|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
4-411 |
2.51e-148 |
|
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: 427.26 E-value: 2.51e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 4 KTVPFNEEQIRSIIAEHPTPFHIYDEKAIVDNVRKLIKAFDWAyDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELE 83
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGS-GAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 84 LCDKVGIKGHDIVFSSNDTPYAEFKRAMELGAL-VNLDDISMIEFMEERGPLPEW---ICARYNPGPLLKGGNDIIGTPE 159
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVGhINVDSLSELERLAELAAELGKrapVGLRVNPGVDAGTHEYISTGGK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 160 EAKYGMTREQIIDAFRILKD-KGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNmLGINIEFLDFGGGIGLPYRP 238
Cdd:COG0019 167 DSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRE-LGIDLEWLDLGGGLGIPYTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 239 EESFIDYDELSAGIKKHFEEIMEPagldKCRISFECGRAITGPYGYLVTTAIHHKHIW-KEYIGVDACMANLMRPGMYGS 317
Cdd:COG0019 246 GDEPPDLEELAAAIKEALEELCGL----GPELILEPGRALVGNAGVLLTRVLDVKENGgRRFVIVDAGMNDLMRPALYGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 318 YHHITVMGKENAPKDHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLLHaDGSVT 397
Cdd:COG0019 322 YHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVD-DGEAR 400
|
410
....*....|....
gi 2543900857 398 QIRRAETLDDLFAT 411
Cdd:COG0019 401 LIRRRETYEDLLAS 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
20-390 |
1.18e-145 |
|
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: 418.81 E-value: 1.18e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 20 HPTPFHIYDEKAIVDNVRKLIKAFDWaYDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSS 99
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSG-PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 100 NDTPYAEFKRAMELG-ALVNLDDISMIEFMEERGP---LPEWICARYNPGPLLKGGNDIIGTPEEAKYGMTREQIIDAFR 175
Cdd:cd06828 80 NGKSDEELELALELGiLRINVDSLSELERLGEIAPelgKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 176 ILKD-KGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNmLGINIEFLDFGGGIGLPYRPEESFIDYDELSAGIKK 254
Cdd:cd06828 160 RAKElPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRE-LGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 255 HFEEIMEpaGLDKCRISFECGRAITGPYGYLVTTAIHHKHI-WKEYIGVDACMANLMRPGMYGSYHHITVMGKENAPKDH 333
Cdd:cd06828 239 ALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETgGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2543900857 334 VYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLL 390
Cdd:cd06828 317 KVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
18-410 |
4.93e-91 |
|
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: 281.10 E-value: 4.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 18 AEHPTPFHIYDEKAIVDNVRKLIKAF-DWAYDFkeyFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIV 96
Cdd:TIGR01048 21 QEFGTPLYVYDEDTIRRRFRAYKEAFgGRSLVC---YAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 97 FSSNDTPYAEFKRAMELGALVNLDDISMIEFMEE---RGPLPEWICARYNPGPLLKGGNDIIGTPEEAKYGMTREQIIDA 173
Cdd:TIGR01048 98 FSGNGKSRAELERALELGICINVDSFSELERLNEiapELGKKARISLRVNPGVDAKTHPYISTGLKDSKFGIDVEEALEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 174 FR-ILKDKGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQnmLGINIEFLDFGGGIGLPYRPEESFIDYDELSAGI 252
Cdd:TIGR01048 178 YLyALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLA--EGIDLEFLDLGGGLGIPYTPEEEPPDLSEYAQAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 253 KKHFEEIMEpAGLDKcRISFECGRAITGPYGYLVTTAIHHKHI-WKEYIGVDACMANLMRPGMYGSYHHITVMGKENAPK 331
Cdd:TIGR01048 256 LNALEGYAD-LGLDP-KLILEPGRSIVANAGVLLTRVGFVKETgSRNFVIVDAGMNDLIRPALYGAYHHIIVLNRTNDAP 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543900857 332 DHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLLHaDGSVTQIRRAETLDDLFA 410
Cdd:TIGR01048 334 TEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVD-GGQARLIRRRETYEDLWA 411
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
24-369 |
5.12e-74 |
|
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: 234.69 E-value: 5.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 24 FHIYDEKAIVDNVRKLIKAFdwAYDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSNDTP 103
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAAL--PPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 104 YAEFKRAMELG-ALVNLDDISMIEFMEERGP-LPEWICARYNPGPLLKGGNDIIGtPEEAKYGMTREQIIDAFRILKDKG 181
Cdd:pfam00278 79 DSEIRYALEAGvLCFNVDSEDELEKIAKLAPeLVARVALRINPDVDAGTHKISTG-GLSSKFGIDLEDAPELLALAKELG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 182 VKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNmLGINIEFLDFGGGIGLPYRPEESFiDYDELSAGIKKHFEEIME 261
Cdd:pfam00278 158 LNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRE-LGIDLKLLDIGGGFGIPYRDEPPP-DFEEYAAAIREALDEYFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 262 PagldKCRISFECGRAITGPYGYLVTTAIHHKHIW-KEYIGVDACMANLMRPGMYGSYHHITVMGKENAPKDHVYDVAGS 340
Cdd:pfam00278 236 P----DLEIIAEPGRYLVANAGVLVTRVIAVKTGGgKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETYDVVGP 311
|
330 340
....*....|....*....|....*....
gi 2543900857 341 LCENCDKFAIDRSLPEIDDGDILVIHDTG 369
Cdd:pfam00278 312 TCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
17-392 |
3.76e-53 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 189.91 E-value: 3.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 17 IAEHPTPFHIYDEKAIVDNVRKL--IKAFDwaydfKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKV--GIKG 92
Cdd:PRK08961 498 LSDAGSPCYVYHLPTVRARARALaaLAAVD-----QRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSP 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 93 HDIVFSSNDTPYAEFKRAMELGALVNLDDISmiefmeergPLPEW--------ICARYNPG-------PLLKGGNdiigt 157
Cdd:PRK08961 573 ERVLFTPNFAPRAEYEAAFALGVTVTLDNVE---------PLRNWpelfrgreVWLRIDPGhgdghheKVRTGGK----- 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 158 peEAKYGMTREQIIDAFRILKDKGVKHFGLHTmvvsnelHVNGLINTA---KMMFELAVEVQNMLGiNIEFLDFGGGIGL 234
Cdd:PRK08961 639 --ESKFGLSQTRIDEFVDLAKTLGITVVGLHA-------HLGSGIETGehwRRMADELASFARRFP-DVRTIDLGGGLGI 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 235 PYRPEESFIDYDELSAGIkkhfeeiMEPAGL-DKCRISFECGRAITGPYGYLVTTAIHHKHIWK-EYIGVDACMANLMRP 312
Cdd:PRK08961 709 PESAGDEPFDLDALDAGL-------AEVKAQhPGYQLWIEPGRYLVAEAGVLLARVTQVKEKDGvRRVGLETGMNSLIRP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 313 GMYGSYHHITVMGKENAPKDHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLLHA 392
Cdd:PRK08961 782 ALYGAYHEIVNLSRLDEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLDA 861
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
4-411 |
2.51e-148 |
|
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: 427.26 E-value: 2.51e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 4 KTVPFNEEQIRSIIAEHPTPFHIYDEKAIVDNVRKLIKAFDWAyDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELE 83
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGS-GAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 84 LCDKVGIKGHDIVFSSNDTPYAEFKRAMELGAL-VNLDDISMIEFMEERGPLPEW---ICARYNPGPLLKGGNDIIGTPE 159
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVGhINVDSLSELERLAELAAELGKrapVGLRVNPGVDAGTHEYISTGGK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 160 EAKYGMTREQIIDAFRILKD-KGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNmLGINIEFLDFGGGIGLPYRP 238
Cdd:COG0019 167 DSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRE-LGIDLEWLDLGGGLGIPYTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 239 EESFIDYDELSAGIKKHFEEIMEPagldKCRISFECGRAITGPYGYLVTTAIHHKHIW-KEYIGVDACMANLMRPGMYGS 317
Cdd:COG0019 246 GDEPPDLEELAAAIKEALEELCGL----GPELILEPGRALVGNAGVLLTRVLDVKENGgRRFVIVDAGMNDLMRPALYGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 318 YHHITVMGKENAPKDHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLLHaDGSVT 397
Cdd:COG0019 322 YHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVD-DGEAR 400
|
410
....*....|....
gi 2543900857 398 QIRRAETLDDLFAT 411
Cdd:COG0019 401 LIRRRETYEDLLAS 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
20-390 |
1.18e-145 |
|
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: 418.81 E-value: 1.18e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 20 HPTPFHIYDEKAIVDNVRKLIKAFDWaYDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSS 99
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSG-PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 100 NDTPYAEFKRAMELG-ALVNLDDISMIEFMEERGP---LPEWICARYNPGPLLKGGNDIIGTPEEAKYGMTREQIIDAFR 175
Cdd:cd06828 80 NGKSDEELELALELGiLRINVDSLSELERLGEIAPelgKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 176 ILKD-KGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNmLGINIEFLDFGGGIGLPYRPEESFIDYDELSAGIKK 254
Cdd:cd06828 160 RAKElPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRE-LGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 255 HFEEIMEpaGLDKCRISFECGRAITGPYGYLVTTAIHHKHI-WKEYIGVDACMANLMRPGMYGSYHHITVMGKENAPKDH 333
Cdd:cd06828 239 ALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETgGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2543900857 334 VYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLL 390
Cdd:cd06828 317 KVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
18-410 |
4.93e-91 |
|
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: 281.10 E-value: 4.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 18 AEHPTPFHIYDEKAIVDNVRKLIKAF-DWAYDFkeyFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIV 96
Cdd:TIGR01048 21 QEFGTPLYVYDEDTIRRRFRAYKEAFgGRSLVC---YAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 97 FSSNDTPYAEFKRAMELGALVNLDDISMIEFMEE---RGPLPEWICARYNPGPLLKGGNDIIGTPEEAKYGMTREQIIDA 173
Cdd:TIGR01048 98 FSGNGKSRAELERALELGICINVDSFSELERLNEiapELGKKARISLRVNPGVDAKTHPYISTGLKDSKFGIDVEEALEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 174 FR-ILKDKGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQnmLGINIEFLDFGGGIGLPYRPEESFIDYDELSAGI 252
Cdd:TIGR01048 178 YLyALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLA--EGIDLEFLDLGGGLGIPYTPEEEPPDLSEYAQAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 253 KKHFEEIMEpAGLDKcRISFECGRAITGPYGYLVTTAIHHKHI-WKEYIGVDACMANLMRPGMYGSYHHITVMGKENAPK 331
Cdd:TIGR01048 256 LNALEGYAD-LGLDP-KLILEPGRSIVANAGVLLTRVGFVKETgSRNFVIVDAGMNDLIRPALYGAYHHIIVLNRTNDAP 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2543900857 332 DHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLLHaDGSVTQIRRAETLDDLFA 410
Cdd:TIGR01048 334 TEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVD-GGQARLIRRRETYEDLWA 411
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
24-369 |
5.12e-74 |
|
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: 234.69 E-value: 5.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 24 FHIYDEKAIVDNVRKLIKAFdwAYDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSNDTP 103
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAAL--PPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 104 YAEFKRAMELG-ALVNLDDISMIEFMEERGP-LPEWICARYNPGPLLKGGNDIIGtPEEAKYGMTREQIIDAFRILKDKG 181
Cdd:pfam00278 79 DSEIRYALEAGvLCFNVDSEDELEKIAKLAPeLVARVALRINPDVDAGTHKISTG-GLSSKFGIDLEDAPELLALAKELG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 182 VKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNmLGINIEFLDFGGGIGLPYRPEESFiDYDELSAGIKKHFEEIME 261
Cdd:pfam00278 158 LNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRE-LGIDLKLLDIGGGFGIPYRDEPPP-DFEEYAAAIREALDEYFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 262 PagldKCRISFECGRAITGPYGYLVTTAIHHKHIW-KEYIGVDACMANLMRPGMYGSYHHITVMGKENAPKDHVYDVAGS 340
Cdd:pfam00278 236 P----DLEIIAEPGRYLVANAGVLVTRVIAVKTGGgKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETYDVVGP 311
|
330 340
....*....|....*....|....*....
gi 2543900857 341 LCENCDKFAIDRSLPEIDDGDILVIHDTG 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 |
4.52e-68 |
|
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: 220.25 E-value: 4.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 22 TPFHIYDEKAIVDNVRKLIKAFdwAYDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSND 101
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEAL--PSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 102 TPYAEFKRAMELG-ALVNLDDISM----IEFMEERGPLPEwICARYNPGpLLKGGNDIIGTPEEAKYGMTREQIIDAFRI 176
Cdd:cd06810 79 KSVSEIEAALASGvDHIVVDSLDElerlNELAKKLGPKAR-ILLRVNPD-VSAGTHKISTGGLKSKFGLSLSEARAALER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 177 LKDKGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNMlGINIEFLDFGGGIGLPYRPEEsfIDYDELSAGIKKHF 256
Cdd:cd06810 157 AKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEM-GFPLEMLDLGGGLGIPYDEQP--LDFEEYAALINPLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 257 EEimEPAGLDKCRISFECGRAITGPYGYLVTTAIHHKHI-WKEYIGVDACMANLMRPGM-YGSYHHITVMGKENAPKDHV 334
Cdd:cd06810 234 KK--YFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNgGRFFAVVDGGMNHSFRPALaYDAYHPITPLKAPGPDEPLV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2543900857 335 -YDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLL 390
Cdd:cd06810 312 pATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
17-392 |
3.76e-53 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 189.91 E-value: 3.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 17 IAEHPTPFHIYDEKAIVDNVRKL--IKAFDwaydfKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKV--GIKG 92
Cdd:PRK08961 498 LSDAGSPCYVYHLPTVRARARALaaLAAVD-----QRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSP 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 93 HDIVFSSNDTPYAEFKRAMELGALVNLDDISmiefmeergPLPEW--------ICARYNPG-------PLLKGGNdiigt 157
Cdd:PRK08961 573 ERVLFTPNFAPRAEYEAAFALGVTVTLDNVE---------PLRNWpelfrgreVWLRIDPGhgdghheKVRTGGK----- 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 158 peEAKYGMTREQIIDAFRILKDKGVKHFGLHTmvvsnelHVNGLINTA---KMMFELAVEVQNMLGiNIEFLDFGGGIGL 234
Cdd:PRK08961 639 --ESKFGLSQTRIDEFVDLAKTLGITVVGLHA-------HLGSGIETGehwRRMADELASFARRFP-DVRTIDLGGGLGI 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 235 PYRPEESFIDYDELSAGIkkhfeeiMEPAGL-DKCRISFECGRAITGPYGYLVTTAIHHKHIWK-EYIGVDACMANLMRP 312
Cdd:PRK08961 709 PESAGDEPFDLDALDAGL-------AEVKAQhPGYQLWIEPGRYLVAEAGVLLARVTQVKEKDGvRRVGLETGMNSLIRP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 313 GMYGSYHHITVMGKENAPKDHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLLHA 392
Cdd:PRK08961 782 ALYGAYHEIVNLSRLDEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLDA 861
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
17-390 |
1.56e-51 |
|
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: 176.86 E-value: 1.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 17 IAEHPTPFHIYDEKAIVDNVRKL--IKAFDwaydfKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKV--GIKG 92
Cdd:cd06840 7 LAPDVGPCYVYDLETVRARARQVsaLKAVD-----SLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 93 HDIVFSSNDTPYAEFKRAMELGALVNLDDISmiefmeergPLPEW--------ICARYNPGP-------LLKGGNdiigt 157
Cdd:cd06840 82 RRVLFTPNFAARSEYEQALELGVNVTVDNLH---------PLREWpelfrgreVILRIDPGQgeghhkhVRTGGP----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 158 peEAKYGMTREQIIDAFRILKDKGVKHFGLHTMVVSnelhvnGLINT---AKMMFELAVEVQNMLGINIefLDFGGGIGL 234
Cdd:cd06840 148 --ESKFGLDVDELDEARDLAKKAGIIVIGLHAHSGS------GVEDTdhwARHGDYLASLARHFPAVRI--LNVGGGLGI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 235 PYRPEESFIDYDELSAGIKK------HFEEIMEPagldkcrisfecGRAITGPYGYLVT--TAIHHKHIWKeYIGVDACM 306
Cdd:cd06840 218 PEAPGGRPIDLDALDAALAAakaahpQYQLWMEP------------GRFIVAESGVLLArvTQIKHKDGVR-FVGLETGM 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 307 ANLMRPGMYGSYHHITVMGKENAPKDHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSA 386
Cdd:cd06840 285 NSLIRPALYGAYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYNLREPAE 364
|
....
gi 2543900857 387 ELLL 390
Cdd:cd06840 365 EVVL 368
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
16-375 |
1.20e-48 |
|
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: 169.75 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 16 IIAEHPTPFHIYDEKAIVDNVRKLIKAFDWAY-DFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHD 94
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRYpNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 95 IVFSSNDTPYAEFKRAMELGALVNLDDISMIEFMEErgplpewICARYNPGPllKGG---NDIIGTPEEAKYGMTREQII 171
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEGALINIDSFDELERILE-------IAKELGRVA--KVGirlNMNYGNNVWSRFGFDIEENG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 172 DAFRILK----DKGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVqnmLGINIEFLDFGGGIG------LPYRPEES 241
Cdd:cd06841 152 EALAALKkiqeSKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRL---FGLELEYLDLGGGFPaktplsLAYPQEDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 242 FIDYDELSAGIKKHFEEiMEPAGLDKCRISFECGRAITGPYGYLVTTAIHHKHIWKEYIGVDACMANLMRPgMYGSYHHI 321
Cdd:cd06841 229 VPDPEDYAEAIASTLKE-YYANKENKPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINNIPT-IFWYHHPI 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2543900857 322 TVMGKENAPKDH-VYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSM 375
Cdd:cd06841 307 LVLRPGKEDPTSkNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQ 361
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
33-386 |
2.42e-40 |
|
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: 147.54 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 33 VDNVRKLIKAFDWAY--DFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSNDTPYAEFKRA 110
Cdd:cd06836 10 LDGFRALVARLTAAFpaPVLHTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 111 MELGALVNLD--------DISMIEFMEERGPlpewICARYNPgplLKGGNDI----IGTPeEAKYGM-----TREQIIDA 173
Cdd:cd06836 90 LELGVAINIDnfqeleriDALVAEFKEASSR----IGLRVNP---QVGAGKIgalsTATA-TSKFGValedgARDEIIDA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 174 FriLKDKGVKhfGLHTMVVSNELHVNGLINTAKMMFELAVEVQNMLGIN-IEFLDFGGGIGLPYRPEE---SFIDY-DEL 248
Cdd:cd06836 162 F--ARRPWLN--GLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRVGRRqITRIDIGGGLPVNFESEDitpTFADYaAAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 249 SAGIKKHFEeimepaglDKCRISFECGRAITGPYGYLVTTAIHHK-----HIWKEYIGVDACMANLMRPGMYgsYHHITV 323
Cdd:cd06836 238 KAAVPELFD--------GRYQLVTEFGRSLLAKCGTIVSRVEYTKssggrRIAITHAGAQVATRTAYAPDDW--PLRVTV 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543900857 324 MGKENAPKD---HVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSA 386
Cdd:cd06836 308 FDANGEPKTgpeVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
22-374 |
4.33e-40 |
|
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: 146.97 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 22 TPFHIYDEKAIVDNVRKLIKAFDWAYDFkeYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSND 101
Cdd:cd06839 7 TPFYVYDRDRVRERYAALRAALPPAIEI--YYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 102 TPYAEFKRAMELG-ALVNLD---DISMIEFMEERGPLPEWICARYNPGPLLKG-GNDIIGTPeeAKYGMTREQIIDAF-R 175
Cdd:cd06839 85 KSDAELRRAIEAGiGTINVEsleELERIDALAEEHGVVARVALRINPDFELKGsGMKMGGGP--SQFGIDVEELPAVLaR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 176 ILKDKGVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNMLGINIEFLDFGGGIGLPYRPEESFIDYDELSAGIKKH 255
Cdd:cd06839 163 IAALPNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLAEELGLPLEFLDLGGGFGIPYFPGETPLDLEALGAALAAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 256 FEEImePAGLDKCRISFECGRAITGPYGYLVTTAIHHKHIWKEYIGV-DAcmanlmrpgmyGSYHH-------------- 320
Cdd:cd06839 243 LAEL--GDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVtDG-----------GMHHHlaasgnfgqvlrrn 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2543900857 321 --ITVMGKENAPKDHVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHS 374
Cdd:cd06839 310 ypLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLS 365
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
22-407 |
5.24e-40 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 147.25 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 22 TPFHIYDEKAIVDNVRKLIKAFDWAYDFKEYfAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSND 101
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALEGLRSIIGY-AIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 102 TPYAEFKRAMELGALVNLD---DISMIEFMEERGPLPEWICARYNPG------PLLKGGNdiigtpEEAKYGMTREQI-- 170
Cdd:PLN02537 97 KLLEDLVLAAQEGVFVNVDsefDLENIVEAARIAGKKVNVLLRINPDvdpqvhPYVATGN------KNSKFGIRNEKLqw 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 171 -IDAFRILKDKgVKHFGLHTMVVSNELHVNGLINTAKMMFELAVEVQNMlGINIEFLDFGGGIGLPY--------RPEES 241
Cdd:PLN02537 171 fLDAVKAHPNE-LKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQ-GFELSYLNIGGGLGIDYyhagavlpTPRDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 242 FIDYDELSagIKKHFEEIMEPagldkcrisfecGRAITGPYGYLVTTAIHHK-HIWKEYIGVDACMANLMRPGMYGSYHH 320
Cdd:PLN02537 249 IDTVRELV--LSRDLTLIIEP------------GRSLIANTCCFVNRVTGVKtNGTKNFIVIDGSMAELIRPSLYDAYQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 321 ITVMG--KENAPKDhVYDVAGSLCENCDKFAIDRSLPEIDDGDILVIHDTGAHGHSMGFNYNGKLRSAELLLHADGSVTQ 398
Cdd:PLN02537 315 IELVSppPPDAEVS-TFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITK 393
|
....*....
gi 2543900857 399 IRRAETLDD 407
Cdd:PLN02537 394 IRHAETFDD 402
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
22-381 |
1.51e-29 |
|
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: 117.60 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 22 TPFHIYDEKAIVDNVRKLIKAFDWAydfKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSND 101
Cdd:cd00622 2 TPFLVVDLGDVVRKYRRWKKALPRV---RPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 102 TPYAEFKRAMELGalVNL---DdiSMIEFMEergplpewiCARYNPGP--LLKggndiIGTPEE-------AKYGMTREQ 169
Cdd:cd00622 79 KSISDIRYAAELG--VRLftfD--SEDELEK---------IAKHAPGAklLLR-----IATDDSgalcplsRKFGADPEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 170 IIDAFRILKDKGVKHFGLHTMVVSNELHVN---GLINTAKMMFELAVEvqnmLGINIEFLDFGGGI-GLPYRPEESFIDY 245
Cdd:cd00622 141 ARELLRRAKELGLNVVGVSFHVGSQCTDPSayvDAIADAREVFDEAAE----LGFKLKLLDIGGGFpGSYDGVVPSFEEI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 246 -DELSAGIKKHFeeimepaGLDKCRISFECGRAITGPYGYLVTTAI-------HHKHIWKeYIGVdacmanlmrpGMYGS 317
Cdd:cd00622 217 aAVINRALDEYF-------PDEGVRIIAEPGRYLVASAFTLAVNVIakrkrgdDDRERWY-YLND----------GVYGS 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2543900857 318 ----------YHHITVMGKENAPKDHVYDVAGSLCENCDKFAIDRSLPE-IDDGDILVIHDTGAHGHSMGFNYNG 381
Cdd:cd00622 279 fneilfdhirYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNG 353
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
33-280 |
2.06e-19 |
|
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: 86.57 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 33 VDNVRKLIKAFDWAY-DFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSNDTPYAEFKRAM 111
Cdd:pfam02784 1 LGSIERRHRRWKKALpRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 112 ELGA-LVNLDDISMIEFMEERGPLPEWIcARYNPGpllkggnDIIGT-PEEAKYGMTreqIIDAFRILKDKGVKHfglHT 189
Cdd:pfam02784 81 EVGVgCVTVDNVDELEKLARLAPEARVL-LRIKPD-------DSAATcPLSSKFGAD---LDEDVEALLEAAKLL---NL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 190 MVVSNELHV-NGLINTAKmmFELAVE-------VQNMLGINIEFLDFGGGIGLPYRPEESFIDYDE----LSAGIKKHFE 257
Cdd:pfam02784 147 QVVGVSFHVgSGCTDAEA--FVLALEdargvfdQGAELGFNLKILDLGGGFGVDYTEGEEPLDFEEyanvINEALEEYFP 224
|
250 260
....*....|....*....|...
gi 2543900857 258 eimepaGLDKCRISFECGRAITG 280
Cdd:pfam02784 225 ------GDPGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
52-372 |
7.14e-18 |
|
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: 84.64 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 52 YFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHdIVFSSNDTPYAEFKRAMELG-ALVN---LDDISMIEF 127
Cdd:cd06843 30 FYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDAP-LIFGGPGKTDSELAQALAQGvERIHvesELELRRLNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 128 MEERGPLPEWICARYNP-GPLLKGGNDIIG---TPeeakYGMTREQIIDAFRILKDKGVKHF-GLHTMVVSNELHVNGLI 202
Cdd:cd06843 109 VARRAGRTAPVLLRVNLaLPDLPSSTLTMGgqpTP----FGIDEADLPDALELLRDLPNIRLrGFHFHLMSHNLDAAAHL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 203 NTAKMMFELAVEVQNMLGINIEFLDFGGGIGLPY-RPEESFiDYDELSAGIKKHFEEIMepaglDKCRISFECGRAITGP 281
Cdd:cd06843 185 ALVKAYLETARQWAAEHGLDLDVVNVGGGIGVNYaDPEEQF-DWAGFCEGLDQLLAEYE-----PGLTLRFECGRYISAY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 282 YGYLVTTAIHHKHIWKEYIGVDACMANLMR-PGMYGSYHHITVMGKENAP--------KDHVYDVAGSLCENCDKFAIDR 352
Cdd:cd06843 259 CGYYVTEVLDLKRSHGEWFAVLRGGTHHFRlPAAWGHNHPFSVLPVEEWPypwprpsvRDTPVTLVGQLCTPKDVLARDV 338
|
330 340
....*....|....*....|
gi 2543900857 353 SLPEIDDGDILVIHDTGAHG 372
Cdd:cd06843 339 PVDRLRAGDLVVFPLAGAYG 358
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
32-240 |
2.80e-15 |
|
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: 74.28 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 32 IVDNVRKLIKAFdwAYDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSNDTPYAEFKRAM 111
Cdd:cd06808 1 IRHNYRRLREAA--PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 112 ELGAL-VNLDDISMIEFMEE-RGPLPE----WIcaRYNPGPLLKggndiigtpeeaKYGMTREQIIDAFRILKD-KGVKH 184
Cdd:cd06808 79 EQGVIvVTVDSLEELEKLEEaALKAGPparvLL--RIDTGDENG------------KFGVRPEELKALLERAKElPHLRL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2543900857 185 FGLHTMVVSNELHVNGLI-NTAKM--MFELAVEvqnmLGINIEFLDFGGGIGLPYRPEE 240
Cdd:cd06808 145 VGLHTHFGSADEDYSPFVeALSRFvaALDQLGE----LGIDLEQLSIGGSFAILYLQEL 199
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
158-287 |
1.61e-10 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family.
Pssm-ID: 143503 [Multi-domain] Cd Length: 409 Bit Score: 62.20 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 158 PEEAKYGMTREQIIDAFRILKDKGVKHFG--LHTMV---VSNELHV-NGLINTAKMMFELAvevqnMLGINIEFLDFGGG 231
Cdd:cd06830 159 GDRSKFGLTASEILEVVEKLKEAGMLDRLklLHFHIgsqITDIRRIkSALREAARIYAELR-----KLGANLRYLDIGGG 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543900857 232 IGLPY----RPEESFIDYD--ELSAGIKKHFEEIMEPAGLDKCRISFECGRAITGPYGYLVT 287
Cdd:cd06830 234 LGVDYdgsrSSSDSSFNYSleEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIF 295
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
16-241 |
8.97e-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: 59.97 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 16 IIAEHPTPFHIYDEKAIVDNVRKLIKAFDWA-YDFKEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHD 94
Cdd:cd06842 4 LVEAYGSPLNVLFPQTFRENIAALRAVLDRHgVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 95 IVFSSNDTPYAEFKRAMELGALVNLDDISMIEFMEERGPL----PEWICARYNPGPLLKggndiigtpeEAKYGMTREQI 170
Cdd:cd06842 84 IVATGPAKTDEFLWLAVRHGATIAVDSLDELDRLLALARGyttgPARVLLRLSPFPASL----------PSRFGMPAAEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 171 IDAFRILKD--KGVKHFGLHtmvvsneLHVNG--------LINTAKMMFELAVEvqnmLGINIEFLDFGGGIGLPYRPEE 240
Cdd:cd06842 154 RTALERLAQlrERVRLVGFH-------FHLDGysaaqrvaALQECLPLIDRARA----LGLAPRFIDIGGGFPVSYLADA 222
|
.
gi 2543900857 241 S 241
Cdd:cd06842 223 A 223
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
159-246 |
1.71e-04 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 43.91 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 159 EEAKYGMTREQIIDAFRILKDKGVK------HFGLHTMVVSNELHVNGLINTAKMMFELAvevqnMLGINIEFLDFGGGI 232
Cdd:PLN02439 156 EKGKFGLTATEIVRVVRKLRKEGMLdclqllHFHIGSQIPSTSLLKDGVSEAAQIYCELV-----RLGAPMRVIDIGGGL 230
|
90
....*....|....
gi 2543900857 233 GlpyrpeesfIDYD 246
Cdd:PLN02439 231 G---------IDYD 235
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
159-287 |
3.20e-04 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 42.80 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 159 EEAKYGMTREQIIDAFRILKDKGVK------HFGLHTMVvsNELHV--NGLINTAKMMFELAvevqnMLGINIEFLDFGG 230
Cdd:PRK05354 219 EKSKFGLSATEVLEAVERLREAGLLdclqllHFHLGSQI--ANIRDikTAVREAARFYVELR-----KLGAPIQYLDVGG 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543900857 231 GIGlpyrpeesfIDYD---------------ELSAGIKKHFEEIMEPAGLDKCRISFECGRAITGPYGYLVT 287
Cdd:PRK05354 292 GLG---------VDYDgtrsqsdssvnyslqEYANDVVYTLKEICEEHGVPHPTIISESGRALTAHHAVLVF 354
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
50-231 |
6.60e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor; Antizyme inhibitor (AZI) is homologous to the fold type III PLP-dependent enzyme ODC but does not retain any decarboxylase activity. Like ODC, AZI is presumed to exist as a homodimer. Antizyme is a regulatory protein that binds directly to the ODC monomer to block its active site, leading to its degradation by the 26S proteasome. AZI binds to Antizyme with a higher affinity than ODC, preventing the formation of the Antizyme-ODC complex. Thus, AZI blocks the ability of Antizyme to promote ODC degradation, which leads to increased ODC enzymatic activity and polyamine levels. AZI also prevents the degradation of other proteins regulated by Antizyme, such as cyclin D1.
Pssm-ID: 143504 Cd Length: 394 Bit Score: 38.68 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 50 KEYFAVKATPNPYIMRLLQKEGVGADCSSLAELELCDKVGIKGHDIVFSSNDTPYAEFKRAMELGALVNLDDiSMIEFME 129
Cdd:cd06831 38 KPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCD-NEIELKK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543900857 130 ergplpewiCARYNPGP--LLKGGNDIIGTPEEA--KYGMTREQIIDAFRILKDKGVKHFGL--HTMVVSNELHV-NGLI 202
Cdd:cd06831 117 ---------IARNHPNAklLLHIATEDNIGGEEMnmKFGTTLKNCRHLLECAKELDVQIVGVkfHVSSSCKEYQTyVHAL 187
|
170 180
....*....|....*....|....*....
gi 2543900857 203 NTAKMMFELAVEvqnmLGINIEFLDFGGG 231
Cdd:cd06831 188 SDARCVFDMAEE----FGFKMNMLDIGGG 212
|
|
| |
