|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
41-484 |
1.44e-178 |
|
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: 506.99 E-value: 1.44e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 41 GELAVQGVPASVLAERFGTPVLVLDEDDFRARARAFREGFDAAfeslcgGADVYFAGKSMLTLSTARWAAEEGLRVDTAS 120
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGS------GAKVLYAVKANSNLAVLRLLAEEGLGADVVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 121 GGELAIALRAGVLPEHIGLHGNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDFI 200
Cdd:COG0019 82 GGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVNPGVDAGTHEYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 201 ATAHEDQKFGLSLtpsatgrdgneagvAPAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEH 280
Cdd:COG0019 162 STGGKDSKFGIPL--------------EDALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELR-EL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 281 GVELPELDLGGGHGIAYTAVDEPRPAAEIADALADdvqkAVERLGLTCPRISIEPGRAISGPAGLTLYSVGVTKTvdvda 360
Cdd:COG0019 227 GIDLEWLDLGGGLGIPYTEGDEPPDLEELAAAIKE----ALEELCGLGPELILEPGRALVGNAGVLLTRVLDVKE----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 361 pddgTASRRYVAVDGGMSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPeDVARGDLLAVPAT 440
Cdd:COG0019 298 ----NGGRRFVIVDAGMNDLMRPALYGAYHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLP-PLEPGDLLAFLDA 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2103903196 441 GAYTHSMSSNYNALLRPAVVAVRDGEAREIVRRETLDDLLRREV 484
Cdd:COG0019 373 GAYGFSMASNYNGRPRPAEVLVDDGEARLIRRRETYEDLLASEV 416
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
41-484 |
9.68e-151 |
|
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: 436.34 E-value: 9.68e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 41 GELAVQGVPASVLAERFGTPVLVLDEDDFRARARAFREGFDAAfeslcggADVYFAGKSMLTLSTARWAAEEGLRVDTAS 120
Cdd:TIGR01048 7 GELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGR-------SLVCYAVKANSNLAVLRLLAELGSGFDVVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 121 GGELAIALRAGVLPEHIGLHGNNKSAAELATALDAGVgRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDFI 200
Cdd:TIGR01048 80 GGELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHPYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 201 ATAHEDQKFGLSLTpsatgrdgneagvaPAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKDeh 280
Cdd:TIGR01048 159 STGLKDSKFGIDVE--------------EALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 281 GVELPELDLGGGHGIAYTAVDEPRPAAEIADALADDVQKAvERLGLTcPRISIEPGRAISGPAGLTLYSVGVTKTVDvda 360
Cdd:TIGR01048 223 GIDLEFLDLGGGLGIPYTPEEEPPDLSEYAQAILNALEGY-ADLGLD-PKLILEPGRSIVANAGVLLTRVGFVKETG--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 361 pddgtaSRRYVAVDGGMSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPAT 440
Cdd:TIGR01048 298 ------SRNFVIVDAGMNDLIRPALYGAYHHIIVLNRTNDAPTEVADVVGPVCESGDVLAKDRELPE-VEPGDLLAVFDA 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2103903196 441 GAYTHSMSSNYNALLRPAVVAVRDGEAREIVRRETLDDLLRREV 484
Cdd:TIGR01048 371 GAYGFSMSSNYNSRPRPAEVLVDGGQARLIRRRETYEDLWALEV 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
57-462 |
1.55e-149 |
|
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: 431.52 E-value: 1.55e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 57 FGTPVLVLDEDDFRARARAFREgfdaAFESLcgGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEH 136
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKE----AFSGP--GFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 137 IGLHGNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDFIATAHEDQKFGLSLtps 216
Cdd:cd06828 75 IVFTGNGKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 217 atgrdgneagvAPAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGGGHGIA 296
Cdd:cd06828 152 -----------EQALEAYRRAKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELR-ELGIDLEFLDLGGGLGIP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 297 YTAVDEPRPAAEIADALADDVQKAVERLGLtcPRISIEPGRAISGPAGLTLYSVGVTKTvdvdapddgTASRRYVAVDGG 376
Cdd:cd06828 220 YRDEDEPLDIEEYAEAIAEALKELCEGGPD--LKLIIEPGRYIVANAGVLLTRVGYVKE---------TGGKTFVGVDAG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 377 MSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATGAYTHSMSSNYNALLR 456
Cdd:cd06828 289 MNDLIRPALYGAYHEIVPVNKPGEGETEKVDVVGPICESGDVFAKDRELPE-VEEGDLLAIHDAGAYGYSMSSNYNSRPR 367
|
....*.
gi 2103903196 457 PAVVAV 462
Cdd:cd06828 368 PAEVLV 373
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
63-441 |
1.85e-81 |
|
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: 256.26 E-value: 1.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 63 VLDEDDFRARARAFREGFDaafeslcGGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEHIGLHGN 142
Cdd:pfam00278 3 VYDLATLRRNYRRWKAALP-------PRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 143 NKSAAELATALDAGVGRIIVDSVDELEFLAALAaeRGQIAPVMLRVTPGVHAHTHdFIATAHEDQKFGLSLTpsatgrdg 222
Cdd:pfam00278 76 GKTDSEIRYALEAGVLCFNVDSEDELEKIAKLA--PELVARVALRINPDVDAGTH-KISTGGLSSKFGIDLE-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 223 neagvapAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGGGHGIAYTAVDE 302
Cdd:pfam00278 145 -------DAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLR-ELGIDLKLLDIGGGFGIPYRDEPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 303 PRPaaeiaDALADDVQKAVERLGLTCPRISIEPGRAISGPAGLTLYSVGVTKTVDvdapddgtaSRRYVAVDGGMSDNPR 382
Cdd:pfam00278 217 PDF-----EEYAAAIREALDEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGG---------GKTFVIVDAGMNDLFR 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2103903196 383 PVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATG 441
Cdd:pfam00278 283 PALYDAYHPIPVVKEPGEGPLETYDVVGPTCESGDVLAKDRELPE-LEVGDLLAFEDAG 340
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
120-481 |
1.14e-48 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 172.28 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 120 SGGELAIALRAGVLPEHIGLHGNNKSAAELATALDAGVgRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDF 199
Cdd:PLN02537 73 SGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 200 IATAHEDQKFGLSltpsatgrdgNEAGVAPAAVAVRtalQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKDE 279
Cdd:PLN02537 152 VATGNKNSKFGIR----------NEKLQWFLDAVKA---HPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 280 hGVELPELDLGGGHGIAYTAVDEPRPAAEiadALADDVQKAVERLGLTcprISIEPGRAISGPAGLTLYSVGVTKTvdvd 359
Cdd:PLN02537 219 -GFELSYLNIGGGLGIDYYHAGAVLPTPR---DLIDTVRELVLSRDLT---LIIEPGRSLIANTCCFVNRVTGVKT---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 360 apdDGTasRRYVAVDGGMSDNPRPVLYDADYTAALASRTSDAAPALS-RVVGKHCESGDILVRDVWLPEDvARGDLLAVP 438
Cdd:PLN02537 288 ---NGT--KNFIVIDGSMAELIRPSLYDAYQHIELVSPPPPDAEVSTfDVVGPVCESADFLGKDRELPTP-PKGAGLVVH 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2103903196 439 ATGAYTHSMSSNYNALLRPAVVAVR-DGEAREIVRRETLDDLLR 481
Cdd:PLN02537 362 DAGAYCMSMASTYNLKMRPPEYWVEeDGSITKIRHAETFDDHLR 405
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
41-484 |
1.44e-178 |
|
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: 506.99 E-value: 1.44e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 41 GELAVQGVPASVLAERFGTPVLVLDEDDFRARARAFREGFDAAfeslcgGADVYFAGKSMLTLSTARWAAEEGLRVDTAS 120
Cdd:COG0019 8 GELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGS------GAKVLYAVKANSNLAVLRLLAEEGLGADVVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 121 GGELAIALRAGVLPEHIGLHGNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDFI 200
Cdd:COG0019 82 GGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVNPGVDAGTHEYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 201 ATAHEDQKFGLSLtpsatgrdgneagvAPAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEH 280
Cdd:COG0019 162 STGGKDSKFGIPL--------------EDALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELR-EL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 281 GVELPELDLGGGHGIAYTAVDEPRPAAEIADALADdvqkAVERLGLTCPRISIEPGRAISGPAGLTLYSVGVTKTvdvda 360
Cdd:COG0019 227 GIDLEWLDLGGGLGIPYTEGDEPPDLEELAAAIKE----ALEELCGLGPELILEPGRALVGNAGVLLTRVLDVKE----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 361 pddgTASRRYVAVDGGMSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPeDVARGDLLAVPAT 440
Cdd:COG0019 298 ----NGGRRFVIVDAGMNDLMRPALYGAYHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLP-PLEPGDLLAFLDA 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2103903196 441 GAYTHSMSSNYNALLRPAVVAVRDGEAREIVRRETLDDLLRREV 484
Cdd:COG0019 373 GAYGFSMASNYNGRPRPAEVLVDDGEARLIRRRETYEDLLASEV 416
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
41-484 |
9.68e-151 |
|
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: 436.34 E-value: 9.68e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 41 GELAVQGVPASVLAERFGTPVLVLDEDDFRARARAFREGFDAAfeslcggADVYFAGKSMLTLSTARWAAEEGLRVDTAS 120
Cdd:TIGR01048 7 GELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGR-------SLVCYAVKANSNLAVLRLLAELGSGFDVVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 121 GGELAIALRAGVLPEHIGLHGNNKSAAELATALDAGVgRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDFI 200
Cdd:TIGR01048 80 GGELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHPYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 201 ATAHEDQKFGLSLTpsatgrdgneagvaPAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKDeh 280
Cdd:TIGR01048 159 STGLKDSKFGIDVE--------------EALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 281 GVELPELDLGGGHGIAYTAVDEPRPAAEIADALADDVQKAvERLGLTcPRISIEPGRAISGPAGLTLYSVGVTKTVDvda 360
Cdd:TIGR01048 223 GIDLEFLDLGGGLGIPYTPEEEPPDLSEYAQAILNALEGY-ADLGLD-PKLILEPGRSIVANAGVLLTRVGFVKETG--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 361 pddgtaSRRYVAVDGGMSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPAT 440
Cdd:TIGR01048 298 ------SRNFVIVDAGMNDLIRPALYGAYHHIIVLNRTNDAPTEVADVVGPVCESGDVLAKDRELPE-VEPGDLLAVFDA 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2103903196 441 GAYTHSMSSNYNALLRPAVVAVRDGEAREIVRRETLDDLLRREV 484
Cdd:TIGR01048 371 GAYGFSMSSNYNSRPRPAEVLVDGGQARLIRRRETYEDLWALEV 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
57-462 |
1.55e-149 |
|
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: 431.52 E-value: 1.55e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 57 FGTPVLVLDEDDFRARARAFREgfdaAFESLcgGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEH 136
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKE----AFSGP--GFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 137 IGLHGNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDFIATAHEDQKFGLSLtps 216
Cdd:cd06828 75 IVFTGNGKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 217 atgrdgneagvAPAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGGGHGIA 296
Cdd:cd06828 152 -----------EQALEAYRRAKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELR-ELGIDLEFLDLGGGLGIP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 297 YTAVDEPRPAAEIADALADDVQKAVERLGLtcPRISIEPGRAISGPAGLTLYSVGVTKTvdvdapddgTASRRYVAVDGG 376
Cdd:cd06828 220 YRDEDEPLDIEEYAEAIAEALKELCEGGPD--LKLIIEPGRYIVANAGVLLTRVGYVKE---------TGGKTFVGVDAG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 377 MSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATGAYTHSMSSNYNALLR 456
Cdd:cd06828 289 MNDLIRPALYGAYHEIVPVNKPGEGETEKVDVVGPICESGDVFAKDRELPE-VEEGDLLAIHDAGAYGYSMSSNYNSRPR 367
|
....*.
gi 2103903196 457 PAVVAV 462
Cdd:cd06828 368 PAEVLV 373
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
59-462 |
4.97e-87 |
|
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: 271.48 E-value: 4.97e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 59 TPVLVLDEDDFRARARAFREgfdaAFESlcgGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEHIG 138
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKE----ALPS---GVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 139 LHGNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHdFIATAHEDQKFGLSLTpsat 218
Cdd:cd06810 74 FTGPAKSVSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTH-KISTGGLKSKFGLSLS---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 219 grdgneagvapAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGGGHGIAYT 298
Cdd:cd06810 149 -----------EARAALERAKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELV-EMGFPLEMLDLGGGLGIPYD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 299 avDEPRPAAEIADALADDVQKAVERLGLtcPRISIEPGRAISGPAGLTLYSVGVTKTVDvdapddgtaSRRYVAVDGGMS 378
Cdd:cd06810 217 --EQPLDFEEYAALINPLLKKYFPNDPG--VTLILEPGRYIVAQAGVLVTRVVAVKVNG---------GRFFAVVDGGMN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 379 DNPRPVL-YDADYTAALASRTSDAAPAL-SRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATGAYTHSMSSNYNALLR 456
Cdd:cd06810 284 HSFRPALaYDAYHPITPLKAPGPDEPLVpATLAGPLCDSGDVIGRDRLLPE-LEVGDLLVFEDMGAYGFSESSNFNSHPR 362
|
....*.
gi 2103903196 457 PAVVAV 462
Cdd:cd06810 363 PAEYLV 368
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
63-441 |
1.85e-81 |
|
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: 256.26 E-value: 1.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 63 VLDEDDFRARARAFREGFDaafeslcGGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEHIGLHGN 142
Cdd:pfam00278 3 VYDLATLRRNYRRWKAALP-------PRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 143 NKSAAELATALDAGVGRIIVDSVDELEFLAALAaeRGQIAPVMLRVTPGVHAHTHdFIATAHEDQKFGLSLTpsatgrdg 222
Cdd:pfam00278 76 GKTDSEIRYALEAGVLCFNVDSEDELEKIAKLA--PELVARVALRINPDVDAGTH-KISTGGLSSKFGIDLE-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 223 neagvapAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGGGHGIAYTAVDE 302
Cdd:pfam00278 145 -------DAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLR-ELGIDLKLLDIGGGFGIPYRDEPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 303 PRPaaeiaDALADDVQKAVERLGLTCPRISIEPGRAISGPAGLTLYSVGVTKTVDvdapddgtaSRRYVAVDGGMSDNPR 382
Cdd:pfam00278 217 PDF-----EEYAAAIREALDEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGG---------GKTFVIVDAGMNDLFR 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2103903196 383 PVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATG 441
Cdd:pfam00278 283 PALYDAYHPIPVVKEPGEGPLETYDVVGPTCESGDVLAKDRELPE-LEVGDLLAFEDAG 340
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
53-448 |
3.18e-57 |
|
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: 194.35 E-value: 3.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 53 LAERFGTPVLVLDEDDFRARARAFREgfdaafeSLCGGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGV 132
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRA-------ALPPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 133 LPEHIGLHGNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAhthdfiatahedQKFGLS 212
Cdd:cd06839 74 PPEKILFAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRINPDFEL------------KGSGMK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 213 LT--PSATGRDGNEagvapAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKDEHGVELPELDLG 290
Cdd:cd06839 142 MGggPSQFGIDVEE-----LPAVLARIAALPNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLAEELGLPLEFLDLG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 291 GGHGIAYTAVDEPRPAAEIADALADDVQKAVERLGltCPRISIEPGRAISGPAGltlysVGVTKTVDVDAPDDgtasRRY 370
Cdd:cd06839 217 GGFGIPYFPGETPLDLEALGAALAALLAELGDRLP--GTRVVLELGRYLVGEAG-----VYVTRVLDRKVSRG----ETF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 371 VAVDGGM------SDNPRPVLyDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATGAYT 444
Cdd:cd06839 286 LVTDGGMhhhlaaSGNFGQVL-RRNYPLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPP-LEPGDLVAVLQSGAYG 363
|
....
gi 2103903196 445 HSMS 448
Cdd:cd06839 364 LSAS 367
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
66-341 |
2.95e-52 |
|
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: 176.70 E-value: 2.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 66 EDDFRARARAFREGFDAAFeslcggadVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEHIGLHGNNKS 145
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIK--------PFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 146 AAELATALDAGVGRIIVDSVDELEFLAALAAErgqiAPVMLRVTPGVHAHTHDFiataheDQKFGLSLtpsatgrdgnea 225
Cdd:pfam02784 73 RSFLRYALEVGVGCVTVDNVDELEKLARLAPE----ARVLLRIKPDDSAATCPL------SSKFGADL------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 226 gvAPAAVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGGGHGIAYTAVDEPRP 305
Cdd:pfam02784 131 --DEDVEALLEAAKLLNLQVVGVSFHVGSGCTDAEAFVLALEDARGVFDQGA-ELGFNLKILDLGGGFGVDYTEGEEPLD 207
|
250 260 270
....*....|....*....|....*....|....*.
gi 2103903196 306 AAEIADALADDVQKAVErlGLTCPRISIEPGRAISG 341
Cdd:pfam02784 208 FEEYANVINEALEEYFP--GDPGVTIIAEPGRYFVA 241
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
120-481 |
1.14e-48 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 172.28 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 120 SGGELAIALRAGVLPEHIGLHGNNKSAAELATALDAGVgRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGVHAHTHDF 199
Cdd:PLN02537 73 SGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 200 IATAHEDQKFGLSltpsatgrdgNEAGVAPAAVAVRtalQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKDE 279
Cdd:PLN02537 152 VATGNKNSKFGIR----------NEKLQWFLDAVKA---HPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 280 hGVELPELDLGGGHGIAYTAVDEPRPAAEiadALADDVQKAVERLGLTcprISIEPGRAISGPAGLTLYSVGVTKTvdvd 359
Cdd:PLN02537 219 -GFELSYLNIGGGLGIDYYHAGAVLPTPR---DLIDTVRELVLSRDLT---LIIEPGRSLIANTCCFVNRVTGVKT---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 360 apdDGTasRRYVAVDGGMSDNPRPVLYDADYTAALASRTSDAAPALS-RVVGKHCESGDILVRDVWLPEDvARGDLLAVP 438
Cdd:PLN02537 288 ---NGT--KNFIVIDGSMAELIRPSLYDAYQHIELVSPPPPDAEVSTfDVVGPVCESADFLGKDRELPTP-PKGAGLVVH 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2103903196 439 ATGAYTHSMSSNYNALLRPAVVAVR-DGEAREIVRRETLDDLLR 481
Cdd:PLN02537 362 DAGAYCMSMASTYNLKMRPPEYWVEeDGSITKIRHAETFDDHLR 405
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
53-465 |
7.52e-45 |
|
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: 161.28 E-value: 7.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 53 LAERFGTPVLVLDEDDFRARARAFREGFDAAFeslcGGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGV 132
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRY----PNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 133 LPEHIGLHGNNKSAAELATALDAGvGRIIVDSVDELEFLAALAAERGQIAPVMLRVTpgvhahthdFIATAHEDQKFGLS 212
Cdd:cd06841 77 PGKRIIFNGPYKSKEELEKALEEG-ALINIDSFDELERILEIAKELGRVAKVGIRLN---------MNYGNNVWSRFGFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 213 LtpsatgRDGNEAGVAPAAVAvrtalQADSIRLLGLHCHIGSQIFEADGFglaAERVLGFLAEVKDEHGVELPELDLGGG 292
Cdd:cd06841 147 I------EENGEALAALKKIQ-----ESKNLSLVGLHCHVGSNILNPEAY---SAAAKKLIELLDRLFGLELEYLDLGGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 293 -------HGIAYTAVDEPRP---AAEIADAL----ADDVQKaverlgltcPRISIEPGRAISGPAGLTLYSVGVTKTVdv 358
Cdd:cd06841 213 fpaktplSLAYPQEDTVPDPedyAEAIASTLkeyyANKENK---------PKLILEPGRALVDDAGYLLGRVVAVKNR-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 359 dapddgtASRRYVAVDGGMSDNPRPVLYDADYTaALASRTSDAAPALSRVVGKHCESGDILVRDVWLPeDVARGDLLAVP 438
Cdd:cd06841 282 -------YGRNIAVTDAGINNIPTIFWYHHPIL-VLRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLP-PLNVGDILAIR 352
|
410 420
....*....|....*....|....*..
gi 2103903196 439 ATGAYTHSMSSNYnALLRPAVVAVRDG 465
Cdd:cd06841 353 NVGAYNMTQSNQF-IRPRPAVYLIDNN 378
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
60-457 |
2.43e-37 |
|
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: 140.65 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 60 PVLVLDEDDFRARARAFregfdAAFESLCGGadvYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRA--GVLPEHI 137
Cdd:cd06840 13 PCYVYDLETVRARARQV-----SALKAVDSL---FYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 138 GLHGNNKSAAELATALDAGVgRIIVDSVDELEFLAALAAERgqiaPVMLRVTPGVHAHTHDFIATAHEDQKFGLSLTPSA 217
Cdd:cd06840 85 LFTPNFAARSEYEQALELGV-NVTVDNLHPLREWPELFRGR----EVILRIDPGQGEGHHKHVRTGGPESKFGLDVDELD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 218 TGRDgneagvapaavavrtALQADSIRLLGLHCHIGSQIFEADGFglaaERVLGFLAEVKDEHGvELPELDLGGGHGIAY 297
Cdd:cd06840 160 EARD---------------LAKKAGIIVIGLHAHSGSGVEDTDHW----ARHGDYLASLARHFP-AVRILNVGGGLGIPE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 298 TAVDEPRPAAEIADALADdVQKAVERLgltcpRISIEPGRAISGPAGLTLYSVGVTKTVDvdapddgtaSRRYVAVDGGM 377
Cdd:cd06840 220 APGGRPIDLDALDAALAA-AKAAHPQY-----QLWMEPGRFIVAESGVLLARVTQIKHKD---------GVRFVGLETGM 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 378 SDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATGAYTHSMSSNYNalLRP 457
Cdd:cd06840 285 NSLIRPALYGAYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRLLPE-TEEGDVILIANAGAYGFCMASTYN--LRE 361
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
58-462 |
6.51e-37 |
|
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: 139.17 E-value: 6.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 58 GTPVLVLDEDDFRARARAFREGFDaafeslcgGADVYFAGKS-----MLTLstarwAAEEGLRVDTASGGELAIALRAGV 132
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALP--------RVRPFYAVKCnpdpaVLRT-----LAALGAGFDCASKGEIELVLGLGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 133 LPEHIgLHGN-NKSAAELATALDAGVGRIIVDSVDELEFLAALAAErgqiAPVMLRV-TPGVHAhTHDFiataheDQKFG 210
Cdd:cd00622 68 SPERI-IFANpCKSISDIRYAAELGVRLFTFDSEDELEKIAKHAPG----AKLLLRIaTDDSGA-LCPL------SRKFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 211 LSLTpsatgrdgneagvapaavavrtalqaDSIRLL-----------GLHCHIGSQIFEADGFGLAAERVlgflAEVKD- 278
Cdd:cd00622 136 ADPE--------------------------EARELLrrakelglnvvGVSFHVGSQCTDPSAYVDAIADA----REVFDe 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 279 --EHGVELPELDLGGGHGIAYTAVDEPrpAAEIADAladdVQKAVERL-GLTCPRISIEPGRAISGPAGlTLYS--VGVT 353
Cdd:cd00622 186 aaELGFKLKLLDIGGGFPGSYDGVVPS--FEEIAAV----INRALDEYfPDEGVRIIAEPGRYLVASAF-TLAVnvIAKR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 354 KTVDVDAP-----DDGtasrRYvavdGGMSDnprpVLYD-ADYTAALASRTSDAAPALSRVV-GKHCESGDILVRDVWLP 426
Cdd:cd00622 259 KRGDDDRErwyylNDG----VY----GSFNE----ILFDhIRYPPRVLKDGGRDGELYPSSLwGPTCDSLDVIYEDVLLP 326
|
410 420 430
....*....|....*....|....*....|....*.
gi 2103903196 427 EDVARGDLLAVPATGAYTHSMSSNYNALLRPAVVAV 462
Cdd:cd00622 327 EDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
61-463 |
3.78e-36 |
|
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: 137.52 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 61 VLVLDEDDFRARARAFREGFDAafeslcgGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEHIGLH 140
Cdd:cd06836 5 VGLYDLDGFRALVARLTAAFPA-------PVLHTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 141 GNNKSAAELATALDAGVgRIIVDSVDELEFLAALAAERGQIA-PVMLRVTPGVHAHTHDFIATAHEDQKFGLSLTPSAtg 219
Cdd:cd06836 78 SPAKTRAELREALELGV-AINIDNFQELERIDALVAEFKEASsRIGLRVNPQVGAGKIGALSTATATSKFGVALEDGA-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 220 RDgneagvapaavaVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKDEHG-VELPELDLGGGHGIAYT 298
Cdd:cd06836 155 RD------------EIIDAFARRPWLNGLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRVGrRQITRIDIGGGLPVNFE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 299 AVDEPRPAAEIADALaddvQKAVERLGLTCPRISIEPGRAISGPAGLTLYSVGVTKTvdvdapddgTASRRYVAVDGGMS 378
Cdd:cd06836 223 SEDITPTFADYAAAL----KAAVPELFDGRYQLVTEFGRSLLAKCGTIVSRVEYTKS---------SGGRRIAITHAGAQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 379 DNPRPVLYDADYTAALASRTSDAAP-----ALSRVVGKHCESGDILVRDVWLPEdVARGDLLAVPATGAYTHSMSSNYNA 453
Cdd:cd06836 290 VATRTAYAPDDWPLRVTVFDANGEPktgpeVVTDVAGPCCFAGDVLAKERALPP-LEPGDYVAVHDTGAYYFSSHSSYNS 368
|
410
....*....|
gi 2103903196 454 LLRPAVVAVR 463
Cdd:cd06836 369 LPRPAVYGVR 378
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
58-471 |
6.39e-35 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 139.06 E-value: 6.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 58 GTPVLVLDEDDFRARARAFRegfdaafeSLCGGADVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRA--GVLPE 135
Cdd:PRK08961 502 GSPCYVYHLPTVRARARALA--------ALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 136 HIGLHGNNKSAAELATALDAGVgRIIVDSVDELEFLAALAAERgqiaPVMLRVTPGVHAHTHDFIATAHEDQKFGLSLTP 215
Cdd:PRK08961 574 RVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNWPELFRGR----EVWLRIDPGHGDGHHEKVRTGGKESKFGLSQTR 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 216 SATGRDgneagvapaavavrtALQADSIRLLGLHCHIGSQIFEADGFglaaERVLGFLAEVKDEHGvELPELDLGGGHGI 295
Cdd:PRK08961 649 IDEFVD---------------LAKTLGITVVGLHAHLGSGIETGEHW----RRMADELASFARRFP-DVRTIDLGGGLGI 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 296 AYTAVDEPRPAAEIADALADdVQKAVERLgltcpRISIEPGRAISGPAGLTLYSVGVTKTVDvdapddgtaSRRYVAVDG 375
Cdd:PRK08961 709 PESAGDEPFDLDALDAGLAE-VKAQHPGY-----QLWIEPGRYLVAEAGVLLARVTQVKEKD---------GVRRVGLET 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 376 GMSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGDILVRDVWLPeDVARGDLLAVPATGAYTHSMSSNYNalL 455
Cdd:PRK08961 774 GMNSLIRPALYGAYHEIVNLSRLDEPAAGTADVVGPICESSDVLGKRRRLP-ATAEGDVILIANAGAYGYSMSSTYN--L 850
|
410
....*....|....*.
gi 2103903196 456 RPAvvavrdgeAREIV 471
Cdd:PRK08961 851 REP--------AREVV 858
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
69-297 |
4.21e-31 |
|
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: 119.35 E-value: 4.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 69 FRARARAFREGFDAAFEslcggadVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEHIGLHGNNKSAAE 148
Cdd:cd06808 1 IRHNYRRLREAAPAGIT-------LFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 149 LATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPGvhahthdfiataHEDQKFGLSLTPSAtgrdgneagva 228
Cdd:cd06808 74 LEDAAEQGVIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTG------------DENGKFGVRPEELK----------- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2103903196 229 paaVAVRTALQADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGGGHGIAY 297
Cdd:cd06808 131 ---ALLERAKELPHLRLVGLHTHFGSADEDYSPFVEALSRFVAALDQLG-ELGIDLEQLSIGGSFAILY 195
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
53-443 |
6.64e-27 |
|
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: 112.35 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 53 LAERFGTPVLVLDEDDFRARARAFREGFDAAFESLCggadVYFAGKSMLTLSTARWAAEEGLRVDTASGGELAIALRAGV 132
Cdd:cd06842 4 LVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGR----VYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 133 LPEHIGLHGNNKSAAELATALDAGVgRIIVDSVDELEFLAALA-AERGQIAPVMLRVTPGVHAHthdfiataheDQKFGl 211
Cdd:cd06842 80 RGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLALArGYTTGPARVLLRLSPFPASL----------PSRFG- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 212 slTPSATGRDGNEAGVAPaavavrtalqADSIRLLGLHCHIGSqiFEADGFGLAAERVLGFLAEVKdEHGVELPELDLGG 291
Cdd:cd06842 148 --MPAAEVRTALERLAQL----------RERVRLVGFHFHLDG--YSAAQRVAALQECLPLIDRAR-ALGLAPRFIDIGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 292 GHGIAYTAVDE----------------------------------------PRPAA----EIADALADDVQKAVERL--- 324
Cdd:cd06842 213 GFPVSYLADAAeweaflaaltealygygrpltwrneggtlrgpddfypygqPLVAAdwlrAILSAPLPQGRTIAERLrdn 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 325 GLTcprISIEPGRAISGPAGLTLYSVgvtktVDVDAPDDGTasrRYVAVDGGMSDN--------PRPVLYDAdytaalAS 396
Cdd:cd06842 293 GIT---LALEPGRALLDQCGLTVARV-----AFVKQLGDGN---HLIGLEGNSFSAcefsseflVDPLLIPA------PE 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2103903196 397 RTSDAAPALSRVVGKHC-ESGDILVRDVWLPEDVARGDLLAVPATGAY 443
Cdd:cd06842 356 PTTDGAPIEAYLAGASClESDLITRRKIPFPRLPKPGDLLVFPNTAGY 403
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
63-448 |
4.92e-26 |
|
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: 109.29 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 63 VLDEDDFRARARAFREgfdaafeSLCGGADVYFAGKSMLTLSTARWAAE--EGLRVdtASGGELAiALRAGVLPEHIGLH 140
Cdd:cd06843 6 VYDLAALRAHARALRA-------SLPPGCELFYAIKANSDPPILRALAPhvDGFEV--ASGGEIA-HVRAAVPDAPLIFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 141 GNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAERGQIAPVMLRVTPgvhahTHDFIATAhedqKFGLSLTPSATGR 220
Cdd:cd06843 76 GPGKTDSELAQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNL-----ALPDLPSS----TLTMGGQPTPFGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 221 DGNEAGVAPAAVAVrtalqADSIRLLGLHCHIGSQIFEADGFGLAAERVLGFLAEVKDEHGVELPELDLGGGHGIAYTAV 300
Cdd:cd06843 147 DEADLPDALELLRD-----LPNIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEHGLDLDVVNVGGGIGVNYADP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 301 DEPRPAAEIADALADDVQKAVERLgltcpRISIEPGRAISGPAGltlysVGVTKTVDVDAPDDGTasrrYVAVDGGMS-- 378
Cdd:cd06843 222 EEQFDWAGFCEGLDQLLAEYEPGL-----TLRFECGRYISAYCG-----YYVTEVLDLKRSHGEW----FAVLRGGTHhf 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2103903196 379 --------DNPRPVLYDADYTAALaSRTSDAAPALSrVVGKHCESGDILVRDVWLPeDVARGDLLAVPATGAYTHSMS 448
Cdd:cd06843 288 rlpaawghNHPFSVLPVEEWPYPW-PRPSVRDTPVT-LVGQLCTPKDVLARDVPVD-RLRAGDLVVFPLAGAYGWNIS 362
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
160-357 |
1.53e-11 |
|
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: 66.05 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 160 IIVDSVDELEFLAALAAERGqIAPVM-LRVTPGVhAHTHDFIATAHEDQKFGLSLtpsatgrdgNEAGVAPAAVAVRTAL 238
Cdd:cd06830 116 IVIEKLSELDLILELAKKLG-VKPLLgVRIKLAS-KGSGKWQESGGDRSKFGLTA---------SEILEVVEKLKEAGML 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 239 qaDSIRLLglHCHIGSQIFEADGFGLAAERVLGFLAEVKDEhGVELPELDLGGGHGIAYTAVDEPRPAA------EIADA 312
Cdd:cd06830 185 --DRLKLL--HFHIGSQITDIRRIKSALREAARIYAELRKL-GANLRYLDIGGGLGVDYDGSRSSSDSSfnysleEYAND 259
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2103903196 313 LADDVQKAVERLGLTCPRISIEPGRAISGPAGLTLYSV-GVTKTVD 357
Cdd:cd06830 260 IVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVlGVKRLAD 305
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
241-366 |
2.09e-03 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 40.85 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 241 DSIRLLglHCHIGSQIfeAD------GFGLAAeRvlgFLAEVKDEhGVELPELDLGGGHGIAYTA------------VDE 302
Cdd:COG1166 240 DCLQLL--HFHLGSQI--PNirdikrAVREAA-R---FYAELRKL-GAPIEYLDVGGGLGVDYDGsrsnsdssmnysLQE 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103903196 303 prPAAEIADALADdvqkAVERLGLTCPRISIEPGRAISGPagltlYSVGVTKTVDVDAPDDGTA 366
Cdd:COG1166 311 --YANDVVYAIKE----VCDEAGVPHPTIISESGRALTAH-----HSVLIFNVLDVERAPPEPP 363
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
37-487 |
4.37e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 39.86 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 37 RDAAGELAVQGVP---ASVLAERFGTPV----------------LVLDEDDFRARARAFREGFDAAFESLCGGADVYFAG 97
Cdd:COG3321 834 LTALAQLWVAGVPvdwSALYPGRGRRRVplptypfqredaaaalLAAALAAALAAAAALGALLLAALAAALAAALLALAA 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 98 KSMLTLSTARWAAEEGLRVDTASGGELAIALRAGVLPEHIGLHGNNKSAAELATALDAGVGRIIVDSVDELEFLAALAAE 177
Cdd:COG3321 914 AAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAA 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 178 RGQIAPVMLRVTPGVHAHTHDFIATAHEDQKFGLSLTPSATGRDGNEAGVAPAAVAVRTALQADSIRLLGLHCHIGSQIF 257
Cdd:COG3321 994 AALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAA 1073
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 258 EADGFGLAAERVLGFLAEVKDEHGVELPELDLGGGHGIAYTAVDEPRPAAEIADALADDVQKAVERLGLTCPRISIEPGR 337
Cdd:COG3321 1074 LAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALA 1153
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 338 AISGPAGLTLYSVGVTKTVDVDAPDDGTASRRYVAVDGGMSDNPRPVLYDADYTAALASRTSDAAPALSRVVGKHCESGD 417
Cdd:COG3321 1154 AAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAAL 1233
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 418 ILVRDVWLPEDVARGDLLAVPATGAYTHSMSSNYNALLRPAVVAVRDGEAREIVRRETLDDLLRREVDPQ 487
Cdd:COG3321 1234 ALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLA 1303
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
145-339 |
4.55e-03 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 39.67 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 145 SAAELATALdaGVGRIIV-DSVDELEfLAALAAERGQIAPVMlrvtpGVHA-----HTHDFIATAHEDQKFGLSLTpsat 218
Cdd:PLN02439 98 SLALLARKL--GLNTVIVlEQEEELD-LVIEASQRLGVRPVI-----GVRAklrtkHSGHFGSTSGEKGKFGLTAT---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103903196 219 grdgnEAGVAPAAVAVRTALqaDSIRLLglHCHIGSQIFEADGFGLAAERVLGFLAEVKDEhGVELPELDLGGGHGIAY- 297
Cdd:PLN02439 166 -----EIVRVVRKLRKEGML--DCLQLL--HFHIGSQIPSTSLLKDGVSEAAQIYCELVRL-GAPMRVIDIGGGLGIDYd 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2103903196 298 ----------TAVDEPrpaaEIADALADDVQKAVERLGLTCPRISIEPGRAI 339
Cdd:PLN02439 236 gsksgssdmsVAYSLE----EYANAVVAAVRDVCDRKGVKHPVICSESGRAL 283
|
|
| |
