|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
19-387 |
1.48e-139 |
|
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: 403.40 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 19 FPTPFHLYDEKSIRETARAVNAAFSWnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTS 98
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSG-PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 99 NDTRAEEFVYARDIN-ATINLDAYEDIFFLEEAA---GLPETLSLRFNPGGVFSLGTDIMDHPEESKFGMTKEQLFKGYA 174
Cdd:cd06828 80 NGKSDEELELALELGiLRINVDSLSELERLGEIApelGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 175 YLKE-KGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDYTPANKQNDIAVIGEGVHT 253
Cdd:cd06828 160 RAKElPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELR-ELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 254 KFDEILVpnDLGDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVDASAVNLLRPAMYDAYHHITNMTNPN-GDIQ 331
Cdd:cd06828 239 ALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGgKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGeGETE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2125487987 332 VVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEIL 387
Cdd:cd06828 317 KVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVL 372
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
3-409 |
3.00e-137 |
|
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: 399.14 E-value: 3.00e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 3 KTPFITADKLDQITAEFPTPFHLYDEKSIRETARAVNAAFSWnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELV 82
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPG-SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 83 MSNKIGFDSTAISFTSNDTRAEEFVYARDINA-TINLDAYEDIFFLEEAA---GLPETLSLRFNPGgvFSLGT--DIMDH 156
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELAaelGKRAPVGLRVNPG--VDAGTheYISTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 157 PEESKFGMTKEQLFKGYAYLKE-KGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDY 235
Cdd:COG0019 165 GKDSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELR-ELGIDLEWLDLGGGLGIPY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 236 TPANKQNDIAVIGEGVHTKFDEILVPndlgDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVDASAVNLLRPAMY 314
Cdd:COG0019 244 TEGDEPPDLEELAAAIKEALEELCGL----GPELILEPGRALVGNAGVLLTRVLDVKENGgRRFVIVDAGMNDLMRPALY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 315 DAYHHITNMTNPN-GDIQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEILYqEDGT 393
Cdd:COG0019 320 GAYHPIVPVGRPSgAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLV-DDGE 398
|
410
....*....|....*.
gi 2125487987 394 ARMIRRAETMNDYFAT 409
Cdd:COG0019 399 ARLIRRRETYEDLLAS 414
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
6-408 |
8.68e-92 |
|
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: 283.03 E-value: 8.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 6 FITADKLDQITAEFPTPFHLYDEKSIRETARAVNAAFSWNPGFkeFFAVKATPNPAILKILKEEGCGVDCATDTELVMSN 85
Cdd:TIGR01048 10 FIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRSLV--CYAVKANSNLAVLRLLAELGSGFDVVSGGELYRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 86 KIGFDSTAISFTSNDTRAEEFVYARDINATINLDAYEDIFFLEEAA---GLPETLSLRFNPGgvFSLGTdimdHP----- 157
Cdd:TIGR01048 88 AAGFPPEKIVFSGNGKSRAELERALELGICINVDSFSELERLNEIApelGKKARISLRVNPG--VDAKT----HPyistg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 158 -EESKFGMTKEQLFKGYAY-LKEKGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIknELGVSLDFINLSGGVGVDY 235
Cdd:TIGR01048 162 lKDSKFGIDVEEALEAYLYaLQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESL--AEGIDLEFLDLGGGLGIPY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 236 TPANKQNDIA----VIGEGVHTKFDEILVPNdlgdisIYTELGRFMTAPHGLVVTKVLHIKDT-YRRYVGVDASAVNLLR 310
Cdd:TIGR01048 240 TPEEEPPDLSeyaqAILNALEGYADLGLDPK------LILEPGRSIVANAGVLLTRVGFVKETgSRNFVIVDAGMNDLIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 311 PAMYDAYHHITNMTNPN-GDIQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEILYq 389
Cdd:TIGR01048 314 PALYGAYHHIIVLNRTNdAPTEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLV- 392
|
410
....*....|....*....
gi 2125487987 390 EDGTARMIRRAETMNDYFA 408
Cdd:TIGR01048 393 DGGQARLIRRRETYEDLWA 411
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
23-367 |
4.63e-71 |
|
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: 226.98 E-value: 4.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 23 FHLYDEKSIRETARAVNAAFSwnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTSNDTR 102
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALP--PRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 103 AEEFVYARDIN-ATINLDAYEDIFFLEE-AAGLPETLSLRFNPgGVFSLGTDIMDHPEESKFGMTKEQLFKGYAYLKEKG 180
Cdd:pfam00278 79 DSEIRYALEAGvLCFNVDSEDELEKIAKlAPELVARVALRINP-DVDAGTHKISTGGLSSKFGIDLEDAPELLALAKELG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 181 VKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDYTPaNKQNDIAVIGEGVHTKFDEILV 260
Cdd:pfam00278 158 LNVVGVHFHIGSQITDLEPFVEALQRARELFDRLR-ELGIDLKLLDIGGGFGIPYRD-EPPPDFEEYAAAIREALDEYFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 261 PndlgDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVDASAVNLLRPAMYDAYHHI-TNMTNPNGDIQVVDVTGS 338
Cdd:pfam00278 236 P----DLEIIAEPGRYLVANAGVLVTRVIAVKTGGgKTFVIVDAGMNDLFRPALYDAYHPIpVVKEPGEGPLETYDVVGP 311
|
330 340
....*....|....*....|....*....
gi 2125487987 339 LCENNDKFAKNRELPEARIGDTLVIHDTG 367
Cdd:pfam00278 312 TCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
16-386 |
2.00e-54 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 193.76 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 16 TAEFPTPFHLYDEKSIRETARAVNAAFSWNPGFkefFAVKATPNPAILKILKEEGCGVDCATDTEL--VMSNKIGFDSTA 93
Cdd:PRK08961 498 LSDAGSPCYVYHLPTVRARARALAALAAVDQRF---YAIKANPHPAILRTLEEEGFGFECVSIGELrrVFELFPELSPER 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 94 ISFTSNDTRAEEFVYARDINATINLD------AYEDIFfleeaAGlpETLSLRFNPGgvfslgtdimdHPE--------- 158
Cdd:PRK08961 575 VLFTPNFAPRAEYEAAFALGVTVTLDnveplrNWPELF-----RG--REVWLRIDPG-----------HGDghhekvrtg 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 159 --ESKFGMTKEQLFKGYAYLKEKGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnelgvSLDFINLSGGVGVDYT 236
Cdd:PRK08961 637 gkESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFP-----DVRTIDLGGGLGIPES 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 237 PANKQNDIAVIGEG------VHTKFDeilvpndlgdisIYTELGRFMTAPHGLVVTKVLHIKDTYR-RYVGVDASAVNLL 309
Cdd:PRK08961 712 AGDEPFDLDALDAGlaevkaQHPGYQ------------LWIEPGRYLVAEAGVLLARVTQVKEKDGvRRVGLETGMNSLI 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 310 RPAMYDAYHHITNMTN----PNGdiqVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAE 385
Cdd:PRK08961 780 RPALYGAYHEIVNLSRldepAAG---TADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPARE 856
|
.
gi 2125487987 386 I 386
Cdd:PRK08961 857 V 857
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
19-387 |
1.48e-139 |
|
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: 403.40 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 19 FPTPFHLYDEKSIRETARAVNAAFSWnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTS 98
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSG-PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 99 NDTRAEEFVYARDIN-ATINLDAYEDIFFLEEAA---GLPETLSLRFNPGGVFSLGTDIMDHPEESKFGMTKEQLFKGYA 174
Cdd:cd06828 80 NGKSDEELELALELGiLRINVDSLSELERLGEIApelGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 175 YLKE-KGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDYTPANKQNDIAVIGEGVHT 253
Cdd:cd06828 160 RAKElPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELR-ELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 254 KFDEILVpnDLGDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVDASAVNLLRPAMYDAYHHITNMTNPN-GDIQ 331
Cdd:cd06828 239 ALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGgKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGeGETE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2125487987 332 VVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEIL 387
Cdd:cd06828 317 KVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVL 372
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
3-409 |
3.00e-137 |
|
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: 399.14 E-value: 3.00e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 3 KTPFITADKLDQITAEFPTPFHLYDEKSIRETARAVNAAFSWnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELV 82
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPG-SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 83 MSNKIGFDSTAISFTSNDTRAEEFVYARDINA-TINLDAYEDIFFLEEAA---GLPETLSLRFNPGgvFSLGT--DIMDH 156
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELAaelGKRAPVGLRVNPG--VDAGTheYISTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 157 PEESKFGMTKEQLFKGYAYLKE-KGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDY 235
Cdd:COG0019 165 GKDSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELR-ELGIDLEWLDLGGGLGIPY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 236 TPANKQNDIAVIGEGVHTKFDEILVPndlgDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVDASAVNLLRPAMY 314
Cdd:COG0019 244 TEGDEPPDLEELAAAIKEALEELCGL----GPELILEPGRALVGNAGVLLTRVLDVKENGgRRFVIVDAGMNDLMRPALY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 315 DAYHHITNMTNPN-GDIQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEILYqEDGT 393
Cdd:COG0019 320 GAYHPIVPVGRPSgAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLV-DDGE 398
|
410
....*....|....*.
gi 2125487987 394 ARMIRRAETMNDYFAT 409
Cdd:COG0019 399 ARLIRRRETYEDLLAS 414
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
6-408 |
8.68e-92 |
|
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: 283.03 E-value: 8.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 6 FITADKLDQITAEFPTPFHLYDEKSIRETARAVNAAFSWNPGFkeFFAVKATPNPAILKILKEEGCGVDCATDTELVMSN 85
Cdd:TIGR01048 10 FIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRSLV--CYAVKANSNLAVLRLLAELGSGFDVVSGGELYRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 86 KIGFDSTAISFTSNDTRAEEFVYARDINATINLDAYEDIFFLEEAA---GLPETLSLRFNPGgvFSLGTdimdHP----- 157
Cdd:TIGR01048 88 AAGFPPEKIVFSGNGKSRAELERALELGICINVDSFSELERLNEIApelGKKARISLRVNPG--VDAKT----HPyistg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 158 -EESKFGMTKEQLFKGYAY-LKEKGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIknELGVSLDFINLSGGVGVDY 235
Cdd:TIGR01048 162 lKDSKFGIDVEEALEAYLYaLQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESL--AEGIDLEFLDLGGGLGIPY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 236 TPANKQNDIA----VIGEGVHTKFDEILVPNdlgdisIYTELGRFMTAPHGLVVTKVLHIKDT-YRRYVGVDASAVNLLR 310
Cdd:TIGR01048 240 TPEEEPPDLSeyaqAILNALEGYADLGLDPK------LILEPGRSIVANAGVLLTRVGFVKETgSRNFVIVDAGMNDLIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 311 PAMYDAYHHITNMTNPN-GDIQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEILYq 389
Cdd:TIGR01048 314 PALYGAYHHIIVLNRTNdAPTEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLV- 392
|
410
....*....|....*....
gi 2125487987 390 EDGTARMIRRAETMNDYFA 408
Cdd:TIGR01048 393 DGGQARLIRRRETYEDLWA 411
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
23-367 |
4.63e-71 |
|
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: 226.98 E-value: 4.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 23 FHLYDEKSIRETARAVNAAFSwnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTSNDTR 102
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALP--PRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 103 AEEFVYARDIN-ATINLDAYEDIFFLEE-AAGLPETLSLRFNPgGVFSLGTDIMDHPEESKFGMTKEQLFKGYAYLKEKG 180
Cdd:pfam00278 79 DSEIRYALEAGvLCFNVDSEDELEKIAKlAPELVARVALRINP-DVDAGTHKISTGGLSSKFGIDLEDAPELLALAKELG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 181 VKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDYTPaNKQNDIAVIGEGVHTKFDEILV 260
Cdd:pfam00278 158 LNVVGVHFHIGSQITDLEPFVEALQRARELFDRLR-ELGIDLKLLDIGGGFGIPYRD-EPPPDFEEYAAAIREALDEYFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 261 PndlgDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVDASAVNLLRPAMYDAYHHI-TNMTNPNGDIQVVDVTGS 338
Cdd:pfam00278 236 P----DLEIIAEPGRYLVANAGVLVTRVIAVKTGGgKTFVIVDAGMNDLFRPALYDAYHPIpVVKEPGEGPLETYDVVGP 311
|
330 340
....*....|....*....|....*....
gi 2125487987 339 LCENNDKFAKNRELPEARIGDTLVIHDTG 367
Cdd:pfam00278 312 TCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
21-388 |
7.47e-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: 219.48 E-value: 7.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 21 TPFHLYDEKSIRETARAVNAAFswNPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTSND 100
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEAL--PSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 101 TRAEEFVYARDIN-ATINLDAYEDIFFLEEAA---GLPETLSLRFNPGgvFSLGTDIMDHP-EESKFGMTKEQLFKGYAY 175
Cdd:cd06810 79 KSVSEIEAALASGvDHIVVDSLDELERLNELAkklGPKARILLRVNPD--VSAGTHKISTGgLKSKFGLSLSEARAALER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 176 LKEKGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIkNELGVSLDFINLSGGVGVDYT--PANKQNDIAVIGEgvht 253
Cdd:cd06810 157 AKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEEL-VEMGFPLEMLDLGGGLGIPYDeqPLDFEEYAALINP---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 254 kFDEILVPNDlGDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVDASAVNLLRPAM-YDAYHHITNMTNPNGDIQ 331
Cdd:cd06810 232 -LLKKYFPND-PGVTLILEPGRYIVAQAGVLVTRVVAVKVNGgRFFAVVDGGMNHSFRPALaYDAYHPITPLKAPGPDEP 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2125487987 332 --VVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEILY 388
Cdd:cd06810 310 lvPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
22-387 |
3.08e-56 |
|
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: 189.57 E-value: 3.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 22 PFHLYDEKSIRETARAVNAAFSWNPGFkefFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKI--GFDSTAISFTSN 99
Cdd:cd06840 13 PCYVYDLETVRARARQVSALKAVDSLF---YAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 100 -DTRAE-EFVYARDINATIN----LDAYEDIFfleeaAGlpETLSLRFNPGGVFSLGTDIMDHPEESKFGMTKEQLFKGY 173
Cdd:cd06840 90 fAARSEyEQALELGVNVTVDnlhpLREWPELF-----RG--REVILRIDPGQGEGHHKHVRTGGPESKFGLDVDELDEAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 174 AYLKEKGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnelgvSLDFINLSGGVGVDYTPANKQNDIAVIGEGV-- 251
Cdd:cd06840 163 DLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDYLASLARHFP-----AVRILNVGGGLGIPEAPGGRPIDLDALDAALaa 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 252 ----HTKFDeilvpndlgdisIYTELGRFMTAPHGLVVTKVLHIKDTYR-RYVGVDASAVNLLRPAMYDAYHHITNMTN- 325
Cdd:cd06840 238 akaaHPQYQ------------LWMEPGRFIVAESGVLLARVTQIKHKDGvRFVGLETGMNSLIRPALYGAYHEIVNLSRl 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2125487987 326 ---PNGdiqVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEIL 387
Cdd:cd06840 306 depPAG---NADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYNLREPAEEVV 367
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
16-386 |
2.00e-54 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 193.76 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 16 TAEFPTPFHLYDEKSIRETARAVNAAFSWNPGFkefFAVKATPNPAILKILKEEGCGVDCATDTEL--VMSNKIGFDSTA 93
Cdd:PRK08961 498 LSDAGSPCYVYHLPTVRARARALAALAAVDQRF---YAIKANPHPAILRTLEEEGFGFECVSIGELrrVFELFPELSPER 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 94 ISFTSNDTRAEEFVYARDINATINLD------AYEDIFfleeaAGlpETLSLRFNPGgvfslgtdimdHPE--------- 158
Cdd:PRK08961 575 VLFTPNFAPRAEYEAAFALGVTVTLDnveplrNWPELF-----RG--REVWLRIDPG-----------HGDghhekvrtg 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 159 --ESKFGMTKEQLFKGYAYLKEKGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKnelgvSLDFINLSGGVGVDYT 236
Cdd:PRK08961 637 gkESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFP-----DVRTIDLGGGLGIPES 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 237 PANKQNDIAVIGEG------VHTKFDeilvpndlgdisIYTELGRFMTAPHGLVVTKVLHIKDTYR-RYVGVDASAVNLL 309
Cdd:PRK08961 712 AGDEPFDLDALDAGlaevkaQHPGYQ------------LWIEPGRYLVAEAGVLLARVTQVKEKDGvRRVGLETGMNSLI 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 310 RPAMYDAYHHITNMTN----PNGdiqVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAE 385
Cdd:PRK08961 780 RPALYGAYHEIVNLSRldepAAG---TADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPARE 856
|
.
gi 2125487987 386 I 386
Cdd:PRK08961 857 V 857
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
21-412 |
2.75e-54 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 185.38 E-value: 2.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 21 TPFHLYDEKSIRETARAVNAAFSwnpGFKEF--FAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTS 98
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALE---GLRSIigYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 99 NDTRAEEFVYARDINATINLDAYEDIFFLEEAA---GLPETLSLRFNPGgvfslgTDIMDHP------EESKFGMTKEQL 169
Cdd:PLN02537 95 NGKLLEDLVLAAQEGVFVNVDSEFDLENIVEAAriaGKKVNVLLRINPD------VDPQVHPyvatgnKNSKFGIRNEKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 170 --FKGYAYLKEKGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKNElGVSLDFINLSGGVGVDYTPAnkqndiavi 247
Cdd:PLN02537 169 qwFLDAVKAHPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQ-GFELSYLNIGGGLGIDYYHA--------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 248 GEGVHTKFDEILVPNDL---GDISIYTELGRFMTAPHGLVVTKVLHIK-DTYRRYVGVDASAVNLLRPAMYDAYHHI--T 321
Cdd:PLN02537 239 GAVLPTPRDLIDTVRELvlsRDLTLIIEPGRSLIANTCCFVNRVTGVKtNGTKNFIVIDGSMAELIRPSLYDAYQHIelV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 322 NMTNPNGDIQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSAEILYQEDGTARMIRRAE 401
Cdd:PLN02537 319 SPPPPDAEVSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITKIRHAE 398
|
410
....*....|.
gi 2125487987 402 TMNDYFATLDG 412
Cdd:PLN02537 399 TFDDHLRFFEG 409
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
15-372 |
3.05e-52 |
|
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: 179.33 E-value: 3.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 15 ITAEFPTPFHLYDEKSIRETARAVNAAFswNPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAI 94
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAAL--PPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 95 SFTS-NDTRAE-EFVYARDInATINLDAYEDIFFLEEAA---GLPETLSLRFNPGgvFSLGTDIMD---HPeeSKFGMTK 166
Cdd:cd06839 79 LFAGpGKSDAElRRAIEAGI-GTINVESLEELERIDALAeehGVVARVALRINPD--FELKGSGMKmggGP--SQFGIDV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 167 EQLFKGYAYLK-EKGVKSFGLHAFLASNTVTNEyypTLAAQL---FELAVEIKNELGVSLDFINLSGGVGVDYTPANKQN 242
Cdd:cd06839 154 EELPAVLARIAaLPNLRFVGLHIYPGTQILDAD---ALIEAFrqtLALALRLAEELGLPLEFLDLGGGFGIPYFPGETPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 243 DIAVIGEGVHTKFDEIlvPNDLGDISIYTELGRFMTAPHGLVVTKVLHIKDTY-RRYVGVD-------ASAVNLLRPAMY 314
Cdd:cd06839 231 DLEALGAALAALLAEL--GDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVSRgETFLVTDggmhhhlAASGNFGQVLRR 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2125487987 315 DAYHHITNMtNPNGDIQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFS 372
Cdd:cd06839 309 NYPLAILNR-MGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLS 365
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
17-392 |
5.67e-38 |
|
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: 141.25 E-value: 5.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 17 AEFPTPFHLYDEKSIRETARAVNAAFSWN-PGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAIS 95
Cdd:cd06841 3 ESYGSPFFVFDEDALRENYRELLGAFKKRyPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 96 FTSNDTRAEEFVYARDINATINLDAYEDIFFLEEAA---GLPETLSLRFNpggvFSLGTDIMdhpeeSKFGMTKEQLFKG 172
Cdd:cd06841 83 FNGPYKSKEELEKALEEGALINIDSFDELERILEIAkelGRVAKVGIRLN----MNYGNNVW-----SRFGFDIEENGEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 173 YAYLKE----KGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIkneLGVSLDFINLSGGVGVDYTPANKQN------ 242
Cdd:cd06841 154 LAALKKiqesKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRL---FGLELEYLDLGGGFPAKTPLSLAYPqedtvp 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 243 DIAVIGEGVHTKFDEILvPNDLGDISIYTELGRFMTAPHGLVVTKVLHIKDTYRRYVGVDASAVNLLRPAMYdaYHH--- 319
Cdd:cd06841 231 DPEDYAEAIASTLKEYY-ANKENKPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINNIPTIFW--YHHpil 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2125487987 320 ITNMTNPNGDIQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNgRLRSAEILYQEDG 392
Cdd:cd06841 308 VLRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQFI-RPRPAVYLIDNNG 379
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
25-384 |
3.34e-37 |
|
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: 139.07 E-value: 3.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 25 LYDEKSIRETARAVNAAFSwnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTSNDTRAE 104
Cdd:cd06836 7 LYDLDGFRALVARLTAAFP--APVLHTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 105 EFVYARDINATINLDAYEDIFFLEEA-AGLPETLS---LRFNP----GGVFSLGTDIMDhpeeSKFGM-----TKEQL-- 169
Cdd:cd06836 85 ELREALELGVAINIDNFQELERIDALvAEFKEASSrigLRVNPqvgaGKIGALSTATAT----SKFGValedgARDEIid 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 170 -FKGYAYLKekgvksfGLHAFLASNTVTNEYYPTLAAQLFELAVEIKNELGVS-LDFINLSGGVGVDY-----TPANKQN 242
Cdd:cd06836 161 aFARRPWLN-------GLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRVGRRqITRIDIGGGLPVNFesediTPTFADY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 243 dIAVIGEGVHTKFDeilvpndlGDISIYTELGRFMTAPHGLVVTKVLHIKDTYRRYVGVDASAVN-LLRPA-MYDAYHHI 320
Cdd:cd06836 234 -AAALKAAVPELFD--------GRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIAITHAGAQvATRTAyAPDDWPLR 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2125487987 321 TNMTNPNGD-----IQVVDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFSMGYNYNGRLRSA 384
Cdd:cd06836 305 VTVFDANGEpktgpEVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
21-379 |
1.19e-27 |
|
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: 112.59 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 21 TPFHLYDEKSIRETARAVNAAFswnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFtSND 100
Cdd:cd00622 2 TPFLVVDLGDVVRKYRRWKKAL---PRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIF-ANP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 101 TRAEEFV-YARDINatINL---DAYEDIFFLEEAAglPE-TLSLRF---NPGGVFSLGTdimdhpeesKFGMTKE---QL 169
Cdd:cd00622 78 CKSISDIrYAAELG--VRLftfDSEDELEKIAKHA--PGaKLLLRIatdDSGALCPLSR---------KFGADPEearEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 170 FKgyaYLKEKGVKSFGLH-----------AFLAsntvtneyYPTLAAQLFELAVEikneLGVSLDFINLSGGVGVDYTPA 238
Cdd:cd00622 145 LR---RAKELGLNVVGVSfhvgsqctdpsAYVD--------AIADAREVFDEAAE----LGFKLKLLDIGGGFPGSYDGV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 239 NkqNDIAVIGEGVHTKFDEILVPNDLGDISiytELGRFMTAPHGLVVTKVLHIK----DTYRRYVGVDASAVNLLRPAMY 314
Cdd:cd00622 210 V--PSFEEIAAVINRALDEYFPDEGVRIIA---EPGRYLVASAFTLAVNVIAKRkrgdDDRERWYYLNDGVYGSFNEILF 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2125487987 315 DAYH---HITNMTNPNGDIQVVDVTGSLCENNDKFAKNRELPEA-RIGDTLVIHDTGAHGFSMGYNYNG 379
Cdd:cd00622 285 DHIRyppRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEDlAVGDWLLFENMGAYTTAYASTFNG 353
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
20-372 |
3.47e-27 |
|
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: 111.60 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 20 PTPFHLYDEKSIRETARAVNAAFSwnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAIsFTSN 99
Cdd:cd06843 1 PLCAYVYDLAALRAHARALRASLP--PGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDAPLI-FGGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 100 DTRAEEFVYARDIN-ATINLDAYEDIFFLEEAA---GLPETLSLRFNPGGVFSLGTDIMDHPEESKFGMTKEQLFKGYAY 175
Cdd:cd06843 78 GKTDSELAQALAQGvERIHVESELELRRLNAVArraGRTAPVLLRVNLALPDLPSSTLTMGGQPTPFGIDEADLPDALEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 176 LKE-KGVKSFGLHAFLASNTVTNEYYPTLAAQLFELAVEIKNELGVSLDFINLSGGVGVDYTPANKQNDIAVIGEGVHTk 254
Cdd:cd06843 158 LRDlPNIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEHGLDLDVVNVGGGIGVNYADPEEQFDWAGFCEGLDQ- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 255 fdeiLVPNDLGDISIYTELGRFMTAPHGLVVTKVLHIKDTYRRYVGVDASAVNLLR-PAMYDAYH---HITNMTNPNGDI 330
Cdd:cd06843 237 ----LLAEYEPGLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRlPAAWGHNHpfsVLPVEEWPYPWP 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2125487987 331 QV------VDVTGSLCENNDKFAKNRELPEARIGDTLVIHDTGAHGFS 372
Cdd:cd06843 313 RPsvrdtpVTLVGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYGWN 360
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
30-279 |
6.70e-25 |
|
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: 101.97 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 30 SIRETARAVNAAFswnPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTSNDTRAEEFVYA 109
Cdd:pfam02784 3 SIERRHRRWKKAL---PRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 110 RDINAT-INLDAYEDIFFLEEAAGLPEtLSLRFNPGgvFSLGTdimdHPEESKFGMTKEQLFKGYAYL-KEKGVKSFGLH 187
Cdd:pfam02784 80 LEVGVGcVTVDNVDELEKLARLAPEAR-VLLRIKPD--DSAAT----CPLSSKFGADLDEDVEALLEAaKLLNLQVVGVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 188 AFLAS-NTVTNEYYPTL--AAQLFELAVeiknELGVSLDFINLSGGVGVDYTPANKQNDIAVIGEGVHTKFDEILVPNDl 264
Cdd:pfam02784 153 FHVGSgCTDAEAFVLALedARGVFDQGA----ELGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINEALEEYFPGDP- 227
|
250
....*....|....*
gi 2125487987 265 gDISIYTELGRFMTA 279
Cdd:pfam02784 228 -GVTIIAEPGRYFVA 241
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
31-248 |
2.33e-18 |
|
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: 83.14 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 31 IRETARAVNAAFswNPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFDSTAISFTSNDTRAEEFVYAR 110
Cdd:cd06808 1 IRHNYRRLREAA--PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 111 DINA-TINLDAYEDIFFLEEAAG-LPETLS--LRFNPGgvfslgtdimdhPEESKFGMTKEQLFKGYAYLKE-KGVKSFG 185
Cdd:cd06808 79 EQGViVVTVDSLEELEKLEEAALkAGPPARvlLRIDTG------------DENGKFGVRPEELKALLERAKElPHLRLVG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2125487987 186 LHAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDYTPANKQ--NDIAVIG 248
Cdd:cd06808 147 LHTHFGSADEDYSPFVEALSRFVAALDQLG-ELGIDLEQLSIGGSFAILYLQELPLgtFIIVEPG 210
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
12-241 |
1.47e-11 |
|
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: 65.75 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 12 LDQITAEFPTPFHLYDEKSIRETARAVNAAFS-WNPGFKEFFAVKATPNPAILKILKEEGCGVDCATDTELVMSNKIGFD 90
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDrHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 91 STAISFTSnDTRAEEFVY-ARDINATINLDAYEDIFFLEEAAGLPET----LSLRFNPggvfslgtdiMDHPEESKFGMT 165
Cdd:cd06842 81 GDRIVATG-PAKTDEFLWlAVRHGATIAVDSLDELDRLLALARGYTTgparVLLRLSP----------FPASLPSRFGMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 166 KE---QLFKGYAYLKEkGVKSFGLHAFLasntvtNEYYPT----LAAQLFELAVEIKnELGVSLDFINLSGGVGVDYTPA 238
Cdd:cd06842 150 AAevrTALERLAQLRE-RVRLVGFHFHL------DGYSAAqrvaALQECLPLIDRAR-ALGLAPRFIDIGGGFPVSYLAD 221
|
...
gi 2125487987 239 NKQ 241
Cdd:cd06842 222 AAE 224
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
104-298 |
2.93e-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: 61.43 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 104 EEFV----YARDI--NATINLDAYEDIF-FLEEAAGLPE--TLSLRF----NPGGVFSlgtdiMDHPEESKFGMTKEQLF 170
Cdd:cd06830 98 DEYIelalLARKLghNVIIVIEKLSELDlILELAKKLGVkpLLGVRIklasKGSGKWQ-----ESGGDRSKFGLTASEIL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 171 KGYAYLKEKGVK-SFGL-HAFLASNTVTNEYYPTLAAQLFELAVEIKnELGVSLDFINLSGGVGVDYTPANKQNDIAV-- 246
Cdd:cd06830 173 EVVEKLKEAGMLdRLKLlHFHIGSQITDIRRIKSALREAARIYAELR-KLGANLRYLDIGGGLGVDYDGSRSSSDSSFny 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2125487987 247 --------IGEGVHTKFDE--ILVPNdlgdisIYTELGRFMTAPHGLVVTKVLHIKDTYRRY 298
Cdd:cd06830 252 sleeyandIVKTVKEICDEagVPHPT------IVTESGRAIVAHHSVLIFEVLGVKRLADWY 307
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
158-289 |
4.02e-06 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 48.96 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125487987 158 EESKFGMTKEQLFKGYAYLKEKG-VKSFGL-HAFLASNtVTN---------EyyptlAAQLF-ELAveiknELGVSLDFI 225
Cdd:PRK05354 219 EKSKFGLSATEVLEAVERLREAGlLDCLQLlHFHLGSQ-IANirdiktavrE-----AARFYvELR-----KLGAPIQYL 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2125487987 226 NLSGGVGVDYTPANKQND--------------IAVIGEGVHTKfdEILVPNdlgdisIYTELGRFMTAPHGLVVTKVL 289
Cdd:PRK05354 288 DVGGGLGVDYDGTRSQSDssvnyslqeyandvVYTLKEICEEH--GVPHPT------IISESGRALTAHHAVLVFNVL 357
|
|
| |
