|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
13-352 |
1.37e-123 |
|
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: 360.33 E-value: 1.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQALKQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEvlaEADGSIHLTTPG 92
Cdd:cd06829 1 TPCYVLDEAKLRRNLEILKRVQERSGAKILLALKAFSMWSVFPLIREYLDGTTASSLFEARLGRE---EFGGEVHTYSPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 93 LRPDEFAELSRLCSHISFNSLPQHQRLKASVSDY--SQGLRVNPKLSFADDQRYDPCRPHSKLGVDIELLRDGLPANVEG 170
Cdd:cd06829 78 YRDDEIDEILRLADHIIFNSLSQLERFKDRAKAAgiSVGLRINPEYSEVETDLYDPCAPGSRLGVTLDELEEEDLDGIEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 171 LHFHTVFACrDFRPLQQTL----EKLRPILKRnrLKWLNVGGGYlyHAIAEQQD---LAELIRDVRAEFGVDVYVEPGKG 243
Cdd:cd06829 158 LHFHTLCEQ-DFDALERTLeaveERFGEYLPQ--LKWLNLGGGH--HITRPDYDvdrLIALIKRFKEKYGVEVYLEPGEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 244 LVGNAGYLLTTVLDrFVSDGKQVLILDTSVNHH-PEVFEYQIKPRLL--EEAGGGEQSAILAGSTCLAGDVFGEYRFRRI 320
Cdd:cd06829 233 VALNTGYLVATVLD-IVENGMPIAILDASATAHmPDVLEMPYRPPIRgaGEPGEGAHTYRLGGNSCLAGDVIGDYSFDEP 311
|
330 340 350
....*....|....*....|....*....|..
gi 1914496624 321 PEVGERLVFADVGAYSLIKANRFNGYQLPDVY 352
Cdd:cd06829 312 LQVGDRLVFEDMAHYTMVKTNTFNGVRLPSIA 343
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
5-372 |
3.43e-86 |
|
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: 267.01 E-value: 3.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 5 ELKQQIPTsPALVLDEAQILANLKRLQALKQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEvlAEADG 84
Cdd:COG0019 19 ELAEEYGT-PLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALA--AGFPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 85 S-IHLTTPGLRPDEFAELSRLC-SHISFNSLPQHQRLKASVSDYSQ----GLRVNPKLSFADDQRYDPCRPHSKLGVDIE 158
Cdd:COG0019 96 ErIVFSGNGKSEEELEEALELGvGHINVDSLSELERLAELAAELGKrapvGLRVNPGVDAGTHEYISTGGKDSKFGIPLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 159 LLRDGLPA-------NVEGLHFHTVFACRDFRPLQQTLEKLRPILKRNR-----LKWLNVGGGYL--YHAIAEQQDLAEL 224
Cdd:COG0019 176 DALEAYRRaaalpglRLVGLHFHIGSQILDLEPFEEALERLLELAEELRelgidLEWLDLGGGLGipYTEGDEPPDLEEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 225 IRDVRAEF------GVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHH-PEVFE---YQIKPrLLEEAGG 294
Cdd:COG0019 256 AAAIKEALeelcglGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLmRPALYgayHPIVP-VGRPSGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 295 GEQSAILAGSTCLAGDVFGEYrfRRIPEV--GERLVFADVGAYSLIKANRFNGYQLPDVYSVNPARW-LLQKRDSYADYR 371
Cdd:COG0019 335 EAETYDVVGPLCESGDVLGKD--RSLPPLepGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGEArLIRRRETYEDLL 412
|
.
gi 1914496624 372 R 372
Cdd:COG0019 413 A 413
|
|
| nspC |
TIGR01047 |
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. ... |
10-372 |
1.88e-80 |
|
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. It is the last enzyme in norspermidine biosynthesis by an unusual pathway shown in Vibrio alginolyticus. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 273414 [Multi-domain] Cd Length: 379 Bit Score: 251.24 E-value: 1.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 10 IPTsPALVLDEAQILANLKRLQALKQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEvlaEADGSIHLT 89
Cdd:TIGR01047 1 IPT-PAFVLEEEKLRKNLEILESVQQQSGAKVLLALKGFAFWGAFPILREYLKGCTASGLWEAKLAKE---EFGKEIHVY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 90 TPGLRPDEFAELSRLCSHISFNSLPQHQRLKASV----SDYSQGLRVNPKLSFADDQRYDPCRPHSKLGVDIELLRDGLP 165
Cdd:TIGR01047 77 SPAYKEDDIPEIIPLADHIVFNSLAQWHRYRHKVqgknSAVKLGLRINPEYSEVPTDLYNPCGRFSRLGVQAKDFEEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 166 ANVEGLHFHTVfaC-RDFRPLQQTL----EKLRPILkrNRLKWLNVGGGYlyHAIAEQQDLAELIRDVRA---EFGVDVY 237
Cdd:TIGR01047 157 DGIEGLHFHTL--CeKDADALERTLevieEKFGEYL--PQMKWVNFGGGH--HITKKGYDVEKLIAVIKAfseRHGVQVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 238 VEPGKGLVGNAGYLLTTVLDrFVSDGKQVLILDTSVN-HHPEVFEYQIKPRLLE-----------EAGGGEQSAILAGST 305
Cdd:TIGR01047 231 LEPGEAIGWQTGFLVASVVD-IVENEKQIAILDVSFEaHMPDTLEMPYRPEVLGardpatreneaQDKEGEFSYLLGGNT 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914496624 306 CLAGDVFGEYRFRRIPEVGERLVFADVGAYSLIKANRFNGYQLPDVYSVNPARWL-LQKRDSYADYRR 372
Cdd:TIGR01047 310 CLAGDVMGEYAFDKPLKVGDKIVFLDMIHYTMVKNTTFNGVKLPSLGCLRAKGEFqMIRTFGYEDYKN 377
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
17-333 |
1.45e-50 |
|
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: 172.67 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 17 VLDEAQILANLKRLQALkQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADgSIHLTTPGLRPD 96
Cdd:pfam00278 3 VYDLATLRRNYRRWKAA-LPPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPE-RIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 97 EFAE-LSRLCSHISFNSLPQ-------HQRLKASVSdysqgLRVNPKLSfADDQRYDPCRPHSKLGVDIELLRDGLPA-- 166
Cdd:pfam00278 81 EIRYaLEAGVLCFNVDSEDElekiaklAPELVARVA-----LRINPDVD-AGTHKISTGGLSSKFGIDLEDAPELLALak 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 167 ----NVEGLHFHTVFACRDFRPLQQTLEKLRPILKRNR-----LKWLNVGGG----YLYHAIAEQQDLAELIRDVRAEF- 232
Cdd:pfam00278 155 elglNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRelgidLKLLDIGGGfgipYRDEPPPDFEEYAAAIREALDEYf 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 233 --GVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHH--PEVFE-YQIKPRLLEEAGGGEQSAILAGSTCL 307
Cdd:pfam00278 235 ppDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLfrPALYDaYHPIPVVKEPGEGPLETYDVVGPTCE 314
|
330 340
....*....|....*....|....*...
gi 1914496624 308 AGDVFGeyRFRRIPE--VGERLVFADVG 333
Cdd:pfam00278 315 SGDVLA--KDRELPEleVGDLLAFEDAG 340
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
13-344 |
1.06e-13 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 72.81 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQALKQASgcKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADGSIHLTTPG 92
Cdd:PRK08961 503 SPCYVYHLPTVRARARALAALAAVD--QRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELFPELSPERVLFTPN 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 93 LRP-DEFAELSRLCSHISFNSLPQHQRLKASVSDYSQGLRVNPKLSFADDQRYDPCRPHSKLGV---DIELLRD---GLP 165
Cdd:PRK08961 581 FAPrAEYEAAFALGVTVTLDNVEPLRNWPELFRGREVWLRIDPGHGDGHHEKVRTGGKESKFGLsqtRIDEFVDlakTLG 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 166 ANVEGLHFHTVFACRDFRPLQQTLEKLRPILKR-NRLKWLNVGGGY--LYHAIAEQQDL---AELIRDVRAEF-GVDVYV 238
Cdd:PRK08961 661 ITVVGLHAHLGSGIETGEHWRRMADELASFARRfPDVRTIDLGGGLgiPESAGDEPFDLdalDAGLAEVKAQHpGYQLWI 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 239 EPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVN----------HHpevfEYQIKPRLLEEAgggEQSAILAGSTCLA 308
Cdd:PRK08961 741 EPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNslirpalygaYH----EIVNLSRLDEPA---AGTADVVGPICES 813
|
330 340 350
....*....|....*....|....*....|....*...
gi 1914496624 309 GDVFGeYRfRRIPEV--GERLVFADVGAYSLIKANRFN 344
Cdd:PRK08961 814 SDVLG-KR-RRLPATaeGDVILIANAGAYGYSMSSTYN 849
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
13-352 |
1.37e-123 |
|
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: 360.33 E-value: 1.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQALKQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEvlaEADGSIHLTTPG 92
Cdd:cd06829 1 TPCYVLDEAKLRRNLEILKRVQERSGAKILLALKAFSMWSVFPLIREYLDGTTASSLFEARLGRE---EFGGEVHTYSPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 93 LRPDEFAELSRLCSHISFNSLPQHQRLKASVSDY--SQGLRVNPKLSFADDQRYDPCRPHSKLGVDIELLRDGLPANVEG 170
Cdd:cd06829 78 YRDDEIDEILRLADHIIFNSLSQLERFKDRAKAAgiSVGLRINPEYSEVETDLYDPCAPGSRLGVTLDELEEEDLDGIEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 171 LHFHTVFACrDFRPLQQTL----EKLRPILKRnrLKWLNVGGGYlyHAIAEQQD---LAELIRDVRAEFGVDVYVEPGKG 243
Cdd:cd06829 158 LHFHTLCEQ-DFDALERTLeaveERFGEYLPQ--LKWLNLGGGH--HITRPDYDvdrLIALIKRFKEKYGVEVYLEPGEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 244 LVGNAGYLLTTVLDrFVSDGKQVLILDTSVNHH-PEVFEYQIKPRLL--EEAGGGEQSAILAGSTCLAGDVFGEYRFRRI 320
Cdd:cd06829 233 VALNTGYLVATVLD-IVENGMPIAILDASATAHmPDVLEMPYRPPIRgaGEPGEGAHTYRLGGNSCLAGDVIGDYSFDEP 311
|
330 340 350
....*....|....*....|....*....|..
gi 1914496624 321 PEVGERLVFADVGAYSLIKANRFNGYQLPDVY 352
Cdd:cd06829 312 LQVGDRLVFEDMAHYTMVKTNTFNGVRLPSIA 343
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
5-372 |
3.43e-86 |
|
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: 267.01 E-value: 3.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 5 ELKQQIPTsPALVLDEAQILANLKRLQALKQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEvlAEADG 84
Cdd:COG0019 19 ELAEEYGT-PLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALA--AGFPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 85 S-IHLTTPGLRPDEFAELSRLC-SHISFNSLPQHQRLKASVSDYSQ----GLRVNPKLSFADDQRYDPCRPHSKLGVDIE 158
Cdd:COG0019 96 ErIVFSGNGKSEEELEEALELGvGHINVDSLSELERLAELAAELGKrapvGLRVNPGVDAGTHEYISTGGKDSKFGIPLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 159 LLRDGLPA-------NVEGLHFHTVFACRDFRPLQQTLEKLRPILKRNR-----LKWLNVGGGYL--YHAIAEQQDLAEL 224
Cdd:COG0019 176 DALEAYRRaaalpglRLVGLHFHIGSQILDLEPFEEALERLLELAEELRelgidLEWLDLGGGLGipYTEGDEPPDLEEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 225 IRDVRAEF------GVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHH-PEVFE---YQIKPrLLEEAGG 294
Cdd:COG0019 256 AAAIKEALeelcglGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLmRPALYgayHPIVP-VGRPSGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 295 GEQSAILAGSTCLAGDVFGEYrfRRIPEV--GERLVFADVGAYSLIKANRFNGYQLPDVYSVNPARW-LLQKRDSYADYR 371
Cdd:COG0019 335 EAETYDVVGPLCESGDVLGKD--RSLPPLepGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGEArLIRRRETYEDLL 412
|
.
gi 1914496624 372 R 372
Cdd:COG0019 413 A 413
|
|
| nspC |
TIGR01047 |
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. ... |
10-372 |
1.88e-80 |
|
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. It is the last enzyme in norspermidine biosynthesis by an unusual pathway shown in Vibrio alginolyticus. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 273414 [Multi-domain] Cd Length: 379 Bit Score: 251.24 E-value: 1.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 10 IPTsPALVLDEAQILANLKRLQALKQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEvlaEADGSIHLT 89
Cdd:TIGR01047 1 IPT-PAFVLEEEKLRKNLEILESVQQQSGAKVLLALKGFAFWGAFPILREYLKGCTASGLWEAKLAKE---EFGKEIHVY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 90 TPGLRPDEFAELSRLCSHISFNSLPQHQRLKASV----SDYSQGLRVNPKLSFADDQRYDPCRPHSKLGVDIELLRDGLP 165
Cdd:TIGR01047 77 SPAYKEDDIPEIIPLADHIVFNSLAQWHRYRHKVqgknSAVKLGLRINPEYSEVPTDLYNPCGRFSRLGVQAKDFEEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 166 ANVEGLHFHTVfaC-RDFRPLQQTL----EKLRPILkrNRLKWLNVGGGYlyHAIAEQQDLAELIRDVRA---EFGVDVY 237
Cdd:TIGR01047 157 DGIEGLHFHTL--CeKDADALERTLevieEKFGEYL--PQMKWVNFGGGH--HITKKGYDVEKLIAVIKAfseRHGVQVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 238 VEPGKGLVGNAGYLLTTVLDrFVSDGKQVLILDTSVN-HHPEVFEYQIKPRLLE-----------EAGGGEQSAILAGST 305
Cdd:TIGR01047 231 LEPGEAIGWQTGFLVASVVD-IVENEKQIAILDVSFEaHMPDTLEMPYRPEVLGardpatreneaQDKEGEFSYLLGGNT 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914496624 306 CLAGDVFGEYRFRRIPEVGERLVFADVGAYSLIKANRFNGYQLPDVYSVNPARWL-LQKRDSYADYRR 372
Cdd:TIGR01047 310 CLAGDVMGEYAFDKPLKVGDKIVFLDMIHYTMVKNTTFNGVKLPSLGCLRAKGEFqMIRTFGYEDYKN 377
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
17-333 |
1.45e-50 |
|
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: 172.67 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 17 VLDEAQILANLKRLQALkQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADgSIHLTTPGLRPD 96
Cdd:pfam00278 3 VYDLATLRRNYRRWKAA-LPPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPE-RIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 97 EFAE-LSRLCSHISFNSLPQ-------HQRLKASVSdysqgLRVNPKLSfADDQRYDPCRPHSKLGVDIELLRDGLPA-- 166
Cdd:pfam00278 81 EIRYaLEAGVLCFNVDSEDElekiaklAPELVARVA-----LRINPDVD-AGTHKISTGGLSSKFGIDLEDAPELLALak 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 167 ----NVEGLHFHTVFACRDFRPLQQTLEKLRPILKRNR-----LKWLNVGGG----YLYHAIAEQQDLAELIRDVRAEF- 232
Cdd:pfam00278 155 elglNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRelgidLKLLDIGGGfgipYRDEPPPDFEEYAAAIREALDEYf 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 233 --GVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHH--PEVFE-YQIKPRLLEEAGGGEQSAILAGSTCL 307
Cdd:pfam00278 235 ppDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLfrPALYDaYHPIPVVKEPGEGPLETYDVVGPTCE 314
|
330 340
....*....|....*....|....*...
gi 1914496624 308 AGDVFGeyRFRRIPE--VGERLVFADVG 333
Cdd:pfam00278 315 SGDVLA--KDRELPEleVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
13-352 |
1.50e-45 |
|
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: 160.16 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQALkQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADgSIHLTTPG 92
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEA-LPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPE-RIIFTGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 93 LRPDE---FAELSrlCSHISFNSLPQHQRLKASVS----DYSQGLRVNPKLSFADdQRYDPCRPHSKLGVDIELLRD--- 162
Cdd:cd06810 79 KSVSEieaALASG--VDHIVVDSLDELERLNELAKklgpKARILLRVNPDVSAGT-HKISTGGLKSKFGLSLSEARAale 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 163 ---GLPANVEGLHFHTVFACRDFRPLQQTLEKLRPILKRNR-----LKWLNVGGG----YLYHAIAeQQDLAELIRDVRA 230
Cdd:cd06810 156 rakELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVemgfpLEMLDLGGGlgipYDEQPLD-FEEYAALINPLLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 231 EF-----GVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHHPE-VFEY--QIKPRLLEEAGGGEQS--AI 300
Cdd:cd06810 235 KYfpndpGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHSFRpALAYdaYHPITPLKAPGPDEPLvpAT 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1914496624 301 LAGSTCLAGDVFGEYRFRRIPEVGERLVFADVGAYSLIKANRFNGYQLPDVY 352
Cdd:cd06810 315 LAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEY 366
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
13-354 |
1.56e-32 |
|
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: 125.29 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQALKQASGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLAseVLAEADGS-IHLTTP 91
Cdd:cd06828 3 TPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRA--LKAGFPPErIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 92 GLRPDEFAELSRL-CSHISFNSLPQHQRLKASVSDYSQG----LRVNP--------KLSFAddqrydpcRPHSKLGVDIE 158
Cdd:cd06828 81 GKSDEELELALELgILRINVDSLSELERLGEIAPELGKGapvaLRVNPgvdagthpYISTG--------GKDSKFGIPLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 159 LLRDGLPA-------NVEGLHFHT---VFacrDFRPLQQTLEKLRPILKRNR-----LKWLNVGGGY--LYHAIAEQQDL 221
Cdd:cd06828 153 QALEAYRRakelpglKLVGLHCHIgsqIL---DLEPFVEAAEKLLDLAAELRelgidLEFLDLGGGLgiPYRDEDEPLDI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 222 AELIRDVRAEFG--------VDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHH--PEVFE--YQIKPrLL 289
Cdd:cd06828 230 EEYAEAIAEALKelceggpdLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLirPALYGayHEIVP-VN 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914496624 290 EEAGGGEQSAILAGSTCLAGDVFGEYRFRRIPEVGERLVFADVGAYSLIKANRFNGYQLPDVYSV 354
Cdd:cd06828 309 KPGEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
13-352 |
3.65e-21 |
|
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: 93.87 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQA--LKQASGCKILYSMKALPLAALLTLIKDQvdGFS--VSSLFEARLA------------- 75
Cdd:cd06841 7 SPFFVFDEDALRENYRELLGafKKRYPNVVIAYSYKTNYLPAICKILHEE--GGYaeVVSAMEYELAlklgvpgkriifn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 76 -----SEVLAEA---DGSIHLttpglrpDEFAELSRLcshisfNSLPQHQRLKASVsdysqGLRVNpklSFADDQRYdpc 147
Cdd:cd06841 85 gpyksKEELEKAleeGALINI-------DSFDELERI------LEIAKELGRVAKV-----GIRLN---MNYGNNVW--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 148 rphSKLGVDIELLRDGLPA----------NVEGLHFHTVFACRDFRPLQQTLEKLRPILKR---NRLKWLNVGGGYLYH- 213
Cdd:cd06841 141 ---SRFGFDIEENGEALAAlkkiqesknlSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRlfgLELEYLDLGGGFPAKt 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 214 --AIAEQQ--------DLAELIRDVRAEFGVD------VYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHHP 277
Cdd:cd06841 218 plSLAYPQedtvpdpeDYAEAIASTLKEYYANkenkpkLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINNIP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 278 EVFEYQ--IKPRLLEEAGGGEQSAILAGSTCLAGDVFgeyrFRRIP----EVGERLVFADVGAYSLIKANRFNGYQlPDV 351
Cdd:cd06841 298 TIFWYHhpILVLRPGKEDPTSKNYDVYGFNCMESDVL----FPNVPlpplNVGDILAIRNVGAYNMTQSNQFIRPR-PAV 372
|
.
gi 1914496624 352 Y 352
Cdd:cd06841 373 Y 373
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
152-354 |
5.84e-19 |
|
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: 87.16 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 152 KLGVDIELLRD--------GLpaNVEGLHFHTVFACRDFRPLQQTLEKLRPILKRNR-----LKWLNVGGGYLYHAIAEQ 218
Cdd:cd00622 133 KFGADPEEAREllrrakelGL--NVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAelgfkLKLLDIGGGFPGSYDGVV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 219 QDL---AELIRDVRAEF----GVDVYVEPGKGLVGNAGYLLTTVL---DRFVSDGKQVLILDTSVNH--------HpevF 280
Cdd:cd00622 211 PSFeeiAAVINRALDEYfpdeGVRIIAEPGRYLVASAFTLAVNVIakrKRGDDDRERWYYLNDGVYGsfneilfdH---I 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914496624 281 EYQIKPRLLEEAGGGEQSAILAGSTCLAGD-VFGEYRFRRIPEVGERLVFADVGAYSLIKANRFNGYQLPDVYSV 354
Cdd:cd00622 288 RYPPRVLKDGGRDGELYPSSLWGPTCDSLDvIYEDVLLPEDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
9-337 |
1.85e-17 |
|
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: 83.03 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 9 QIPTSPALVLDEAQILAnlkRLQALKQA--SGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADgSI 86
Cdd:cd06839 3 DAYGTPFYVYDRDRVRE---RYAALRAAlpPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPE-KI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 87 HLTTPGLRPDEFA---ELSRLCSHI-SFNSLPQHQRL------KASVSdysqgLRVNPKLSFaddqrydpcrPHSKL--- 153
Cdd:cd06839 79 LFAGPGKSDAELRraiEAGIGTINVeSLEELERIDALaeehgvVARVA-----LRINPDFEL----------KGSGMkmg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 154 ------GVDIELLRDGLPA-------NVEGLHFHTVFACRD-------FRPLQQTLEKLRPILKRnRLKWLNVGGGY--L 211
Cdd:cd06839 144 ggpsqfGIDVEELPAVLARiaalpnlRFVGLHIYPGTQILDadalieaFRQTLALALRLAEELGL-PLEFLDLGGGFgiP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 212 YHAIAEQQDLAEL---IRDVRAEF-----GVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNHHPEV---F 280
Cdd:cd06839 223 YFPGETPLDLEALgaaLAALLAELgdrlpGTRVVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVTDGGMHHHLAAsgnF 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914496624 281 EYQIK---P-RLLEEAGGGE-QSAILAGSTCLAGDVFGeyrfRRI----PEVGERLVFADVGAYSL 337
Cdd:cd06839 303 GQVLRrnyPlAILNRMGGEErETVTVVGPLCTPLDLLG----RNVelppLEPGDLVAVLQSGAYGL 364
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
13-344 |
1.06e-13 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 72.81 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQALKQASgcKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADGSIHLTTPG 92
Cdd:PRK08961 503 SPCYVYHLPTVRARARALAALAAVD--QRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELFPELSPERVLFTPN 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 93 LRP-DEFAELSRLCSHISFNSLPQHQRLKASVSDYSQGLRVNPKLSFADDQRYDPCRPHSKLGV---DIELLRD---GLP 165
Cdd:PRK08961 581 FAPrAEYEAAFALGVTVTLDNVEPLRNWPELFRGREVWLRIDPGHGDGHHEKVRTGGKESKFGLsqtRIDEFVDlakTLG 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 166 ANVEGLHFHTVFACRDFRPLQQTLEKLRPILKR-NRLKWLNVGGGY--LYHAIAEQQDL---AELIRDVRAEF-GVDVYV 238
Cdd:PRK08961 661 ITVVGLHAHLGSGIETGEHWRRMADELASFARRfPDVRTIDLGGGLgiPESAGDEPFDLdalDAGLAEVKAQHpGYQLWI 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 239 EPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVN----------HHpevfEYQIKPRLLEEAgggEQSAILAGSTCLA 308
Cdd:PRK08961 741 EPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNslirpalygaYH----EIVNLSRLDEPA---AGTADVVGPICES 813
|
330 340 350
....*....|....*....|....*....|....*...
gi 1914496624 309 GDVFGeYRfRRIPEV--GERLVFADVGAYSLIKANRFN 344
Cdd:PRK08961 814 SDVLG-KR-RRLPATaeGDVILIANAGAYGYSMSSTYN 849
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
29-335 |
8.95e-12 |
|
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: 65.77 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 29 RLQALKQA--SGCKILYSMKALPLAALLTLIKDQVDGFSVSSLFE-ARLASEVlaeADGSIHLTTPGLRPDEFA---ELS 102
Cdd:cd06843 15 HARALRASlpPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEiAHVRAAV---PDAPLIFGGPGKTDSELAqalAQG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 103 RLCSHISfnSLPQHQRLKASVSDYSQG----LRVNPKLsfaddqrydPCRPHSKL---------GVD-------IELLRD 162
Cdd:cd06843 92 VERIHVE--SELELRRLNAVARRAGRTapvlLRVNLAL---------PDLPSSTLtmggqptpfGIDeadlpdaLELLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 163 gLPA-NVEGLHFHTVFACRDfrpLQQTLEKLRPILKRNR---------LKWLNVGGGY--LYHAIAEQQD-------LAE 223
Cdd:cd06843 161 -LPNiRLRGFHFHLMSHNLD---AAAHLALVKAYLETARqwaaehgldLDVVNVGGGIgvNYADPEEQFDwagfcegLDQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 224 LIRDvrAEFGVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVNH----------HP-EVFEYQIKPRLLEEA 292
Cdd:cd06843 237 LLAE--YEPGLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHfrlpaawghnHPfSVLPVEEWPYPWPRP 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1914496624 293 GGGEQSAILAGSTCLAGDVFGeyRFRRIPE--VGERLVFADVGAY 335
Cdd:cd06843 315 SVRDTPVTLVGQLCTPKDVLA--RDVPVDRlrAGDLVVFPLAGAY 357
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
12-350 |
3.27e-11 |
|
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: 63.99 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 12 TSPALVLDEAQILANLKRLQALKQASgcKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADGSIHLTTP 91
Cdd:cd06840 11 VGPCYVYDLETVRARARQVSALKAVD--SLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLFPDLDPRRVLFTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 92 GLRP-DEFAELSRLCSHISFNSLPQHQRLKASVSDYSQGLRVNPKLSFADDQRYDPCRPHSKLGV---DIELLRD---GL 164
Cdd:cd06840 89 NFAArSEYEQALELGVNVTVDNLHPLREWPELFRGREVILRIDPGQGEGHHKHVRTGGPESKFGLdvdELDEARDlakKA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 165 PANVEGLHFHTVFACRDFRPLQQTLEKLRPILKR-NRLKWLNVGGGY--LYHAIAEQQDLAEL---IRDVRAEF-GVDVY 237
Cdd:cd06840 169 GIIVIGLHAHSGSGVEDTDHWARHGDYLASLARHfPAVRILNVGGGLgiPEAPGGRPIDLDALdaaLAAAKAAHpQYQLW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 238 VEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVN----------HHpEVFEYQikpRLLEEAGGgeqSAILAGSTCL 307
Cdd:cd06840 249 MEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNslirpalygaYH-EIVNLS---RLDEPPAG---NADVVGPICE 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1914496624 308 AGDVFGeyRFRRIPEV--GERLVFADVGAYSLIKANRFNGYQLPD 350
Cdd:cd06840 322 SGDVLG--RDRLLPETeeGDVILIANAGAYGFCMASTYNLREPAE 364
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
13-335 |
3.34e-09 |
|
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: 58.04 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 13 SPALVLDEAQILANLKRLQALKQASG--CKILYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADgSIHLTT 90
Cdd:cd06842 10 SPLNVLFPQTFRENIAALRAVLDRHGvdGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGD-RIVATG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 91 PgLRPDEFAELSRLC-SHISFNSLPQHQRLKASVSDYSQG-----LRVNPklsfaddqryDPCRPHSKLGVDIELLRDGL 164
Cdd:cd06842 89 P-AKTDEFLWLAVRHgATIAVDSLDELDRLLALARGYTTGparvlLRLSP----------FPASLPSRFGMPAAEVRTAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 165 --------PANVEGLHFHTVFACRDFR--PLQQTLEKLRPILKRN-RLKWLNVGGG------------------------ 209
Cdd:cd06842 158 erlaqlreRVRLVGFHFHLDGYSAAQRvaALQECLPLIDRARALGlAPRFIDIGGGfpvsyladaaeweaflaaltealy 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 210 ---------------------YLYHA---------------IAEQQDLAELIRDVraefGVDVYVEPGKGLVGNAGYLLT 253
Cdd:cd06842 238 gygrpltwrneggtlrgpddfYPYGQplvaadwlrailsapLPQGRTIAERLRDN----GITLALEPGRALLDQCGLTVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 254 TVLDRFV-SDGKQVLILD-TSVNHHPEVFEYQIKPRLL----EEAGGGEQSAILAGSTCLAGDVFGEYR--FRRIPEVGE 325
Cdd:cd06842 314 RVAFVKQlGDGNHLIGLEgNSFSACEFSSEFLVDPLLIpapePTTDGAPIEAYLAGASCLESDLITRRKipFPRLPKPGD 393
|
410
....*....|
gi 1914496624 326 RLVFADVGAY 335
Cdd:cd06842 394 LLVFPNTAGY 403
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
201-354 |
1.71e-08 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 55.95 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 201 LKWLNVGGGY---LYHAIA---EQQDLAELIRDVRAEFGVDVYVEPGKGLVGNAGYLLTTVLDRFVSDGKQVLILDTSVN 274
Cdd:PLN02537 222 LSYLNIGGGLgidYYHAGAvlpTPRDLIDTVRELVLSRDLTLIIEPGRSLIANTCCFVNRVTGVKTNGTKNFIVIDGSMA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 275 H--HPEVFE-YQ----IKPrlleEAGGGEQSAI-LAGSTCLAGDVFGEYRFRRIPEVGERLVFADVGAYSLIKANRFNGY 346
Cdd:PLN02537 302 EliRPSLYDaYQhielVSP----PPPDAEVSTFdVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLK 377
|
....*...
gi 1914496624 347 QLPDVYSV 354
Cdd:PLN02537 378 MRPPEYWV 385
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
129-246 |
3.18e-07 |
|
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: 50.74 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 129 GLRVNPKLSFADdqrydpCRPHSKLGVDIELLRDGLPA-------NVEGLHFHTVFACRDFRPLQQTLEKLRPILKRNR- 200
Cdd:pfam02784 108 LLRIKPDDSAAT------CPLSSKFGADLDEDVEALLEaakllnlQVVGVSFHVGSGCTDAEAFVLALEDARGVFDQGAe 181
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 201 ----LKWLNVGGGY--LYHAIAEQQDL---AELIRDVRAEF-----GVDVYVEPGKGLVG 246
Cdd:pfam02784 182 lgfnLKILDLGGGFgvDYTEGEEPLDFeeyANVINEALEEYfpgdpGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
63-355 |
1.36e-06 |
|
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: 49.70 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 63 GFSVSSLFEARLASEVLAEADgSIHLTTPGLRPDEFAELSRLCSHISFNSLPQHQRLKASVSDYSQ-----GLRVNPK-- 135
Cdd:cd06836 52 GAEVASPGELELALAAGFPPE-RIVFDSPAKTRAELREALELGVAINIDNFQELERIDALVAEFKEassriGLRVNPQvg 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 136 ------LSFADdqrydpcrPHSKLGVDIELL-RDGLPAN------VEGLHFHT-------VFACRDFRPLQQTLEKLRPI 195
Cdd:cd06836 131 agkigaLSTAT--------ATSKFGVALEDGaRDEIIDAfarrpwLNGLHVHVgsqgcelSLLAEGIRRVVDLAEEINRR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 196 LKRNRLKWLNVGGG-------------YLYHAIAEQQDLAELIRDvraefGVDVYVEPGKGLVGNAGYLLTTVLDRFVSD 262
Cdd:cd06836 203 VGRRQITRIDIGGGlpvnfeseditptFADYAAALKAAVPELFDG-----RYQLVTEFGRSLLAKCGTIVSRVEYTKSSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 263 GKQVLILDTSVN------HHPEVFEYQIKPRLL--EEAGGGEQSAILAGSTCLAGDVFGeyRFRRIPEV--GERLVFADV 332
Cdd:cd06836 278 GRRIAITHAGAQvatrtaYAPDDWPLRVTVFDAngEPKTGPEVVTDVAGPCCFAGDVLA--KERALPPLepGDYVAVHDT 355
|
330 340
....*....|....*....|...
gi 1914496624 333 GAYSLIKANRFNGYQLPDVYSVN 355
Cdd:cd06836 356 GAYYFSSHSSYNSLPRPAVYGVR 378
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
28-241 |
3.29e-04 |
|
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: 41.54 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 28 KRLQALKQASGCKI--LYSMKALPLAALLTLIKDQVDGFSVSSLFEARLASEVLAEADGsIHLTTPGLRPDEFAELSRLC 105
Cdd:cd06808 3 HNYRRLREAAPAGItlFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEP-ILFLGPCKQVSELEDAAEQG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 106 sHISFN--SLPQHQRLKASVSDYSQGLRVNPKLsfaddqryDPCRPHSKLGVDIELLRDGLPA-------NVEGLHFHTV 176
Cdd:cd06808 82 -VIVVTvdSLEELEKLEEAALKAGPPARVLLRI--------DTGDENGKFGVRPEELKALLERakelphlRLVGLHTHFG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914496624 177 FACRDFRPLQQTLEKLRPILKR-----NRLKWLNVGGGYlyhAIAEQQDLAELIRDVraefgvdvyVEPG 241
Cdd:cd06808 153 SADEDYSPFVEALSRFVAALDQlgelgIDLEQLSIGGSF---AILYLQELPLGTFII---------VEPG 210
|
|
| |
