|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
22-395 |
1.26e-122 |
|
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: 360.26 E-value: 1.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 22 FGSPVYVYDMATLKANAADVLAFPNAYGLTARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISLSTQ 101
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 102 ELPT-DFAELYELGI-EINACSLSQLERFGQAFP----GRSIGVRFNPGAGSGGNNRTNVGGPASSFGIWHEWIDQVQEI 175
Cdd:cd06828 81 GKSDeELELALELGIlRINVDSLSELERLGEIAPelgkGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 176 VAR-YDLKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQ----FPDVVSLNLGGGYKVARMADEVSTDLQQCGEPVADKF 249
Cdd:cd06828 161 AKElPGLKLVGLHCHIGSQiLDLEPFVEAAEKLLDLAAElrelGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 250 REFaAETGREIRLEIEPGTYLLANACSVLSMVQDKVSTGreGYEFLKLNTGMTEVLRPSIYGAQHPIFILKEATPTETCD 329
Cdd:cd06828 241 KEL-CEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETG--GKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETEK 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502808573 330 YMIAGHCCESGDILTPAsgdpellatRTLPVTEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEVML 395
Cdd:cd06828 318 VDVVGPICESGDVFAKD---------RELPEVEEGDLLAIHDAGAYGYSMSS-NYNSRPRPAEVLV 373
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
1-418 |
4.63e-118 |
|
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: 350.22 E-value: 4.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 1 MTDFTK--PRFLQYTTARQIADQFGSPVYVYDMATLKANAADVLAFPNAYGLTARYAMKASPNAAILRIFNEAGLHIDAS 78
Cdd:COG0019 1 MTHFARdgELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 79 SGYEVRRAIAAGYTPEKISLS----TQElptDFAELYELGIE-INACSLSQLERFGQAFPGR----SIGVRFNPGAGSGG 149
Cdd:COG0019 81 SGGELRLALAAGFPPERIVFSgngkSEE---ELEEALELGVGhINVDSLSELERLAELAAELgkraPVGLRVNPGVDAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 150 NNRTNVGGPASSFGIWHEWIDQVQEIVARYD-LKVIRIHTHIGSGS-DPKVWQKISSMSLELVRQFP----DVVSLNLGG 223
Cdd:COG0019 158 HEYISTGGKDSKFGIPLEDALEAYRRAAALPgLRLVGLHFHIGSQIlDLEPFEEALERLLELAEELRelgiDLEWLDLGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 224 GYKVARMADEVSTDLQQCGEPVADKFREFAaetGREIRLEIEPGTYLLANACSVLSMVQDKVSTGreGYEFLKLNTGMTE 303
Cdd:COG0019 238 GLGIPYTEGDEPPDLEELAAAIKEALEELC---GLGPELILEPGRALVGNAGVLLTRVLDVKENG--GRRFVIVDAGMND 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 304 VLRPSIYGAQHPIFILKEATPTETCDYMIAGHCCESGDILtpasGDPellatRTLPVTEIGDLCVIDGSGAYCSAMSTkN 383
Cdd:COG0019 313 LMRPALYGAYHPIVPVGRPSGAEAETYDVVGPLCESGDVL----GKD-----RSLPPLEPGDLLAFLDAGAYGFSMAS-N 382
|
410 420 430
....*....|....*....|....*....|....*
gi 502808573 384 YNSYPEAAEVMLDEaNRPHLIRKRQDPQALWANEL 418
Cdd:COG0019 383 YNGRPRPAEVLVDD-GEARLIRRRETYEDLLASEV 416
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
15-418 |
1.40e-78 |
|
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: 249.13 E-value: 1.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 15 ARQIADQFGSPVYVYDMATLKANAADVL-AFPNAYGLtaRYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTP 93
Cdd:TIGR01048 16 LLELAQEFGTPLYVYDEDTIRRRFRAYKeAFGGRSLV--CYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 94 EKISL-----STQELptdfAELYELGIEINACSLSQLERFGQAFPGRS----IGVRFNPGAGSGGNNRTNVGGPASSFGI 164
Cdd:TIGR01048 94 EKIVFsgngkSRAEL----ERALELGICINVDSFSELERLNEIAPELGkkarISLRVNPGVDAKTHPYISTGLKDSKFGI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 165 WHEWIDQVQEIVARYD-LKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQFPDVVSL---NLGGGYKVARMADEVSTDLQ 239
Cdd:TIGR01048 170 DVEEALEAYLYALQLPhLELVGIHCHIGSQiTDLSPFVEAAEKVVKLAESLAEGIDLeflDLGGGLGIPYTPEEEPPDLS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 240 QCGEPVADKFREfAAETGREIRLEIEPGTYLLANACSVLSMVQ-DKVSTGREgyeFLKLNTGMTEVLRPSIYGAQHPIFI 318
Cdd:TIGR01048 250 EYAQAILNALEG-YADLGLDPKLILEPGRSIVANAGVLLTRVGfVKETGSRN---FVIVDAGMNDLIRPALYGAYHHIIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 319 LKE--ATPTETCDymIAGHCCESGDILTPAsgdpellatRTLPVTEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEVMLD 396
Cdd:TIGR01048 326 LNRtnDAPTEVAD--VVGPVCESGDVLAKD---------RELPEVEPGDLLAVFDAGAYGFSMSS-NYNSRPRPAEVLVD 393
|
410 420
....*....|....*....|..
gi 502808573 397 EaNRPHLIRKRQDPQALWANEL 418
Cdd:TIGR01048 394 G-GQARLIRRRETYEDLWALEV 414
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
26-373 |
4.24e-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: 227.37 E-value: 4.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 26 VYVYDMATLKANAADVL-AFPNayGLTARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISLS----T 100
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKaALPP--RVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAgpgkT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 101 QElptDFAELYELGIE-INACSLSQLERFGQAFPGR--SIGVRFNPGAGSGGNNrTNVGGPASSFGIWHEWIDQVQEIVA 177
Cdd:pfam00278 79 DS---EIRYALEAGVLcFNVDSEDELEKIAKLAPELvaRVALRINPDVDAGTHK-ISTGGLSSKFGIDLEDAPELLALAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 178 RYDLKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQFP----DVVSLNLGGGYKVARmADEVSTDLQQCGEPVADKFREF 252
Cdd:pfam00278 155 ELGLNVVGVHFHIGSQiTDLEPFVEALQRARELFDRLRelgiDLKLLDIGGGFGIPY-RDEPPPDFEEYAAAIREALDEY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 253 aaeTGREIRLEIEPGTYLLANACSVLSMVQDKVSTGREgyEFLKLNTGMTEVLRPSIYGAQHPIFILKEATPTETCDYMI 332
Cdd:pfam00278 234 ---FPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGK--TFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETYDV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 502808573 333 AGHCCESGDILTPAsgdpellatRTLPVTEIGDLCVIDGSG 373
Cdd:pfam00278 309 VGPTCESGDVLAKD---------RELPELEVGDLLAFEDAG 340
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
23-396 |
1.07e-64 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 222.26 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 23 GSPVYVYDMATLKANAADVLAFPnayGLTAR-YAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAA--GYTPEKIsLS 99
Cdd:PRK08961 502 GSPCYVYHLPTVRARARALAALA---AVDQRfYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERV-LF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 100 TQEL--PTDFAELYELGIEINACSLSQLERFGQAFPGRSIGVRFNPGAGSGGNNRTNVGGPASSFGIWHEWIDQVQEIVA 177
Cdd:PRK08961 578 TPNFapRAEYEAAFALGVTVTLDNVEPLRNWPELFRGREVWLRIDPGHGDGHHEKVRTGGKESKFGLSQTRIDEFVDLAK 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 178 RYDLKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQFPDVVSLNLGGGYKVARMADEVSTDLQQCGEPVAdkfrEFAAET 256
Cdd:PRK08961 658 TLGITVVGLHAHLGSGiETGEHWRRMADELASFARRFPDVRTIDLGGGLGIPESAGDEPFDLDALDAGLA----EVKAQH 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 257 GReIRLEIEPGTYLLANACSVLSMVQDKVSTGreGYEFLKLNTGMTEVLRPSIYGAQHPIFILK--EATPTETCDymIAG 334
Cdd:PRK08961 734 PG-YQLWIEPGRYLVAEAGVLLARVTQVKEKD--GVRRVGLETGMNSLIRPALYGAYHEIVNLSrlDEPAAGTAD--VVG 808
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502808573 335 HCCESGDILTpasgdpellATRTLPVTEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEVMLD 396
Cdd:PRK08961 809 PICESSDVLG---------KRRRLPATAEGDVILIANAGAYGYSMSS-TYNLREPAREVVLD 860
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
22-395 |
1.26e-122 |
|
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: 360.26 E-value: 1.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 22 FGSPVYVYDMATLKANAADVLAFPNAYGLTARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISLSTQ 101
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 102 ELPT-DFAELYELGI-EINACSLSQLERFGQAFP----GRSIGVRFNPGAGSGGNNRTNVGGPASSFGIWHEWIDQVQEI 175
Cdd:cd06828 81 GKSDeELELALELGIlRINVDSLSELERLGEIAPelgkGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 176 VAR-YDLKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQ----FPDVVSLNLGGGYKVARMADEVSTDLQQCGEPVADKF 249
Cdd:cd06828 161 AKElPGLKLVGLHCHIGSQiLDLEPFVEAAEKLLDLAAElrelGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEAIAEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 250 REFaAETGREIRLEIEPGTYLLANACSVLSMVQDKVSTGreGYEFLKLNTGMTEVLRPSIYGAQHPIFILKEATPTETCD 329
Cdd:cd06828 241 KEL-CEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETG--GKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETEK 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502808573 330 YMIAGHCCESGDILTPAsgdpellatRTLPVTEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEVML 395
Cdd:cd06828 318 VDVVGPICESGDVFAKD---------RELPEVEEGDLLAIHDAGAYGYSMSS-NYNSRPRPAEVLV 373
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
1-418 |
4.63e-118 |
|
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: 350.22 E-value: 4.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 1 MTDFTK--PRFLQYTTARQIADQFGSPVYVYDMATLKANAADVLAFPNAYGLTARYAMKASPNAAILRIFNEAGLHIDAS 78
Cdd:COG0019 1 MTHFARdgELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 79 SGYEVRRAIAAGYTPEKISLS----TQElptDFAELYELGIE-INACSLSQLERFGQAFPGR----SIGVRFNPGAGSGG 149
Cdd:COG0019 81 SGGELRLALAAGFPPERIVFSgngkSEE---ELEEALELGVGhINVDSLSELERLAELAAELgkraPVGLRVNPGVDAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 150 NNRTNVGGPASSFGIWHEWIDQVQEIVARYD-LKVIRIHTHIGSGS-DPKVWQKISSMSLELVRQFP----DVVSLNLGG 223
Cdd:COG0019 158 HEYISTGGKDSKFGIPLEDALEAYRRAAALPgLRLVGLHFHIGSQIlDLEPFEEALERLLELAEELRelgiDLEWLDLGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 224 GYKVARMADEVSTDLQQCGEPVADKFREFAaetGREIRLEIEPGTYLLANACSVLSMVQDKVSTGreGYEFLKLNTGMTE 303
Cdd:COG0019 238 GLGIPYTEGDEPPDLEELAAAIKEALEELC---GLGPELILEPGRALVGNAGVLLTRVLDVKENG--GRRFVIVDAGMND 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 304 VLRPSIYGAQHPIFILKEATPTETCDYMIAGHCCESGDILtpasGDPellatRTLPVTEIGDLCVIDGSGAYCSAMSTkN 383
Cdd:COG0019 313 LMRPALYGAYHPIVPVGRPSGAEAETYDVVGPLCESGDVL----GKD-----RSLPPLEPGDLLAFLDAGAYGFSMAS-N 382
|
410 420 430
....*....|....*....|....*....|....*
gi 502808573 384 YNSYPEAAEVMLDEaNRPHLIRKRQDPQALWANEL 418
Cdd:COG0019 383 YNGRPRPAEVLVDD-GEARLIRRRETYEDLLASEV 416
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
15-418 |
1.40e-78 |
|
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: 249.13 E-value: 1.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 15 ARQIADQFGSPVYVYDMATLKANAADVL-AFPNAYGLtaRYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTP 93
Cdd:TIGR01048 16 LLELAQEFGTPLYVYDEDTIRRRFRAYKeAFGGRSLV--CYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 94 EKISL-----STQELptdfAELYELGIEINACSLSQLERFGQAFPGRS----IGVRFNPGAGSGGNNRTNVGGPASSFGI 164
Cdd:TIGR01048 94 EKIVFsgngkSRAEL----ERALELGICINVDSFSELERLNEIAPELGkkarISLRVNPGVDAKTHPYISTGLKDSKFGI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 165 WHEWIDQVQEIVARYD-LKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQFPDVVSL---NLGGGYKVARMADEVSTDLQ 239
Cdd:TIGR01048 170 DVEEALEAYLYALQLPhLELVGIHCHIGSQiTDLSPFVEAAEKVVKLAESLAEGIDLeflDLGGGLGIPYTPEEEPPDLS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 240 QCGEPVADKFREfAAETGREIRLEIEPGTYLLANACSVLSMVQ-DKVSTGREgyeFLKLNTGMTEVLRPSIYGAQHPIFI 318
Cdd:TIGR01048 250 EYAQAILNALEG-YADLGLDPKLILEPGRSIVANAGVLLTRVGfVKETGSRN---FVIVDAGMNDLIRPALYGAYHHIIV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 319 LKE--ATPTETCDymIAGHCCESGDILTPAsgdpellatRTLPVTEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEVMLD 396
Cdd:TIGR01048 326 LNRtnDAPTEVAD--VVGPVCESGDVLAKD---------RELPEVEPGDLLAVFDAGAYGFSMSS-NYNSRPRPAEVLVD 393
|
410 420
....*....|....*....|..
gi 502808573 397 EaNRPHLIRKRQDPQALWANEL 418
Cdd:TIGR01048 394 G-GQARLIRRRETYEDLWALEV 414
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
26-373 |
4.24e-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: 227.37 E-value: 4.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 26 VYVYDMATLKANAADVL-AFPNayGLTARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISLS----T 100
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKaALPP--RVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAgpgkT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 101 QElptDFAELYELGIE-INACSLSQLERFGQAFPGR--SIGVRFNPGAGSGGNNrTNVGGPASSFGIWHEWIDQVQEIVA 177
Cdd:pfam00278 79 DS---EIRYALEAGVLcFNVDSEDELEKIAKLAPELvaRVALRINPDVDAGTHK-ISTGGLSSKFGIDLEDAPELLALAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 178 RYDLKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQFP----DVVSLNLGGGYKVARmADEVSTDLQQCGEPVADKFREF 252
Cdd:pfam00278 155 ELGLNVVGVHFHIGSQiTDLEPFVEALQRARELFDRLRelgiDLKLLDIGGGFGIPY-RDEPPPDFEEYAAAIREALDEY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 253 aaeTGREIRLEIEPGTYLLANACSVLSMVQDKVSTGREgyEFLKLNTGMTEVLRPSIYGAQHPIFILKEATPTETCDYMI 332
Cdd:pfam00278 234 ---FPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGK--TFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLETYDV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 502808573 333 AGHCCESGDILTPAsgdpellatRTLPVTEIGDLCVIDGSG 373
Cdd:pfam00278 309 VGPTCESGDVLAKD---------RELPELEVGDLLAFEDAG 340
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
23-396 |
1.07e-64 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 222.26 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 23 GSPVYVYDMATLKANAADVLAFPnayGLTAR-YAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAA--GYTPEKIsLS 99
Cdd:PRK08961 502 GSPCYVYHLPTVRARARALAALA---AVDQRfYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERV-LF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 100 TQEL--PTDFAELYELGIEINACSLSQLERFGQAFPGRSIGVRFNPGAGSGGNNRTNVGGPASSFGIWHEWIDQVQEIVA 177
Cdd:PRK08961 578 TPNFapRAEYEAAFALGVTVTLDNVEPLRNWPELFRGREVWLRIDPGHGDGHHEKVRTGGKESKFGLSQTRIDEFVDLAK 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 178 RYDLKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQFPDVVSLNLGGGYKVARMADEVSTDLQQCGEPVAdkfrEFAAET 256
Cdd:PRK08961 658 TLGITVVGLHAHLGSGiETGEHWRRMADELASFARRFPDVRTIDLGGGLGIPESAGDEPFDLDALDAGLA----EVKAQH 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 257 GReIRLEIEPGTYLLANACSVLSMVQDKVSTGreGYEFLKLNTGMTEVLRPSIYGAQHPIFILK--EATPTETCDymIAG 334
Cdd:PRK08961 734 PG-YQLWIEPGRYLVAEAGVLLARVTQVKEKD--GVRRVGLETGMNSLIRPALYGAYHEIVNLSrlDEPAAGTAD--VVG 808
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502808573 335 HCCESGDILTpasgdpellATRTLPVTEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEVMLD 396
Cdd:PRK08961 809 PICESSDVLG---------KRRRLPATAEGDVILIANAGAYGYSMSS-TYNLREPAREVVLD 860
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
15-395 |
1.98e-61 |
|
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: 203.05 E-value: 1.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 15 ARQIADQFGsPVYVYDMATLKANAADVlafPNAYGLTAR-YAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAA--GY 91
Cdd:cd06840 4 LLRLAPDVG-PCYVYDLETVRARARQV---SALKAVDSLfYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 92 TPEKIsLSTQEL--PTDFAELYELGIEINACSLSQLERFGQAFPGRSIGVRFNPGAGSGGNNRTNVGGPASSFGIWHEWI 169
Cdd:cd06840 80 DPRRV-LFTPNFaaRSEYEQALELGVNVTVDNLHPLREWPELFRGREVILRIDPGQGEGHHKHVRTGGPESKFGLDVDEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 170 DQVQEIVARYDLKVIRIHTHIGSG-SDPKVWQKISSMSLELVRQFPDVVSLNLGGGYKVARMADEVSTDLQQCGEPVADK 248
Cdd:cd06840 159 DEARDLAKKAGIIVIGLHAHSGSGvEDTDHWARHGDYLASLARHFPAVRILNVGGGLGIPEAPGGRPIDLDALDAALAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 249 FREFAaetgrEIRLEIEPGTYLLANACSVLSMVQDKVSTGreGYEFLKLNTGMTEVLRPSIYGAQHPIFILK--EATPTE 326
Cdd:cd06840 239 KAAHP-----QYQLWMEPGRFIVAESGVLLARVTQIKHKD--GVRFVGLETGMNSLIRPALYGAYHEIVNLSrlDEPPAG 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502808573 327 TCDymIAGHCCESGDILTpasgdpellATRTLPVTEIGDLCVIDGSGAYCSAMSTKnYNSYPEAAEVML 395
Cdd:cd06840 312 NAD--VVGPICESGDVLG---------RDRLLPETEEGDVILIANAGAYGFCMAST-YNLREPAEEVVL 368
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
24-393 |
7.53e-59 |
|
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: 196.37 E-value: 7.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 24 SPVYVYDMATLKANAADVLAFPNAyGLTARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISLSTqel 103
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPS-GVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 104 PTDFAELYELGIEINAC-----SLSQLERFGQAFPGR----SIGVRFNPGAGSGGNNrTNVGGPASSFGIWHEWIDQVQE 174
Cdd:cd06810 77 PAKSVSEIEAALASGVDhivvdSLDELERLNELAKKLgpkaRILLRVNPDVSAGTHK-ISTGGLKSKFGLSLSEARAALE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 175 IVARYDLKVIRIHTHIGSGSdpKVWQKISSMSLELVRQF-------PDVVSLNLGGGYKVARMADEVSTdlqqcgEPVAD 247
Cdd:cd06810 156 RAKELDLRLVGLHFHVGSQI--LDLETIVQALSDARELIeelvemgFPLEMLDLGGGLGIPYDEQPLDF------EEYAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 248 KFREFAAETGRE---IRLEIEPGTYLLANACSVLSMVQDKVStgREGYEFLKLNTGMTEVLRPSI-YGAQHPIFILKEA- 322
Cdd:cd06810 228 LINPLLKKYFPNdpgVTLILEPGRYIVAQAGVLVTRVVAVKV--NGGRFFAVVDGGMNHSFRPALaYDAYHPITPLKAPg 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502808573 323 --TPTETCDymIAGHCCESGDILTPASGDPELlatrtlpvtEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEV 393
Cdd:cd06810 306 pdEPLVPAT--LAGPLCDSGDVIGRDRLLPEL---------EVGDLLVFEDMGAYGFSESS-NFNSHPRPAEY 366
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
18-395 |
2.41e-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: 147.74 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 18 IADQFGSPVYVYDMATLKANAADV-LAFPNAYGLtaRYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKI 96
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALrAALPPAIEI--YYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 97 SL-----STQELptdfAELYELGI-EINACSLSQLERFGQAFP--GR--SIGVRFNPGAGSGGnNRTNVGGPASSFGIWH 166
Cdd:cd06839 79 LFagpgkSDAEL----RRAIEAGIgTINVESLEELERIDALAEehGVvaRVALRINPDFELKG-SGMKMGGGPSQFGIDV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 167 EWIDQV-QEIVARYDLKVIRIHTHIGS-GSDPKV----WQKISSMSLELVRQFPDVVS-LNLGGGYKVARMADEVSTDLQ 239
Cdd:cd06839 154 EELPAVlARIAALPNLRFVGLHIYPGTqILDADAlieaFRQTLALALRLAEELGLPLEfLDLGGGFGIPYFPGETPLDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 240 QCGE---PVADKFREFAAETgreiRLEIEPGTYLLANACSVLSMVQD-KVSTGRegyEFLKLNTGMTEVLRPSIYGAQH- 314
Cdd:cd06839 234 ALGAalaALLAELGDRLPGT----RVVLELGRYLVGEAGVYVTRVLDrKVSRGE---TFLVTDGGMHHHLAASGNFGQVl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 315 ----PIFILKEATPTETCDYMIAGHCCESGDILTPASgdpellatrTLPVTEIGDLCVIDGSGAYCSAMSTKNYNSYPEA 390
Cdd:cd06839 307 rrnyPLAILNRMGGEERETVTVVGPLCTPLDLLGRNV---------ELPPLEPGDLVAVLQSGAYGLSASPLAFLSHPAP 377
|
....*
gi 502808573 391 AEVML 395
Cdd:cd06839 378 AEVLV 382
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
24-405 |
9.90e-30 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 119.13 E-value: 9.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 24 SPVYVYDMATLKANaadVLAFPNAY-GLTA--RYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEK-ISLS 99
Cdd:PLN02537 18 RPFYLYSKPQITRN---YEAYKEALeGLRSiiGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRcIFNG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 100 TQELPTDFAELYELGIEINACSLSQLERFGQA--FPGRSIGV--RFNPGAGSGGNNRTNVGGPASSFGIWHEWIDQVQEI 175
Cdd:PLN02537 95 NGKLLEDLVLAAQEGVFVNVDSEFDLENIVEAarIAGKKVNVllRINPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 176 VARY--DLKVIRIHTHIGSG-SDPKVWQKISSMSLELV----RQFPDVVSLNLGGG----YKVARMADEVSTDLqqcgep 244
Cdd:PLN02537 175 VKAHpnELKLVGAHCHLGSTiTKVDIFRDAAVLMVNYVdeirAQGFELSYLNIGGGlgidYYHAGAVLPTPRDL------ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 245 vADKFREFAAEtgREIRLEIEPGTYLLANACSVLSMVQDKVSTGREgyEFLKLNTGMTEVLRPSIYGA-QHPIFILKEAT 323
Cdd:PLN02537 249 -IDTVRELVLS--RDLTLIIEPGRSLIANTCCFVNRVTGVKTNGTK--NFIVIDGSMAELIRPSLYDAyQHIELVSPPPP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 324 PTETCDYMIAGHCCESGDILTpasgdpellATRTLPVTEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEVMLDEANRPHL 403
Cdd:PLN02537 324 DAEVSTFDVVGPVCESADFLG---------KDRELPTPPKGAGLVVHDAGAYCMSMAS-TYNLKMRPPEYWVEEDGSITK 393
|
..
gi 502808573 404 IR 405
Cdd:PLN02537 394 IR 395
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
26-391 |
3.69e-29 |
|
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: 117.11 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 26 VYVYDMATLKANAADVL-AFPnAYGLTArYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISL-STQEL 103
Cdd:cd06836 5 VGLYDLDGFRALVARLTaAFP-APVLHT-FAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFdSPAKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 104 PTDFAELYELGIEINACSLSQLERF-----GQAFPGRSIGVRFNPGAGSGGNNRTNVGGPASSFGIWHEwIDQVQEIVAR 178
Cdd:cd06836 83 RAELREALELGVAINIDNFQELERIdalvaEFKEASSRIGLRVNPQVGAGKIGALSTATATSKFGVALE-DGARDEIIDA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 179 YD----LKviRIHTHIGSGSDP-----KVWQKISSMSLELVRQFPD--VVSLNLGGGYKVARMADEVSTDLQQcgepVAD 247
Cdd:cd06836 162 FArrpwLN--GLHVHVGSQGCElsllaEGIRRVVDLAEEINRRVGRrqITRIDIGGGLPVNFESEDITPTFAD----YAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 248 KFREFAAE--TGReIRLEIEPGTYLLANACSVLSMVQ-DKVSTGRE------GYEFLKLNTGMTEV--LRPSIYGAQ-HP 315
Cdd:cd06836 236 ALKAAVPElfDGR-YQLVTEFGRSLLAKCGTIVSRVEyTKSSGGRRiaithaGAQVATRTAYAPDDwpLRVTVFDANgEP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502808573 316 ifilkEATPTETCDymIAGHCCESGDILtpASGdpellatRTLPVTEIGDLCVIDGSGAYCSAMSTKnYNSYPEAA 391
Cdd:cd06836 315 -----KTGPEVVTD--VAGPCCFAGDVL--AKE-------RALPPLEPGDYVAVHDTGAYYFSSHSS-YNSLPRPA 373
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
18-397 |
3.88e-26 |
|
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: 108.50 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 18 IADQFGSPVYVYDMATLKANAADVL-AFPNAYGLT-ARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEK 95
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLgAFKKRYPNVvIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 96 I----SLSTQElptDFAELYELGIEINACSLSQLERFGQ--AFPGR--SIGVRFNpgagsggnnrTNVG-GPASSFGI-- 164
Cdd:cd06841 81 IifngPYKSKE---ELEKALEEGALINIDSFDELERILEiaKELGRvaKVGIRLN----------MNYGnNVWSRFGFdi 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 165 --WHEWIDQVQEIVARYDLKVIRIHTHIGS-GSDPKVWQKISSMSLELVRQFPDVVS--LNLGGGY------KVARMADE 233
Cdd:cd06841 148 eeNGEALAALKKIQESKNLSLVGLHCHVGSnILNPEAYSAAAKKLIELLDRLFGLELeyLDLGGGFpaktplSLAYPQED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 234 VSTDLQQCGEPVADKFREFAAETGREIRLEIEPGTYLLANACSVLSMVqdkVST-GREGYEFLKLNTGMTEVlrPSIYGA 312
Cdd:cd06841 228 TVPDPEDYAEAIASTLKEYYANKENKPKLILEPGRALVDDAGYLLGRV---VAVkNRYGRNIAVTDAGINNI--PTIFWY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 313 QHPIFILKE-ATPTETCDYMIAGHCCESGDILTPAsgdpellatRTLPVTEIGDLCVIDGSGAYCsaMSTKNYNSYPEAA 391
Cdd:cd06841 303 HHPILVLRPgKEDPTSKNYDVYGFNCMESDVLFPN---------VPLPPLNVGDILAIRNVGAYN--MTQSNQFIRPRPA 371
|
....*.
gi 502808573 392 EVMLDE 397
Cdd:cd06841 372 VYLIDN 377
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
23-393 |
4.05e-26 |
|
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: 108.35 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 23 GSPVYVYDMATLKANAADVL-AFPNAyglTARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISLS-T 100
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKkALPRV---RPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFAnP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 101 QELPTDFAELYELGIEINAC-SLSQLERFGQAFPGRSIGVRF---NPGAgsggnnRTNVGGpasSFGIWHEWIDQVQEIV 176
Cdd:cd00622 78 CKSISDIRYAAELGVRLFTFdSEDELEKIAKHAPGAKLLLRIatdDSGA------LCPLSR---KFGADPEEARELLRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 177 ARYDLKVIRIHTHIGSGS-DPKVW----QKISSMSLELVRQFPDVVSLNLGGGYKVARmaDEVSTDLQQCGEPVADKFRE 251
Cdd:cd00622 149 KELGLNVVGVSFHVGSQCtDPSAYvdaiADAREVFDEAAELGFKLKLLDIGGGFPGSY--DGVVPSFEEIAAVINRALDE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 252 FAAETGreIRLEIEPGTYLLANACSVLSMVQDKVSTGREGYEF-LKLNTG----MTEVLrpsiYGAQHPIFIL--KEATP 324
Cdd:cd00622 227 YFPDEG--VRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERwYYLNDGvygsFNEIL----FDHIRYPPRVlkDGGRD 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502808573 325 TETCDYMIAGHCCESGDILTPASGDPELLatrtlpvtEIGDLCVIDGSGAYCSAMSTkNYNSYPEAAEV 393
Cdd:cd00622 301 GELYPSSLWGPTCDSLDVIYEDVLLPEDL--------AVGDWLLFENMGAYTTAYAS-TFNGFPPPKIV 360
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
53-272 |
7.75e-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: 85.03 E-value: 7.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 53 RYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISLS----TQElptDFAELYELGIE-INACSLSQLER 127
Cdd:pfam02784 21 FYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFAnpckQRS---FLRYALEVGVGcVTVDNVDELEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 128 FGQAFPGRSIGVRFNPGAGSGgnnrtnvGGPASS-FGIW-HEWIDQVQEIVARYDLKVIRIHTHIGSG-SDPKVWQKiss 204
Cdd:pfam02784 98 LARLAPEARVLLRIKPDDSAA-------TCPLSSkFGADlDEDVEALLEAAKLLNLQVVGVSFHVGSGcTDAEAFVL--- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502808573 205 mSLELVRQFPDVVS--------LNLGGGYKVARMADEVSTDLQQCGEPVADKFREFAAEtGREIRLEIEPGTYLLA 272
Cdd:pfam02784 168 -ALEDARGVFDQGAelgfnlkiLDLGGGFGVDYTEGEEPLDFEEYANVINEALEEYFPG-DPGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
25-375 |
1.75e-16 |
|
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: 80.40 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 25 PVYVYDMATLKANAADVLAfpnayGLTAR----YAMKASPNAAILRIFNEaglHID---ASSGYEVRRAIAAGYTPEKIS 97
Cdd:cd06843 3 CAYVYDLAALRAHARALRA-----SLPPGcelfYAIKANSDPPILRALAP---HVDgfeVASGGEIAHVRAAVPDAPLIF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 98 LSTQELPTDFAELYELGIE-INACSLSQLERFGQ--AFPGRSIGV--RFNPGAGSGGNNRTNVGGPASSFGIWHEWIDQV 172
Cdd:cd06843 75 GGPGKTDSELAQALAQGVErIHVESELELRRLNAvaRRAGRTAPVllRVNLALPDLPSSTLTMGGQPTPFGIDEADLPDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 173 QEIVARYD-LKVIRIHTHIGSGS-DPKVWQKISSMSLELVRQFP-----DVVSLNLGGGYKVARMADEVSTDLqqcgEPV 245
Cdd:cd06843 155 LELLRDLPnIRLRGFHFHLMSHNlDAAAHLALVKAYLETARQWAaehglDLDVVNVGGGIGVNYADPEEQFDW----AGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 246 ADKFREFAAETGREIRLEIEPGTYLLAnACSVLSM-VQDKVSTGREGYEFLKlntGMTEVLR-PSIYGAQHPIFILkeat 323
Cdd:cd06843 231 CEGLDQLLAEYEPGLTLRFECGRYISA-YCGYYVTeVLDLKRSHGEWFAVLR---GGTHHFRlPAAWGHNHPFSVL---- 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 324 PTETCDYMIAGHCCESGDI------LTPAsgdpELLAtRTLPVTEI--GDLCVIDGSGAY 375
Cdd:cd06843 303 PVEEWPYPWPRPSVRDTPVtlvgqlCTPK----DVLA-RDVPVDRLraGDLVVFPLAGAY 357
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
24-375 |
7.94e-15 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.
Pssm-ID: 143502 [Multi-domain] Cd Length: 346 Bit Score: 75.28 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 24 SPVYVYDMATLKAN---AADVLAfpnAYGLTARYAMKASPNAAILRIFNEAGLHIDASSGYEVR----------RAIAAG 90
Cdd:cd06829 1 TPCYVLDEAKLRRNleiLKRVQE---RSGAKILLALKAFSMWSVFPLIREYLDGTTASSLFEARlgreefggevHTYSPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 91 YTPEkislstqelptDFAELYELGIEINACSLSQLERFGQ--AFPGRSIGVRFNPGAGSGGNNRTNVGGPASSFGIwheW 168
Cdd:cd06829 78 YRDD-----------EIDEILRLADHIIFNSLSQLERFKDraKAAGISVGLRINPEYSEVETDLYDPCAPGSRLGV---T 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 169 IDQVQEiVARYDLKVIRIHTHIGSGSDP--KVWQKISSmslELVRQFPDVVSLNLGGGYKVARMADEVstdlqqcgEPVA 246
Cdd:cd06829 144 LDELEE-EDLDGIEGLHFHTLCEQDFDAleRTLEAVEE---RFGEYLPQLKWLNLGGGHHITRPDYDV--------DRLI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 247 DKFREFAAETGREIRLeiEPGTYLLANACSVLSMVQDKVSTGRegyEFLKLNTG----MTEVL----RPSIYGAQHPifi 318
Cdd:cd06829 212 ALIKRFKEKYGVEVYL--EPGEAVALNTGYLVATVLDIVENGM---PIAILDASatahMPDVLempyRPPIRGAGEP--- 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502808573 319 lKEATPTetcdYMIAGHCCESGDILTPASGDPELlatrtlpvtEIGDLCVIDGSGAY 375
Cdd:cd06829 284 -GEGAHT----YRLGGNSCLAGDVIGDYSFDEPL---------QVGDRLVFEDMAHY 326
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
16-233 |
8.00e-15 |
|
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: 75.76 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 16 RQIADQFGSPVYVYDMATLKANAADVLAFPNAYGLTAR--YAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTP 93
Cdd:cd06842 2 VALVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGRvyFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 94 EKISLSTqelPTDFAELYELGIEINAC----SLSQLERF---GQAFPGR--SIGVRFNPGAGSggnnrtnvggPASSFGI 164
Cdd:cd06842 82 DRIVATG---PAKTDEFLWLAVRHGATiavdSLDELDRLlalARGYTTGpaRVLLRLSPFPAS----------LPSRFGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502808573 165 WHEWIDQVQEIVARY--DLKVIRIHTHIGsGSDPKvwQKISSM--SLELVRQ----FPDVVSLNLGGGYKVARMADE 233
Cdd:cd06842 149 PAAEVRTALERLAQLreRVRLVGFHFHLD-GYSAA--QRVAALqeCLPLIDRaralGLAPRFIDIGGGFPVSYLADA 222
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
34-224 |
3.87e-11 |
|
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: 62.34 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 34 LKANAADVLAFPNAyGLTARYAMKASPNAAILRIFNEAGLHIDASSGYEVRRAIAAGYTPEKISL-----STQELPtDFA 108
Cdd:cd06808 1 IRHNYRRLREAAPA-GITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFlgpckQVSELE-DAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502808573 109 ELYElgIEINACSLSQLERFGQA----FPGRSIGVRFNPGAgsgGNNRtnvggpassFGIWHEWIDQVQEIVARYD-LKV 183
Cdd:cd06808 79 EQGV--IVVTVDSLEELEKLEEAalkaGPPARVLLRIDTGD---ENGK---------FGVRPEELKALLERAKELPhLRL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502808573 184 IRIHTHIGSGSDPKV-----WQKISSMSLELVRQFPDVVSLNLGGG 224
Cdd:cd06808 145 VGLHTHFGSADEDYSpfveaLSRFVAALDQLGELGIDLEQLSIGGS 190
|
|
| |
