|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
4-411 |
3.96e-141 |
|
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: 408.77 E-value: 3.96e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 4 KTTPFTKEQLEMIIAQYPTPFHIYDAKGIMDNMRSFLDAFSWaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELI 83
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPG-SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 84 LSEKVGITGDDIMFSSNDTPYEEYKKAMDLGA-IINLDDITHIAYLEQHGE---LPDRFCFRYNPGSLKEGGNTIIGLPE 159
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELAAelgKRAPVGLRVNPGVDAGTHEYISTGGK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 160 EAKYGMTEAQIMEAINYLK-GKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEqTGVEVSFIDLGGGIGVAYKP 238
Cdd:COG0019 167 DSKFGIPLEDALEAYRRAAaLPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRE-LGIDLEWLDLGGGLGIPYTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 239 EQTPVDYKVLSAGVKAAYDRLITgtghSPIQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLMRPALYGS 317
Cdd:COG0019 246 GDEPPDLEELAAAIKEALEELCG----LGPELILEPGRALVGNAGVLLTRVLDVKENGgRRFVIVDAGMNDLMRPALYGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 318 YHHITVMGKENEPANMTYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLLhEDGSVT 397
Cdd:COG0019 322 YHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLV-DDGEAR 400
|
410
....*....|....
gi 1547461023 398 QIRRAETLDDYFAT 411
Cdd:COG0019 401 LIRRRETYEDLLAS 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
20-390 |
4.12e-138 |
|
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: 399.55 E-value: 4.12e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 20 YPTPFHIYDAKGIMDNMRSFLDAFSWaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSS 99
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSG-PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 100 NDTPYEEYKKAMDLG-AIINLDDITHIAYLEQ---HGELPDRFCFRYNPGSLKEGGNTIIGLPEEAKYGMTEAQIMEAIN 175
Cdd:cd06828 80 NGKSDEELELALELGiLRINVDSLSELERLGEiapELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 176 YLK-GKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQtGVEVSFIDLGGGIGVAYKPEQTPVDYKVLSAGVKA 254
Cdd:cd06828 160 RAKeLPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELREL-GIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 255 AYDRLITGtgHSPIQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLMRPALYGSYHHITVMGKENEPANM 333
Cdd:cd06828 239 ALKELCEG--GPDLKLIIEPGRYIVANAGVLLTRVGYVKETGgKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1547461023 334 TYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLL 390
Cdd:cd06828 317 KVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
18-410 |
9.76e-84 |
|
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: 262.23 E-value: 9.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 18 AQYPTPFHIYDAKGIMDNMRSFLDAFSWAPgfKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMF 97
Cdd:TIGR01048 21 QEFGTPLYVYDEDTIRRRFRAYKEAFGGRS--LVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 98 SSNDTPYEEYKKAMDLGAIINLDDITHIAYLEQ-HGEL--PDRFCFRYNPG-SLKEGGNTIIGLpEEAKYGMTEAQIMEA 173
Cdd:TIGR01048 99 SGNGKSRAELERALELGICINVDSFSELERLNEiAPELgkKARISLRVNPGvDAKTHPYISTGL-KDSKFGIDVEEALEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 174 INY-LKGKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEqtGVEVSFIDLGGGIGVAYKPEQTPVDYKVLSAGV 252
Cdd:TIGR01048 178 YLYaLQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE--GIDLEFLDLGGGLGIPYTPEEEPPDLSEYAQAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 253 KAAYDRlITGTGHSPiQLAYECGRMVTGPYGYLVATAIHKKDI-YKHYIGLDACMSNLMRPALYGSYHHITVMGKENEPA 331
Cdd:TIGR01048 256 LNALEG-YADLGLDP-KLILEPGRSIVANAGVLLTRVGFVKETgSRNFVIVDAGMNDLIRPALYGAYHHIIVLNRTNDAP 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1547461023 332 NMTYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLLHEdGSVTQIRRAETLDDYFA 410
Cdd:TIGR01048 334 TEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDG-GQARLIRRRETYEDLWA 411
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
24-369 |
3.00e-69 |
|
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: 222.36 E-value: 3.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 24 FHIYDAKGIMDNMRSFLDAFswAPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSSNDTP 103
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAAL--PPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 104 YEEYKKAMDLG-AIINLDDITHIAYLEQ-HGELPDRFCFRYNPGSLKEGGNTIIGLpEEAKYGMTEAQIMEAINYLKGKG 181
Cdd:pfam00278 79 DSEIRYALEAGvLCFNVDSEDELEKIAKlAPELVARVALRINPDVDAGTHKISTGG-LSSKFGIDLEDAPELLALAKELG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 182 ITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQtGVEVSFIDLGGGIGVAYKPEQTPvDYKVLSAGVKAAYDRLit 261
Cdd:pfam00278 158 LNVVGVHFHIGSQITDLEPFVEALQRARELFDRLREL-GIDLKLLDIGGGFGIPYRDEPPP-DFEEYAAAIREALDEY-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 262 gtGHSPIQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLMRPALYGSYHHITVMGKENEPANMTYDVTGS 340
Cdd:pfam00278 234 --FPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGgKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETYDVVGP 311
|
330 340
....*....|....*....|....*....
gi 1547461023 341 LCENNDKFAIDRQLPKIDMGDRIVIHDAG 369
Cdd:pfam00278 312 TCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
52-380 |
1.04e-58 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 205.70 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 52 YFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKV--GITGDDIMFSSNDTPYEEYKKAMDLGAIINLDDITHiayLE 129
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTVTLDNVEP---LR 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 130 QHGEL-PDRFCF-RYNPGS-------LKEGGNtiiglpeEAKYGMTEAQIMEAINYLKGKGITNFGLHTMVVSNELDVDG 200
Cdd:PRK08961 607 NWPELfRGREVWlRIDPGHgdghhekVRTGGK-------ESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEH 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 201 LVGTAELMFNLALRVKEqtgveVSFIDLGGGIGVAYKPEQTPVDYKVLSAG---VKAAYDRLitgtghspiQLAYECGRM 277
Cdd:PRK08961 680 WRRMADELASFARRFPD-----VRTIDLGGGLGIPESAGDEPFDLDALDAGlaeVKAQHPGY---------QLWIEPGRY 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 278 VTGPYGYLVATA---IHKKDIYkhYIGLDACMSNLMRPALYGSYHHITVMGKENEPANMTYDVTGSLCENNDKFAIDRQL 354
Cdd:PRK08961 746 LVAEAGVLLARVtqvKEKDGVR--RVGLETGMNSLIRPALYGAYHEIVNLSRLDEPAAGTADVVGPICESSDVLGKRRRL 823
|
330 340
....*....|....*....|....*.
gi 1547461023 355 PKIDMGDRIVIHDAGAHGHAMGFNYN 380
Cdd:PRK08961 824 PATAEGDVILIANAGAYGYSMSSTYN 849
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
4-411 |
3.96e-141 |
|
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: 408.77 E-value: 3.96e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 4 KTTPFTKEQLEMIIAQYPTPFHIYDAKGIMDNMRSFLDAFSWaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELI 83
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPG-SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 84 LSEKVGITGDDIMFSSNDTPYEEYKKAMDLGA-IINLDDITHIAYLEQHGE---LPDRFCFRYNPGSLKEGGNTIIGLPE 159
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELAAelgKRAPVGLRVNPGVDAGTHEYISTGGK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 160 EAKYGMTEAQIMEAINYLK-GKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEqTGVEVSFIDLGGGIGVAYKP 238
Cdd:COG0019 167 DSKFGIPLEDALEAYRRAAaLPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRE-LGIDLEWLDLGGGLGIPYTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 239 EQTPVDYKVLSAGVKAAYDRLITgtghSPIQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLMRPALYGS 317
Cdd:COG0019 246 GDEPPDLEELAAAIKEALEELCG----LGPELILEPGRALVGNAGVLLTRVLDVKENGgRRFVIVDAGMNDLMRPALYGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 318 YHHITVMGKENEPANMTYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLLhEDGSVT 397
Cdd:COG0019 322 YHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLV-DDGEAR 400
|
410
....*....|....
gi 1547461023 398 QIRRAETLDDYFAT 411
Cdd:COG0019 401 LIRRRETYEDLLAS 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
20-390 |
4.12e-138 |
|
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: 399.55 E-value: 4.12e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 20 YPTPFHIYDAKGIMDNMRSFLDAFSWaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSS 99
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSG-PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 100 NDTPYEEYKKAMDLG-AIINLDDITHIAYLEQ---HGELPDRFCFRYNPGSLKEGGNTIIGLPEEAKYGMTEAQIMEAIN 175
Cdd:cd06828 80 NGKSDEELELALELGiLRINVDSLSELERLGEiapELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 176 YLK-GKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQtGVEVSFIDLGGGIGVAYKPEQTPVDYKVLSAGVKA 254
Cdd:cd06828 160 RAKeLPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELREL-GIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 255 AYDRLITGtgHSPIQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLMRPALYGSYHHITVMGKENEPANM 333
Cdd:cd06828 239 ALKELCEG--GPDLKLIIEPGRYIVANAGVLLTRVGYVKETGgKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1547461023 334 TYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLL 390
Cdd:cd06828 317 KVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
18-410 |
9.76e-84 |
|
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: 262.23 E-value: 9.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 18 AQYPTPFHIYDAKGIMDNMRSFLDAFSWAPgfKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMF 97
Cdd:TIGR01048 21 QEFGTPLYVYDEDTIRRRFRAYKEAFGGRS--LVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 98 SSNDTPYEEYKKAMDLGAIINLDDITHIAYLEQ-HGEL--PDRFCFRYNPG-SLKEGGNTIIGLpEEAKYGMTEAQIMEA 173
Cdd:TIGR01048 99 SGNGKSRAELERALELGICINVDSFSELERLNEiAPELgkKARISLRVNPGvDAKTHPYISTGL-KDSKFGIDVEEALEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 174 INY-LKGKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEqtGVEVSFIDLGGGIGVAYKPEQTPVDYKVLSAGV 252
Cdd:TIGR01048 178 YLYaLQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE--GIDLEFLDLGGGLGIPYTPEEEPPDLSEYAQAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 253 KAAYDRlITGTGHSPiQLAYECGRMVTGPYGYLVATAIHKKDI-YKHYIGLDACMSNLMRPALYGSYHHITVMGKENEPA 331
Cdd:TIGR01048 256 LNALEG-YADLGLDP-KLILEPGRSIVANAGVLLTRVGFVKETgSRNFVIVDAGMNDLIRPALYGAYHHIIVLNRTNDAP 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1547461023 332 NMTYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLLHEdGSVTQIRRAETLDDYFA 410
Cdd:TIGR01048 334 TEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDG-GQARLIRRRETYEDLWA 411
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
24-369 |
3.00e-69 |
|
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: 222.36 E-value: 3.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 24 FHIYDAKGIMDNMRSFLDAFswAPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSSNDTP 103
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAAL--PPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 104 YEEYKKAMDLG-AIINLDDITHIAYLEQ-HGELPDRFCFRYNPGSLKEGGNTIIGLpEEAKYGMTEAQIMEAINYLKGKG 181
Cdd:pfam00278 79 DSEIRYALEAGvLCFNVDSEDELEKIAKlAPELVARVALRINPDVDAGTHKISTGG-LSSKFGIDLEDAPELLALAKELG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 182 ITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQtGVEVSFIDLGGGIGVAYKPEQTPvDYKVLSAGVKAAYDRLit 261
Cdd:pfam00278 158 LNVVGVHFHIGSQITDLEPFVEALQRARELFDRLREL-GIDLKLLDIGGGFGIPYRDEPPP-DFEEYAAAIREALDEY-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 262 gtGHSPIQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLMRPALYGSYHHITVMGKENEPANMTYDVTGS 340
Cdd:pfam00278 234 --FPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGgKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETYDVVGP 311
|
330 340
....*....|....*....|....*....
gi 1547461023 341 LCENNDKFAIDRQLPKIDMGDRIVIHDAG 369
Cdd:pfam00278 312 TCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
22-390 |
4.74e-61 |
|
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: 201.76 E-value: 4.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 22 TPFHIYDAKGIMDNMRSFLDAFswAPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSSND 101
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEAL--PSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 102 TPYEEYKKAMDLG-AIINLDDITHIAYLEQ-HGEL--PDRFCFRYNPGSLkEGGNTIIGLPEEAKYGMTEAQIMEAINYL 177
Cdd:cd06810 79 KSVSEIEAALASGvDHIVVDSLDELERLNElAKKLgpKARILLRVNPDVS-AGTHKISTGGLKSKFGLSLSEARAALERA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 178 KGKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQtGVEVSFIDLGGGIGVAYKPEqtPVDYKVLSAGVKAAYD 257
Cdd:cd06810 158 KELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEM-GFPLEMLDLGGGLGIPYDEQ--PLDFEEYAALINPLLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 258 RliTGTGHSPIQLAYECGRMVTGPYGYLVATAIHKKDIYK-HYIGLDACMSNLMRPAL-YGSYHHITVMGKENEPANM-T 334
Cdd:cd06810 235 K--YFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGrFFAVVDGGMNHSFRPALaYDAYHPITPLKAPGPDEPLvP 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1547461023 335 YDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLL 390
Cdd:cd06810 313 ATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
52-380 |
1.04e-58 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 205.70 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 52 YFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKV--GITGDDIMFSSNDTPYEEYKKAMDLGAIINLDDITHiayLE 129
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTVTLDNVEP---LR 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 130 QHGEL-PDRFCF-RYNPGS-------LKEGGNtiiglpeEAKYGMTEAQIMEAINYLKGKGITNFGLHTMVVSNELDVDG 200
Cdd:PRK08961 607 NWPELfRGREVWlRIDPGHgdghhekVRTGGK-------ESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEH 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 201 LVGTAELMFNLALRVKEqtgveVSFIDLGGGIGVAYKPEQTPVDYKVLSAG---VKAAYDRLitgtghspiQLAYECGRM 277
Cdd:PRK08961 680 WRRMADELASFARRFPD-----VRTIDLGGGLGIPESAGDEPFDLDALDAGlaeVKAQHPGY---------QLWIEPGRY 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 278 VTGPYGYLVATA---IHKKDIYkhYIGLDACMSNLMRPALYGSYHHITVMGKENEPANMTYDVTGSLCENNDKFAIDRQL 354
Cdd:PRK08961 746 LVAEAGVLLARVtqvKEKDGVR--RVGLETGMNSLIRPALYGAYHEIVNLSRLDEPAAGTADVVGPICESSDVLGKRRRL 823
|
330 340
....*....|....*....|....*.
gi 1547461023 355 PKIDMGDRIVIHDAGAHGHAMGFNYN 380
Cdd:PRK08961 824 PATAEGDVILIANAGAYGYSMSSTYN 849
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
52-390 |
2.70e-55 |
|
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: 186.87 E-value: 2.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 52 YFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKV--GITGDDIMFSSNDTPYEEYKKAMDLGAIINLDDITHiayLE 129
Cdd:cd06840 39 FYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVNVTVDNLHP---LR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 130 QHGEL-PDRFCF-RYNPGS-------LKEGGNtiiglpeEAKYGMTEAQIMEAINYLKGKGITNFGLHTMVVSNELDVDG 200
Cdd:cd06840 116 EWPELfRGREVIlRIDPGQgeghhkhVRTGGP-------ESKFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDH 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 201 LVGTAELMFNLALRVKEqtgveVSFIDLGGGIGVAYKPEQTPVDYKVLSAGVKAAydrlitGTGHSPIQLAYECGRMVTG 280
Cdd:cd06840 189 WARHGDYLASLARHFPA-----VRILNVGGGLGIPEAPGGRPIDLDALDAALAAA------KAAHPQYQLWMEPGRFIVA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 281 PYGYLVA--TAIHKKDIYKhYIGLDACMSNLMRPALYGSYHHITVMGKENEPANMTYDVTGSLCENNDKFAIDRQLPKID 358
Cdd:cd06840 258 ESGVLLArvTQIKHKDGVR-FVGLETGMNSLIRPALYGAYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRLLPETE 336
|
330 340 350
....*....|....*....|....*....|..
gi 1547461023 359 MGDRIVIHDAGAHGHAMGFNYNGKLRSAELLL 390
Cdd:cd06840 337 EGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
22-413 |
1.70e-47 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 167.66 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 22 TPFHIYDAKGIMDNMRSFLDAFSWAPGFKQYfAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSSND 101
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALEGLRSIIGY-AIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 102 TPYEEYKKAMDLGAIINLD---DITHIAYLEQHGELPDRFCFRYNPGSLKEGGNTIIGLPEEAKYGMTEAQIMEAINYLK 178
Cdd:PLN02537 97 KLLEDLVLAAQEGVFVNVDsefDLENIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 179 G--KGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQtGVEVSFIDLGGGIGVAYKPE----QTPVDY------K 246
Cdd:PLN02537 177 AhpNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQ-GFELSYLNIGGGLGIDYYHAgavlPTPRDLidtvreL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 247 VLSAGVKaaydrLITGTGHSPIQLAYECGRMVTGPygylvataihKKDIYKHYIGLDACMSNLMRPALYGSYHHITVMGK 326
Cdd:PLN02537 256 VLSRDLT-----LIIEPGRSLIANTCCFVNRVTGV----------KTNGTKNFIVIDGSMAELIRPSLYDAYQHIELVSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 327 ENEPANM-TYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSAELLLHEDGSVTQIRRAETL 405
Cdd:PLN02537 321 PPPDAEVsTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITKIRHAETF 400
|
....*...
gi 1547461023 406 DDYFATLD 413
Cdd:PLN02537 401 DDHLRFFE 408
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
16-373 |
1.74e-42 |
|
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: 153.52 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 16 IIAQYPTPFHIYDAKGIM---DNMRSFLdafswAPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITG 92
Cdd:cd06839 1 LADAYGTPFYVYDRDRVReryAALRAAL-----PPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 93 DDIMFSSNDTPYEEYKKAMDLGAI-INLD---DITHIAYL-EQHGELPdRFCFRYNPG-SLKEGGNTIIGLPeeAKYGMT 166
Cdd:cd06839 76 EKILFAGPGKSDAELRRAIEAGIGtINVEsleELERIDALaEEHGVVA-RVALRINPDfELKGSGMKMGGGP--SQFGID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 167 EAQIMEAINYLKGKGITNF-GLHTMVVSNELDVDGLVGTAELMFNLALRVKEQTGVEVSFIDLGGGIGVAYKPEQTPVDY 245
Cdd:cd06839 153 VEELPAVLARIAALPNLRFvGLHIYPGTQILDADALIEAFRQTLALALRLAEELGLPLEFLDLGGGFGIPYFPGETPLDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 246 KVLSAGVKAAYDRLitGTGHSPIQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDAcmsnlmrpalyGSYHH---- 320
Cdd:cd06839 233 EALGAALAALLAEL--GDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVSRgETFLVTDG-----------GMHHHlaas 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1547461023 321 ------------ITVMGKENEPANMTYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGH 373
Cdd:cd06839 300 gnfgqvlrrnypLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGL 364
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
16-370 |
2.25e-40 |
|
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: 147.79 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 16 IIAQYPTPFHIYDAKGIMDNMRSFLDAF-SWAPGFKQYFAVKATPNPYIMKMMKEIGIGAD-CSSMaELILSEKVGITGD 93
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFkKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEvVSAM-EYELALKLGVPGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 94 DIMFSSNDTPYEEYKKAMDLGAIINLDDITHIAYLEQHGELPDRfcfRYNPG---SLKEGGNTIiglpeeAKYGMTEAQI 170
Cdd:cd06841 80 RIIFNGPYKSKEELEKALEEGALINIDSFDELERILEIAKELGR---VAKVGirlNMNYGNNVW------SRFGFDIEEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 171 MEAINYLK----GKGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKeqtGVEVSFIDLGGGIG------VAYKPEQ 240
Cdd:cd06841 151 GEALAALKkiqeSKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRLF---GLELEYLDLGGGFPaktplsLAYPQED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 241 TPVDYKVLSAGVKAAYDRLITGTGHSPIqLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLmrPALYGSYH 319
Cdd:cd06841 228 TVPDPEDYAEAIASTLKEYYANKENKPK-LILEPGRALVDDAGYLLGRVVAVKNRYgRNIAVTDAGINNI--PTIFWYHH 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1547461023 320 HITVM-GKENEPANMTYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGA 370
Cdd:cd06841 305 PILVLrPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGA 356
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
26-386 |
6.62e-38 |
|
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: 140.99 E-value: 6.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 26 IYDAKGIMDNMRSFLDAFSwaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSSNDTPYE 105
Cdd:cd06836 7 LYDLDGFRALVARLTAAFP--APVLHTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 106 EYKKAMDLGAIINLDDITHIAYLE----QHGELPDRFCFRYNPGSlkeGGNTIIGLP---EEAKYG--MTEAQIMEAIN- 175
Cdd:cd06836 85 ELREALELGVAINIDNFQELERIDalvaEFKEASSRIGLRVNPQV---GAGKIGALStatATSKFGvaLEDGARDEIIDa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 176 YLKGKGITnfGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQTG-VEVSFIDLGGGIGVAYKPEQTPVDYKVLSAGVKA 254
Cdd:cd06836 162 FARRPWLN--GLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRVGrRQITRIDIGGGLPVNFESEDITPTFADYAAALKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 255 AYDRLITGTghspIQLAYECGRMVTGPYGYLVATAIHKKDIYKHYI-----GLDACMSNLMRPALYgsYHHITVMGKENE 329
Cdd:cd06836 240 AVPELFDGR----YQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIaithaGAQVATRTAYAPDDW--PLRVTVFDANGE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 330 PAN---MTYDVTGSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHGHAMGFNYNGKLRSA 386
Cdd:cd06836 314 PKTgpeVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
21-372 |
2.22e-22 |
|
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: 97.74 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 21 PTPFHIYDAKGI---MDNMRSFLdafswAPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGiTGDDIMF 97
Cdd:cd06843 1 PLCAYVYDLAALrahARALRASL-----PPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAV-PDAPLIF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 98 SSNDTPYEEYKKAMDLG-AIINLDDITHIAYL----EQHGELPDRFcFRYNP-------GSLKEGGntiiglpEEAKYGM 165
Cdd:cd06843 75 GGPGKTDSELAQALAQGvERIHVESELELRRLnavaRRAGRTAPVL-LRVNLalpdlpsSTLTMGG-------QPTPFGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 166 TEAQIMEAINYLKG-KGITNFGLHTMVVSNELDVDGLVGTAELMFNLALRVKEQTGVEVSFIDLGGGIGVAYKPEQTPVD 244
Cdd:cd06843 147 DEADLPDALELLRDlPNIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEHGLDLDVVNVGGGIGVNYADPEEQFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 245 YKVLSAGVkaayDRLITGTGHSPiQLAYECGRMVTGPYGYLVATAIHKKDIY-KHYIGLDACMSNLMRPALYGSYHHITV 323
Cdd:cd06843 227 WAGFCEGL----DQLLAEYEPGL-TLRFECGRYISAYCGYYVTEVLDLKRSHgEWFAVLRGGTHHFRLPAAWGHNHPFSV 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1547461023 324 MGKEN------EPANMTYDVT--GSLCENNDKFAIDRQLPKIDMGDRIVIHDAGAHG 372
Cdd:cd06843 302 LPVEEwpypwpRPSVRDTPVTlvGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYG 358
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
22-381 |
2.36e-17 |
|
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: 82.93 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 22 TPFHIYDAKGIMDNMRSFLDAFswaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELilsEKV---GITGDDIMFS 98
Cdd:cd00622 2 TPFLVVDLGDVVRKYRRWKKAL---PRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEI---ELVlglGVSPERIIFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 99 SNDTPYEEYKKAMDLG----AIINLDDITHIAyleqhgelpdrfcfRYNPGS------LKEGGNTIIGLpeEAKYGMTEA 168
Cdd:cd00622 76 NPCKSISDIRYAAELGvrlfTFDSEDELEKIA--------------KHAPGAklllriATDDSGALCPL--SRKFGADPE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 169 QIMEAINYLKGKGITNFGLHTMVVSNELD----VDGLVGTAELmFNLAlrvkEQTGVEVSFIDLGGGIGVAYKPEQTPVD 244
Cdd:cd00622 140 EARELLRRAKELGLNVVGVSFHVGSQCTDpsayVDAIADAREV-FDEA----AELGFKLKLLDIGGGFPGSYDGVVPSFE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 245 ykVLSAGVKAAYDRLItgtGHSPIQLAYECGRMVTGPYGYLVATAIHKKDIYKH------YI--GLDACMSNLMRPALYG 316
Cdd:cd00622 215 --EIAAVINRALDEYF---PDEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDdrerwyYLndGVYGSFNEILFDHIRY 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1547461023 317 SYHHITVMGKENEPANMTydVTGSLCENNDKFAIDRQLPK-IDMGDRIVIHDAGAHGHAMGFNYNG 381
Cdd:cd00622 290 PPRVLKDGGRDGELYPSS--LWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNG 353
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
36-280 |
3.10e-15 |
|
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: 74.62 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 36 MRSFLDAFswaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSSNDTPYEEYKKAMDLGA 115
Cdd:pfam02784 8 HRRWKKAL---PRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 116 -IINLDDITHIAYLEQHGELPDRFcFRYNPGSLKEGGntiiglPEEAKYGM----TEAQIMEAINYLkgkGITNFGLHTM 190
Cdd:pfam02784 85 gCVTVDNVDELEKLARLAPEARVL-LRIKPDDSAATC------PLSSKFGAdldeDVEALLEAAKLL---NLQVVGVSFH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 191 VVSNELDVDGLVGTAELMFNLALRVKEqTGVEVSFIDLGGGIGVAYKPEQTPVDYKVLSAGVKAAYDRLItgTGHSPIQL 270
Cdd:pfam02784 155 VGSGCTDAEAFVLALEDARGVFDQGAE-LGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINEALEEYF--PGDPGVTI 231
|
250
....*....|
gi 1547461023 271 AYECGRMVTG 280
Cdd:pfam02784 232 IAEPGRYFVA 241
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
32-240 |
6.17e-13 |
|
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: 67.34 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 32 IMDNMRSFLDAFSwaPGFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGITGDDIMFSSNDTPYEEYKKAM 111
Cdd:cd06808 1 IRHNYRRLREAAP--AGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 112 DLGAI-INLDDITHIAYLEQ-HGELPD--RFCFRYNPGSLKEggntiiglpeeaKYGMTEAQIMEAINYLKG-KGITNFG 186
Cdd:cd06808 79 EQGVIvVTVDSLEELEKLEEaALKAGPpaRVLLRIDTGDENG------------KFGVRPEELKALLERAKElPHLRLVG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1547461023 187 LHTMVVSNELDVDGLVgTAELMFNLALRVKEQTGVEVSFIDLGGGIGVAYKPEQ 240
Cdd:cd06808 147 LHTHFGSADEDYSPFV-EALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQEL 199
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
13-236 |
4.17e-10 |
|
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: 61.12 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 13 LEMIIAQYPTPFHIYDAKGIMDNMRSFLDAFSWAP-GFKQYFAVKATPNPYIMKMMKEIGIGADCSSMAELILSEKVGIT 91
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDRHGvDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1547461023 92 GDDIMFSSNDTPYEEYKKAMDLGAIINLDDI----THIAYLEQHGELPDRFCFRYNPGSLKeggntiiglpEEAKYGMTE 167
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGATIAVDSLdeldRLLALARGYTTGPARVLLRLSPFPAS----------LPSRFGMPA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1547461023 168 AQIMEAINYLK--GKGITNFGLHTmvvsnELDVDGLVGTAELMFNLALRVKE--QTGVEVSFIDLGGGIGVAY 236
Cdd:cd06842 151 AEVRTALERLAqlRERVRLVGFHF-----HLDGYSAAQRVAALQECLPLIDRarALGLAPRFIDIGGGFPVSY 218
|
|
| |
