGFHFHLMShNLDAAAhlALVKAyLETARQWAAEHGLDLDVVNVGGGIGVNYADPEEQFDWAGFCEGLDQLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 264 SEikvlgIDAPEIGIEPGRSIVGEAGVTLYEVGTIKEIpeINKYVSIDGGMSDHIRTALYDAKYQALLVNRNEEADD--- 340
Cdd:cd06843 240 EY-----EPGLTLRFECGRYISAYCGYYVTEVLDLKRS--HGEWFAVLRGGTHHFRLPAAWGHNHPFSVLPVEEWPYpwp 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1332406779 341 -------SVTIAGKLCESGDIIIKDAKLPsSVKRGDYLAILSTGAYHYSMA 384
Cdd:cd06843 313 rpsvrdtPVTLVGQLCTPKDVLARDVPVD-RLRAGDLVVFPLAGAYGWNIS 362
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
26-388 |
5.69e-22 |
|
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: 96.87 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 26 GTPTIVYDELQIREQMRRYHRAFKDSGLKYNisYASKaFTCIQMVKLVAEEDLQLDVVSEGELYTA-LEAG--FEPSRIH 102
Cdd:cd06830 4 GLPLLLRFPDILRHRIERLNAAFAKAIEEYG--YKGK-YQGVYPIKVNQQREVVEEIVKAGKRYNIgLEAGskPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 103 FHGNNKT--------KHE--IRYAL-ENNIGY---FVIDSLEEIELIDRYANDtVQVVLRVnpGV-----EAHTHEFIQT 163
Cdd:cd06830 81 ALLKTPDaliicngyKDDeyIELALlARKLGHnviIVIEKLSELDLILELAKK-LGVKPLL--GVriklaSKGSGKWQES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 164 GQEDSKFGLSIQ--YGLAKKAIdKVQQSKHLKLkgVHCHIGSQIEGT----EAFIETAKIVLRwLKEQGIQVELLNLGGG 237
Cdd:cd06830 158 GGDRSKFGLTASeiLEVVEKLK-EAGMLDRLKL--LHFHIGSQITDIrrikSALREAARIYAE-LRKLGANLRYLDIGGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 238 FGIKYvEGDES-------FPIESGIKDITDAIKSEIKVLGIDAPEIGIEPGRSIVGEAGVTLYEVGTIKEIPEinKYV-- 308
Cdd:cd06830 234 LGVDY-DGSRSssdssfnYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGVKRLAD--WYFcn 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 309 -SIDGGMSDHIrtALyDAKYQALLVNR-NEEADDSVTIAGKLCES---------GDIIIKDAKLPSSVKRGDY-LAILST 376
Cdd:cd06830 311 fSLFQSLPDSW--AI-DQLFPIMPLHRlNEKPTRRAVLGDITCDSdgkidsfidPPDILPTLPLHPLRKDEPYyLGFFLV 387
|
410
....*....|..
gi 1332406779 377 GAYHYSMASNYN 388
Cdd:cd06830 388 GAYQEILGDLHN 399
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
125-295 |
9.26e-10 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 60.47 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 125 VIDSLEEIELIDRYANDtvqvvLRVNP--GVEA-----HTHEFIQTGQEDSKFGLSIQ--YGLAKKaIDKVQQSKHLKLk 195
Cdd:PLN02439 113 VLEQEEELDLVIEASQR-----LGVRPviGVRAklrtkHSGHFGSTSGEKGKFGLTATeiVRVVRK-LRKEGMLDCLQL- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 196 gVHCHIGSQIEGT----EAFIETAKIVLRwLKEQGIQVELLNLGGGFGIKY-----VEGDES--FPIESGIKDITDAIKS 264
Cdd:PLN02439 186 -LHFHIGSQIPSTsllkDGVSEAAQIYCE-LVRLGAPMRVIDIGGGLGIDYdgsksGSSDMSvaYSLEEYANAVVAAVRD 263
|
170 180 190
....*....|....*....|....*....|.
gi 1332406779 265 EIKVLGIDAPEIGIEPGRSIVGEAGVTLYEV 295
Cdd:PLN02439 264 VCDRKGVKHPVICSESGRALVSHHSVLIFEA 294
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
27-395 |
9.07e-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: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 27 TPTIVYDELQIREQMRRYHRAFKDSGLKynISYASKAFTCIQMVKLVAEedlQLDVVSEGELYtalEA--GFE--PSRIH 102
Cdd:cd06829 1 TPCYVLDEAKLRRNLEILKRVQERSGAK--ILLALKAFSMWSVFPLIRE---YLDGTTASSLF---EArlGREefGGEVH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 103 FHGNNKTKHEIRYALENNiGYFVIDSLEEIELI-DRYANDTVQVVLRVNPGVEAHTHEFIQTGQEDSKFGLSIQyGLAKK 181
Cdd:cd06829 73 TYSPAYRDDEIDEILRLA-DHIIFNSLSQLERFkDRAKAAGISVGLRINPEYSEVETDLYDPCAPGSRLGVTLD-ELEEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 182 AIDKVQqskhlklkGVHCHIGSQiEGTEAFIETAKIVL----RWLKeqgiQVELLNLGGGFGIKyvegDESFPIESGIKD 257
Cdd:cd06829 151 DLDGIE--------GLHFHTLCE-QDFDALERTLEAVEerfgEYLP----QLKWLNLGGGHHIT----RPDYDVDRLIAL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 258 ITDaIKSEIKVlgidapEIGIEPGRSIVGEAGvtlYEVGTIKEIpeinkyvsIDGGMsdhiRTALYDAK----------- 326
Cdd:cd06829 214 IKR-FKEKYGV------EVYLEPGEAVALNTG---YLVATVLDI--------VENGM----PIAILDASatahmpdvlem 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1332406779 327 -YQ--ALLVNRNEEADDSVTIAGKLCESGDiIIKDAKLPSSVKRGDYLAILSTGayHYSMASN--YNQMQKPSV 395
Cdd:cd06829 272 pYRppIRGAGEPGEGAHTYRLGGNSCLAGD-VIGDYSFDEPLQVGDRLVFEDMA--HYTMVKTntFNGVRLPSI 342
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
123-285 |
1.80e-08 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 56.28 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 123 YFVIDSLEEIELIDRYANDtvqvvLRVNP--GVEA--HTH---EFIQTGQEDSKFGLSIQYGLakKAIDKVQQSKHL-KL 194
Cdd:PRK05354 174 FIVIEKLSELELILEEAKE-----LGVKPrlGVRArlASQgsgKWQSSGGEKSKFGLSATEVL--EAVERLREAGLLdCL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 195 KGVHCHIGSQI-----------EGTEAFIEtakivlrwLKEQGIQVELLNLGGGFGIKYvEGDESFPIES---GIK---- 256
Cdd:PRK05354 247 QLLHFHLGSQIanirdiktavrEAARFYVE--------LRKLGAPIQYLDVGGGLGVDY-DGTRSQSDSSvnySLQeyan 317
|
170 180
....*....|....*....|....*....
gi 1332406779 257 DITDAIKSEIKVLGIDAPEIGIEPGRSIV 285
Cdd:PRK05354 318 DVVYTLKEICEEHGVPHPTIISESGRALT 346
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
123-285 |
6.06e-07 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 51.63 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 123 YFVIDSLEEIELIDRYANDtvqvvLRVNP--GVEA--------HTHEfiqTGQEDSKFGLSIQYGLakKAIDKVQQSKHL 192
Cdd:COG1166 170 IIVIEKLSELELILEEAKE-----LGVKPliGVRVklaskgsgKWQN---SGGERSKFGLSASEIL--EVVERLKEAGML 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 193 K-LKGVHCHIGSQI-----------EGTEAFIEtakivlrwLKEQGIQVELLNLGGGFGIKYvEGDES-FP------IES 253
Cdd:COG1166 240 DcLQLLHFHLGSQIpnirdikravrEAARFYAE--------LRKLGAPIEYLDVGGGLGVDY-DGSRSnSDssmnysLQE 310
|
170 180 190
....*....|....*....|....*....|..
gi 1332406779 254 GIKDITDAIKSEIKVLGIDAPEIGIEPGRSIV 285
Cdd:COG1166 311 YANDVVYAIKEVCDEAGVPHPTIISESGRALT 342
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
84-398 |
2.14e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor; Antizyme inhibitor (AZI) is homologous to the fold type III PLP-dependent enzyme ODC but does not retain any decarboxylase activity. Like ODC, AZI is presumed to exist as a homodimer. Antizyme is a regulatory protein that binds directly to the ODC monomer to block its active site, leading to its degradation by the 26S proteasome. AZI binds to Antizyme with a higher affinity than ODC, preventing the formation of the Antizyme-ODC complex. Thus, AZI blocks the ability of Antizyme to promote ODC degradation, which leads to increased ODC enzymatic activity and polyamine levels. AZI also prevents the degradation of other proteins regulated by Antizyme, such as cyclin D1.
Pssm-ID: 143504 Cd Length: 394 Bit Score: 40.22 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 84 SEGELYTALEAGFEPSRIHFHGNNKTKHEIRYALENNIGYFVIDSLEEIELIDRyANDTVQVVLRVnpGVEAhthefiQT 163
Cdd:cd06831 66 SKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIAR-NHPNAKLLLHI--ATED------NI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 164 GQEDS--KFGLSIqyglaKKAIDKVQQSKHLKLK--GVHCHIGSQIEGTEAFIET---AKIVLRWLKEQGIQVELLNLGG 236
Cdd:cd06831 137 GGEEMnmKFGTTL-----KNCRHLLECAKELDVQivGVKFHVSSSCKEYQTYVHAlsdARCVFDMAEEFGFKMNMLDIGG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 237 GFG--------IKYVEG---DESFPIESGIKDITdaikseikvlgidapeigiEPGRSIVGEAgVTLYEVGTIKEIPEIN 305
Cdd:cd06831 212 GFTgseiqleeVNHVIRpllDVYFPEGSGIQIIA-------------------EPGSYYVSSA-FTLAVNVIAKKAVEND 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 306 KYVSIDGGMSDHIRTALY---DAKYQALL------------VNRNEEADDSV---TIAGKLCESGDIIIKDAKLPSsVKR 367
Cdd:cd06831 272 KHLSSVEKNGSDEPAFVYymnDGVYGSFAsklseklnttpeVHKKYKEDEPLftsSLWGPSCDELDQIVESCLLPE-LNV 350
|
330 340 350
....*....|....*....|....*....|.
gi 1332406779 368 GDYLAILSTGAYHYSMASNYNQMQKPSVFFL 398
Cdd:cd06831 351 GDWLIFDNMGAGSLHEPSTFNDFQRPAIYYM 381
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
112-240 |
4.96e-03 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 38.36 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406779 112 EIRYALENNIgYFVIDSLEEIELIDRYA---NDTVQVVLRVNpgveahthefiqTGqeDSKFGLSIQygLAKKAIDKVQQ 188
Cdd:pfam01168 81 ELALAAEYDL-TPTVDSLEQLEALAAAArrlGKPLRVHLKID------------TG--MGRLGFRPE--EALALLARLAA 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1332406779 189 SKHLKLKGVHCHIGS----QIEGTEAFIETAKIVLRWLKEQGIQVELLNLGGGFGI 240
Cdd:pfam01168 144 LPGLRLEGLMTHFACadepDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAI 199
|
|
| |
