|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02439 |
PLN02439 |
arginine decarboxylase |
97-663 |
0e+00 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 1102.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 97 LIVRFPDVLKNRLECLQSAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLCKG 176
Cdd:PLN02439 1 LIVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPFRFGLEAGSKPELLLAMSCLCKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 177 NPEAFLVCNGFKDSEYISLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKF 256
Cdd:PLN02439 81 SPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 257 GLTTVQILRVVRKLSQVGMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSG 336
Cdd:PLN02439 161 GLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 337 ESDLSVAYSLEEYAAAVVASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAG--QQHETPTDHQFMLEGYSEEV 414
Cdd:PLN02439 241 SSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASkrGVPAADDDDQYLLLGLTEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 415 RGDYENLYGAAMRGDRESCLLYVDQLKQRCVEGFKEGSLGIEQLAGVDGLCEWVIKAIGASDPVLTYHVNLSVFTSIPDF 494
Cdd:PLN02439 321 RADYENLYAAADRGDYEECLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVGASDPVATYHINLSVFTSIPDF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 495 WGIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGGESSLPLHEMDNNGcsGGRYYLGMFLGGAYEEALGGVHN 574
Cdd:PLN02439 401 WAIGQLFPIVPLHRLDERPTVRGILSDLTCDSDGKIDKFIGGEGSLPLHELEKNG--GGPYYLGMFLGGAYQEALGSLHN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 575 LFGGPSVVRVLQSDGPHGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAEEprnnnnkaCGDKGNDKLVVASCLAKS 654
Cdd:PLN02439 479 LFGGPSVVRVSQSDGPGGFAVTRAVPGQSCADVLRAMQHEPELMFETLKHRAEE--------YVHKGGLSGAVAANLARS 550
|
....*....
gi 15227223 655 FNNMPYLSM 663
Cdd:PLN02439 551 FHNMPYLSA 559
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
34-662 |
0e+00 |
|
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to putrescine. One is decarboxylation by this enzyme followed by removal of the urea moeity by agmatinase. In the other, the ureohydrolase (arginase) acts first, followed by ornithine decarboxylase. This pathway leads to spermidine biosynthesis, hence the gene symbol speA. A distinct biodegradative form is also pyridoxal phosphate-dependent but is not similar in sequence. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 273532 [Multi-domain] Cd Length: 624 Bit Score: 924.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 34 WSPSLSSSLYRIDGWGAPYFAANSSGNISVRPHGSNTLphQDIDLMKVVKKVtdpSGLGLQLPLIVRFPDVLKNRLECLQ 113
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTL--QRIDLLELVKQV---EARGLQLPLLVRFPDILQHRIRSLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 114 SAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLCKgnPEAFLVCNGFKDSEYI 193
Cdd:TIGR01273 76 AAFKNAIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGKGEPYGLEAGSKPELMAAMAYATK--PGAPIVCNGYKDREYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 194 SLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQILRVVRKLSQV 273
Cdd:TIGR01273 154 ELALIGRKLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 274 GMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSgESDLSVAYSLEEYAAAV 353
Cdd:TIGR01273 234 GLLDSLQLLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSS-SSDCSVNYGLEEYANDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 354 VASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAGQQHETPtDHQFMlEGYSEEVRgDYENLYGAAMRGDRESC 433
Cdd:TIGR01273 313 VQALREICEEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEYDP-DPKIA-EDAPPLVR-TLRELYGPIDRRSAIEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 434 LLYVDQLKQRCVEGFKEGSLGIEQLAGVDGLCEWVIKAIG----------------ASDPVLTYHVNLSVFTSIPDFWGI 497
Cdd:TIGR01273 390 LHDAQHLKEEAHEGFKLGYLDLEERAWAEQLYLSICHKVHqlsaknkdhrpildelQERLADKYFVNFSVFQSLPDAWGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 498 DQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGG---ESSLPLHEMDNngcsGGRYYLGMFLGGAYEEALGGVHN 574
Cdd:TIGR01273 470 DQLFPIMPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGqgiTSTLPLHELDP----DEGYFLGFFLVGAYQEILGDMHN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 575 LFGGPSVVRVLQSDGPhGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAeeprnNNNKacgDKGNDKLVVASCLAKS 654
Cdd:TIGR01273 546 LFGDTSAVRVVFDGDG-GYEVELIREGDTTEDMLRYVQYDPKELLTLYRDKV-----ANNK---LDAEEKKQFLEELEAG 616
|
....*...
gi 15227223 655 FNNMPYLS 662
Cdd:TIGR01273 617 LSGYPYLS 624
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
34-628 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 732.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 34 WSPSLSSSLYRIDGWGAPYFAANSSGNISVRPHGSntlPHQDIDLMKVVKKVTDpsgLGLQLPLIVRFPDVLKNRLECLQ 113
Cdd:COG1166 5 WTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD---PGPSIDLYELVEELRE---RGLSLPVLLRFPDILRDRVERLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 114 SAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLckGNPEAFLVCNGFKDSEYI 193
Cdd:COG1166 79 EAFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALL--DDPGSLIICNGYKDREYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 194 SLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQILRVVRKLSQV 273
Cdd:COG1166 157 RLALLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 274 GMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSgESDLSVAYSLEEYAAAV 353
Cdd:COG1166 237 GMLDCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRS-NSDSSMNYSLQEYANDV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 354 VASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAGQQHETPtDHQFMLEGYSEEVRgdyeNLYGAAMRGDRESC 433
Cdd:COG1166 316 VYAIKEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEP-PPPAPPEDAHELLR----NLWETYESLTPRNL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 434 L-LYVD--QLKQRCVEGFKEGSLGIEQLAGVDGL----CEWVIKAIGASDPV------L------TYHVNLSVFTSIPDF 494
Cdd:COG1166 391 QeCYHDalQYKEEARSLFNLGYLSLEERALAEQLywaiCRKIRELLDPLEYHpeeldeLnekladKYFCNFSLFQSLPDS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 495 WGIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGG---ESSLPLHEMDNngcsGGRYYLGMFLGGAYEEALGG 571
Cdd:COG1166 471 WAIDQLFPIMPIHRLDEEPTRRAVLADITCDSDGKIDQFIDGqgvKSTLPLHPLKP----GEPYYLGVFLVGAYQEILGD 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 15227223 572 VHNLFGGPSVVRV-LQSDGphGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAEE 628
Cdd:COG1166 547 LHNLFGDTNAVHVrLDEDG--GYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQAEQ 602
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
92-584 |
0e+00 |
|
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: 613.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 92 GLQLPLIVRFPDVLKNRLECLQSAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMS 171
Cdd:cd06830 2 GYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 172 CLCkgNPEAFLVCNGFKDSEYISLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSG 251
Cdd:cd06830 82 LLK--TPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 252 EKGKFGLTTVQILRVVRKLSQVGMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYD 331
Cdd:cd06830 160 DRSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 332 GSKSGeSDLSVAYSLEEYAAAVVASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVsagqqhetptdhqfmlegys 411
Cdd:cd06830 240 GSRSS-SDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVL-------------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 412 eevrgdyenlygaamrgdrescllyvdqlkqrcvegfkegslgieqlaGVDGLCEWvikaigasdpvltYHVNLSVFTSI 491
Cdd:cd06830 299 ------------------------------------------------GVKRLADW-------------YFCNFSLFQSL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 492 PDFWGIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGGESSLPLHEMDNNGcSGGRYYLGMFLGGAYEEALGG 571
Cdd:cd06830 318 PDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLR-KDEPYYLGFFLVGAYQEILGD 396
|
490
....*....|...
gi 15227223 572 VHNLFGGPSVVRV 584
Cdd:cd06830 397 LHNLFGDTNAVHV 409
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
132-381 |
5.92e-33 |
|
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: 127.01 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 132 VYPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAMSClcKGNPEAFLVCNGFKDSEYISLALFGRKlelnTVIVLE 211
Cdd:pfam02784 21 FYAVKCNSDPAVLRLLAELGTGF----DCASKGELERVLAA--GVPPERIIFANPCKQRSFLRYALEVGV----GCVTVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 212 QEEELDLVIDLSQKMNVrpviGLRAKLRTKHSGHFGSTsgekgKFGLTTVQILRVVRKLSQvgmLDCLQL--LHFHIGSQ 289
Cdd:pfam02784 91 NVDELEKLARLAPEARV----LLRIKPDDSAATCPLSS-----KFGADLDEDVEALLEAAK---LLNLQVvgVSFHVGSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 290 IPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYdgsksgeSDLSVAYSLEEYAAAVVASVRFVCdqKSVKHP 369
Cdd:pfam02784 159 CTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDY-------TEGEEPLDFEEYANVINEALEEYF--PGDPGV 229
|
250
....*....|..
gi 15227223 370 VICSESGRAIVS 381
Cdd:pfam02784 230 TIIAEPGRYFVA 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02439 |
PLN02439 |
arginine decarboxylase |
97-663 |
0e+00 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 1102.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 97 LIVRFPDVLKNRLECLQSAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLCKG 176
Cdd:PLN02439 1 LIVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPFRFGLEAGSKPELLLAMSCLCKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 177 NPEAFLVCNGFKDSEYISLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKF 256
Cdd:PLN02439 81 SPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 257 GLTTVQILRVVRKLSQVGMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSG 336
Cdd:PLN02439 161 GLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 337 ESDLSVAYSLEEYAAAVVASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAG--QQHETPTDHQFMLEGYSEEV 414
Cdd:PLN02439 241 SSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASkrGVPAADDDDQYLLLGLTEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 415 RGDYENLYGAAMRGDRESCLLYVDQLKQRCVEGFKEGSLGIEQLAGVDGLCEWVIKAIGASDPVLTYHVNLSVFTSIPDF 494
Cdd:PLN02439 321 RADYENLYAAADRGDYEECLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVGASDPVATYHINLSVFTSIPDF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 495 WGIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGGESSLPLHEMDNNGcsGGRYYLGMFLGGAYEEALGGVHN 574
Cdd:PLN02439 401 WAIGQLFPIVPLHRLDERPTVRGILSDLTCDSDGKIDKFIGGEGSLPLHELEKNG--GGPYYLGMFLGGAYQEALGSLHN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 575 LFGGPSVVRVLQSDGPHGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAEEprnnnnkaCGDKGNDKLVVASCLAKS 654
Cdd:PLN02439 479 LFGGPSVVRVSQSDGPGGFAVTRAVPGQSCADVLRAMQHEPELMFETLKHRAEE--------YVHKGGLSGAVAANLARS 550
|
....*....
gi 15227223 655 FNNMPYLSM 663
Cdd:PLN02439 551 FHNMPYLSA 559
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
34-662 |
0e+00 |
|
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to putrescine. One is decarboxylation by this enzyme followed by removal of the urea moeity by agmatinase. In the other, the ureohydrolase (arginase) acts first, followed by ornithine decarboxylase. This pathway leads to spermidine biosynthesis, hence the gene symbol speA. A distinct biodegradative form is also pyridoxal phosphate-dependent but is not similar in sequence. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 273532 [Multi-domain] Cd Length: 624 Bit Score: 924.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 34 WSPSLSSSLYRIDGWGAPYFAANSSGNISVRPHGSNTLphQDIDLMKVVKKVtdpSGLGLQLPLIVRFPDVLKNRLECLQ 113
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTL--QRIDLLELVKQV---EARGLQLPLLVRFPDILQHRIRSLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 114 SAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLCKgnPEAFLVCNGFKDSEYI 193
Cdd:TIGR01273 76 AAFKNAIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGKGEPYGLEAGSKPELMAAMAYATK--PGAPIVCNGYKDREYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 194 SLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQILRVVRKLSQV 273
Cdd:TIGR01273 154 ELALIGRKLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 274 GMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSgESDLSVAYSLEEYAAAV 353
Cdd:TIGR01273 234 GLLDSLQLLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSS-SSDCSVNYGLEEYANDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 354 VASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAGQQHETPtDHQFMlEGYSEEVRgDYENLYGAAMRGDRESC 433
Cdd:TIGR01273 313 VQALREICEEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEYDP-DPKIA-EDAPPLVR-TLRELYGPIDRRSAIEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 434 LLYVDQLKQRCVEGFKEGSLGIEQLAGVDGLCEWVIKAIG----------------ASDPVLTYHVNLSVFTSIPDFWGI 497
Cdd:TIGR01273 390 LHDAQHLKEEAHEGFKLGYLDLEERAWAEQLYLSICHKVHqlsaknkdhrpildelQERLADKYFVNFSVFQSLPDAWGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 498 DQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGG---ESSLPLHEMDNngcsGGRYYLGMFLGGAYEEALGGVHN 574
Cdd:TIGR01273 470 DQLFPIMPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGqgiTSTLPLHELDP----DEGYFLGFFLVGAYQEILGDMHN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 575 LFGGPSVVRVLQSDGPhGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAeeprnNNNKacgDKGNDKLVVASCLAKS 654
Cdd:TIGR01273 546 LFGDTSAVRVVFDGDG-GYEVELIREGDTTEDMLRYVQYDPKELLTLYRDKV-----ANNK---LDAEEKKQFLEELEAG 616
|
....*...
gi 15227223 655 FNNMPYLS 662
Cdd:TIGR01273 617 LSGYPYLS 624
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
34-628 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 732.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 34 WSPSLSSSLYRIDGWGAPYFAANSSGNISVRPHGSntlPHQDIDLMKVVKKVTDpsgLGLQLPLIVRFPDVLKNRLECLQ 113
Cdd:COG1166 5 WTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD---PGPSIDLYELVEELRE---RGLSLPVLLRFPDILRDRVERLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 114 SAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLckGNPEAFLVCNGFKDSEYI 193
Cdd:COG1166 79 EAFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALL--DDPGSLIICNGYKDREYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 194 SLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQILRVVRKLSQV 273
Cdd:COG1166 157 RLALLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 274 GMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSgESDLSVAYSLEEYAAAV 353
Cdd:COG1166 237 GMLDCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRS-NSDSSMNYSLQEYANDV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 354 VASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVSAGQQHETPtDHQFMLEGYSEEVRgdyeNLYGAAMRGDRESC 433
Cdd:COG1166 316 VYAIKEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEP-PPPAPPEDAHELLR----NLWETYESLTPRNL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 434 L-LYVD--QLKQRCVEGFKEGSLGIEQLAGVDGL----CEWVIKAIGASDPV------L------TYHVNLSVFTSIPDF 494
Cdd:COG1166 391 QeCYHDalQYKEEARSLFNLGYLSLEERALAEQLywaiCRKIRELLDPLEYHpeeldeLnekladKYFCNFSLFQSLPDS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 495 WGIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGG---ESSLPLHEMDNngcsGGRYYLGMFLGGAYEEALGG 571
Cdd:COG1166 471 WAIDQLFPIMPIHRLDEEPTRRAVLADITCDSDGKIDQFIDGqgvKSTLPLHPLKP----GEPYYLGVFLVGAYQEILGD 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 15227223 572 VHNLFGGPSVVRV-LQSDGphGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAEE 628
Cdd:COG1166 547 LHNLFGDTNAVHVrLDEDG--GYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQAEQ 602
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
34-628 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 713.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 34 WSPSLSSSLYRIDGWGAPYFAANSSGNISVRPHGSntlPHQDIDLMKVVKKVTDPsglGLQLPLIVRFPDVLKNRLECLQ 113
Cdd:PRK05354 9 WSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGD---PGASIDLAELVKELRER---GLRLPLLLRFPDILQDRVRSLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 114 SAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMSCLckGNPEAFLVCNGFKDSEYI 193
Cdd:PRK05354 83 AAFKKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPYNLGLEAGSKPELMAVLALA--GDPGALIVCNGYKDREYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 194 SLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQILRVVRKLSQV 273
Cdd:PRK05354 161 RLALIGRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLREA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 274 GMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSgESDLSVAYSLEEYAAAV 353
Cdd:PRK05354 241 GLLDCLQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRS-QSDSSVNYSLQEYANDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 354 VASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVsaGQQHETPTDHQFMLEGYSEEVRGDYENLYGAAMRGDREsc 433
Cdd:PRK05354 320 VYTLKEICEEHGVPHPTIISESGRALTAHHAVLVFNVL--GVESQEYEEPPAPAEDAPPLLQNLWETYQEISERNLQE-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 434 lLYVD--QLKQRCVEGFKEGSLGIEQLAGVDGL----CEWVIKAIGASD---PVL---------TYHVNLSVFTSIPDFW 495
Cdd:PRK05354 396 -IYHDaqQDLEEALTLFALGYLSLQERAWAEQLywaiCRKIQKLLDPKNrhpPELdelqerladKYYVNFSLFQSLPDAW 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 496 GIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGG---ESSLPLHEMDNngcsGGRYYLGMFLGGAYEEALGGV 572
Cdd:PRK05354 475 AIDQLFPIMPLHRLDEEPTRRAVLADITCDSDGKIDQFIDGqgiKTTLPLHELDP----GEPYYLGFFLVGAYQEILGDM 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 15227223 573 HNLFGGPSVVRVLQSDGpHGFAVTRAVMGQSSADVLRAMQHEPELMFQTLKHRAEE 628
Cdd:PRK05354 551 HNLFGDTNAVHVRVDED-GGYEIEHVIEGDTVADVLEYVQYDPKELLERLREKAVK 605
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
92-584 |
0e+00 |
|
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: 613.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 92 GLQLPLIVRFPDVLKNRLECLQSAFDYAIQSQGYDSHYQGVYPVKCNQDRFIIEDIVEFGSGFRFGLEAGSKPEILLAMS 171
Cdd:cd06830 2 GYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 172 CLCkgNPEAFLVCNGFKDSEYISLALFGRKLELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSG 251
Cdd:cd06830 82 LLK--TPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 252 EKGKFGLTTVQILRVVRKLSQVGMLDCLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYD 331
Cdd:cd06830 160 DRSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 332 GSKSGeSDLSVAYSLEEYAAAVVASVRFVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVsagqqhetptdhqfmlegys 411
Cdd:cd06830 240 GSRSS-SDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVL-------------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 412 eevrgdyenlygaamrgdrescllyvdqlkqrcvegfkegslgieqlaGVDGLCEWvikaigasdpvltYHVNLSVFTSI 491
Cdd:cd06830 299 ------------------------------------------------GVKRLADW-------------YFCNFSLFQSL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 492 PDFWGIDQLFPIVPIHKLDQRPAARGILSDLTCDSDGKINKFIGGESSLPLHEMDNNGcSGGRYYLGMFLGGAYEEALGG 571
Cdd:cd06830 318 PDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLR-KDEPYYLGFFLVGAYQEILGD 396
|
490
....*....|...
gi 15227223 572 VHNLFGGPSVVRV 584
Cdd:cd06830 397 LHNLFGDTNAVHV 409
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
96-582 |
2.57e-47 |
|
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: 171.33 E-value: 2.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 96 PLIVRFPDVLKNRLECLQSAFDyaiqsqgydSHYQGVYPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAmscLCK 175
Cdd:cd06810 2 PFYVYDLDIIRAHYAALKEALP---------SGVKLFYAVKANPNPHVLRTLAEAGTGF----DVASKGELALA---LAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 176 GNPEAFLVCNG-FKDSEYISLALfgrKLELNTvIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKG 254
Cdd:cd06810 66 GVPPERIIFTGpAKSVSEIEAAL---ASGVDH-IVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLKS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 255 KFGLTTVQILRVVRKLSQVGMLdcLQLLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGsk 334
Cdd:cd06810 142 KFGLSLSEARAALERAKELDLR--LVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 335 sgesdlsVAYSLEEYAAAVVASVRFVCDQKSVKHpvICSESGRAIVSHHSVLIFEAVSagqqhetptdhqfmlegyseev 414
Cdd:cd06810 218 -------QPLDFEEYAALINPLLKKYFPNDPGVT--LILEPGRYIVAQAGVLVTRVVA---------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 415 rgdyenlygaamrgdrescllyvdqlkqrcvegfkegslgieqlagvdglcewvIKAIGASDpvlTYHVNLSVFTSIPDF 494
Cdd:cd06810 267 ------------------------------------------------------VKVNGGRF---FAVVDGGMNHSFRPA 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 495 WGIDQLFPIVPIHKLD-QRPAARGILSDLTCDSDGKInkfigGESSLPLhEMDNNgcsggrYYLGMFLGGAYEEALGGVH 573
Cdd:cd06810 290 LAYDAYHPITPLKAPGpDEPLVPATLAGPLCDSGDVI-----GRDRLLP-ELEVG------DLLVFEDMGAYGFSESSNF 357
|
....*....
gi 15227223 574 NLFGGPSVV 582
Cdd:cd06810 358 NSHPRPAEY 366
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
132-381 |
5.92e-33 |
|
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: 127.01 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 132 VYPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAMSClcKGNPEAFLVCNGFKDSEYISLALFGRKlelnTVIVLE 211
Cdd:pfam02784 21 FYAVKCNSDPAVLRLLAELGTGF----DCASKGELERVLAA--GVPPERIIFANPCKQRSFLRYALEVGV----GCVTVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 212 QEEELDLVIDLSQKMNVrpviGLRAKLRTKHSGHFGSTsgekgKFGLTTVQILRVVRKLSQvgmLDCLQL--LHFHIGSQ 289
Cdd:pfam02784 91 NVDELEKLARLAPEARV----LLRIKPDDSAATCPLSS-----KFGADLDEDVEALLEAAK---LLNLQVvgVSFHVGSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 290 IPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYdgsksgeSDLSVAYSLEEYAAAVVASVRFVCdqKSVKHP 369
Cdd:pfam02784 159 CTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDY-------TEGEEPLDFEEYANVINEALEEYF--PGDPGV 229
|
250
....*....|..
gi 15227223 370 VICSESGRAIVS 381
Cdd:pfam02784 230 TIIAEPGRYFVA 241
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
69-387 |
1.09e-28 |
|
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: 119.10 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 69 NTLPHQDIDLMKVVKKV-TdpsglglqlPLIVRFPDVLKNRLECLQSAFDYAiqsqGYDSHYqgvyPVKCNQDRFIIEDI 147
Cdd:COG0019 8 GELTIEGVDLAELAEEYgT---------PLYVYDEAALRRNLRALREAFPGS----GAKVLY----AVKANSNLAVLRLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 148 VEFGSGFrfglEAGSKPEILLAMSCLCKGNpEAFLVCNGFKDSEyISLALfgrklELN-TVIVLEQEEELDLVIDLSQKM 226
Cdd:COG0019 71 AEEGLGA----DVVSGGELRLALAAGFPPE-RIVFSGNGKSEEE-LEEAL-----ELGvGHINVDSLSELERLAELAAEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 227 NVRPVIGLRAKLRTKHSGH-FGSTSGEKGKFGLTTVQILRVVRKLSQVGMLDCLQLlHFHIGSQIPSTALLSDGVAEAAQ 305
Cdd:COG0019 140 GKRAPVGLRVNPGVDAGTHeYISTGGKDSKFGIPLEDALEAYRRAAALPGLRLVGL-HFHIGSQILDLEPFEEALERLLE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 306 LYCELVRLGAHMKVIDIGGGLGIDYdgsKSGESDLsvaySLEEYAAAVVASVRFVCDqksvKHPVICSESGRAIVSHHSV 385
Cdd:COG0019 219 LAEELRELGIDLEWLDLGGGLGIPY---TEGDEPP----DLEELAAAIKEALEELCG----LGPELILEPGRALVGNAGV 287
|
..
gi 15227223 386 LI 387
Cdd:COG0019 288 LL 289
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
133-389 |
3.92e-27 |
|
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: 112.97 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 133 YPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAMSClckGNPEAFLVCNG-FKDSEYISLALfgrklELN-TVIVL 210
Cdd:pfam00278 28 YAVKANPNPAVLRLLAELGAGF----DVASGGELERALAA---GVDPERIVFAGpGKTDSEIRYAL-----EAGvLCFNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 211 EQEEELDLVIDLSQKMNVRpvIGLRAKLRTKHSGHFGSTSGEKGKFGLTTVQILRVVRKLSQVGmldcLQL--LHFHIGS 288
Cdd:pfam00278 96 DSEDELEKIAKLAPELVAR--VALRINPDVDAGTHKISTGGLSSKFGIDLEDAPELLALAKELG----LNVvgVHFHIGS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 289 QIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKsgesdlsvAYSLEEYAAAVVAsvrfVCDQKSVKH 368
Cdd:pfam00278 170 QITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEP--------PPDFEEYAAAIRE----ALDEYFPPD 237
|
250 260
....*....|....*....|.
gi 15227223 369 PVICSESGRAIVSHHSVLIFE 389
Cdd:pfam00278 238 LEIIAEPGRYLVANAGVLVTR 258
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
96-392 |
2.74e-26 |
|
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: 112.00 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 96 PLIVRFPDVLKNRLECLQSAFDyaiqsqgydSHYQGVYPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAmscLCK 175
Cdd:TIGR01048 26 PLYVYDEDTIRRRFRAYKEAFG---------GRSLVCYAVKANSNLAVLRLLAELGSGF----DVVSGGELYRA---LAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 176 GNPEAFLVCNGF-KDSEYISLALfgrklELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGH-FGSTSGEK 253
Cdd:TIGR01048 90 GFPPEKIVFSGNgKSRAELERAL-----ELGICINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHpYISTGLKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 254 GKFGLTTVQILRVVRKLSQVGMLDCLQLlHFHIGSQIPSTALLSDGVAEAAQLYCELvRLGAHMKVIDIGGGLGIDYDGS 333
Cdd:TIGR01048 165 SKFGIDVEEALEAYLYALQLPHLELVGI-HCHIGSQITDLSPFVEAAEKVVKLAESL-AEGIDLEFLDLGGGLGIPYTPE 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15227223 334 KSgesdlsvAYSLEEYAAAVVASVRFVCDQKSvkHPVICSESGRAIVSHHSVLIFEAVS 392
Cdd:TIGR01048 243 EE-------PPDLSEYAQAILNALEGYADLGL--DPKLILEPGRSIVANAGVLLTRVGF 292
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
96-387 |
6.42e-24 |
|
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: 104.10 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 96 PLIVRFPDVLKNRLECLQSAFdyaiQSQGYDSHYQgvypVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAMSCLCK 175
Cdd:cd06828 4 PLYVYDEATIRENYRRLKEAF----SGPGFKICYA----VKANSNLAILKLLAEEGLGA----DVVSGGELYRALKAGFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 176 GNpEAFLVCNGFKDSEyISLALfgrklELNTV-IVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGHFG-STSGEK 253
Cdd:cd06828 72 PE-RIVFTGNGKSDEE-LELAL-----ELGILrINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYiSTGGKD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 254 GKFGLTTVQILRVVRKLSQvgmLDCLQL--LHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYD 331
Cdd:cd06828 145 SKFGIPLEQALEAYRRAKE---LPGLKLvgLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYR 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15227223 332 GSKsgesdlsVAYSLEEYAAAVVASVRFVCDQKSVKHpvICSESGRAIVSHHSVLI 387
Cdd:cd06828 222 DED-------EPLDIEEYAEAIAEALKELCEGGPDLK--LIIEPGRYIVANAGVLL 268
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
103-392 |
4.03e-16 |
|
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: 80.77 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 103 DVLKNRLECLQSAFDyaiqsqgydSHYQGV---YPVKCNQDRFIIEDIVEFGsgfrFGLEAGSKPEILLAMSclcKGNPE 179
Cdd:cd06841 15 DALRENYRELLGAFK---------KRYPNVviaYSYKTNYLPAICKILHEEG----GYAEVVSAMEYELALK---LGVPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 180 AFLVCNG-FKDSEYISLALfgrklELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTkhSGHFGStsgekgKFGL 258
Cdd:cd06841 79 KRIIFNGpYKSKEELEKAL-----EEGALINIDSFDELERILEIAKELGRVAKVGIRLNMNY--GNNVWS------RFGF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 259 TTVQILRVVRKLSQVGMLDCLQL--LHFHIGSQIPSTallsDGVAEAAQLYCEL-VRL-GAHMKVIDIGGGLGIDYDgSK 334
Cdd:cd06841 146 DIEENGEALAALKKIQESKNLSLvgLHCHVGSNILNP----EAYSAAAKKLIELlDRLfGLELEYLDLGGGFPAKTP-LS 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15227223 335 SGESDLSVAYSLEEYAAAVVASVRfVCDQKSVKHPVICSESGRAIVSHHSVLIFEAVS 392
Cdd:cd06841 221 LAYPQEDTVPDPEDYAEAIASTLK-EYYANKENKPKLILEPGRALVDDAGYLLGRVVA 277
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
133-387 |
7.25e-16 |
|
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: 79.85 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 133 YPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAMSC------LCKGNPeaflvcngFKDSEYISLALfgrklELN- 205
Cdd:cd00622 30 YAVKCNPDPAVLRTLAALGAGF----DCASKGEIELVLGLgvsperIIFANP--------CKSISDIRYAA-----ELGv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 206 TVIVLEQEEELDLVIDLSQKMNVRpvigLRAKLRTKHSGH-FGstsgekGKFGLT---TVQILRVVRK--LSQVGmldcl 279
Cdd:cd00622 93 RLFTFDSEDELEKIAKHAPGAKLL----LRIATDDSGALCpLS------RKFGADpeeARELLRRAKElgLNVVG----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 280 qlLHFHIGSQIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGsksgesdlsVAYSLEEYAAAVVASV-R 358
Cdd:cd00622 158 --VSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDG---------VVPSFEEIAAVINRALdE 226
|
250 260
....*....|....*....|....*....
gi 15227223 359 FVCDQksvkHPVICSESGRAIVSHHSVLI 387
Cdd:cd00622 227 YFPDE----GVRIIAEPGRYLVASAFTLA 251
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
208-380 |
7.35e-12 |
|
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: 67.62 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 208 IVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTkHSGHFGSTSGEKGK-FGLTTVQILRVVRKLSQVGMLDcLQLLHFHI 286
Cdd:cd06839 101 INVESLEELERIDALAEEHGVVARVALRINPDF-ELKGSGMKMGGGPSqFGIDVEELPAVLARIAALPNLR-FVGLHIYP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 287 GSQIPSTALLSDGVAEAAQLYCELV-RLGAHMKVIDIGGGLGIDYDgskSGESDLsvaySLEEYAAAVVASVRFVCDQKS 365
Cdd:cd06839 179 GTQILDADALIEAFRQTLALALRLAeELGLPLEFLDLGGGFGIPYF---PGETPL----DLEALGAALAALLAELGDRLP 251
|
170
....*....|....*
gi 15227223 366 VKHPVIcsESGRAIV 380
Cdd:cd06839 252 GTRVVL--ELGRYLV 264
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
135-387 |
2.75e-10 |
|
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: 62.80 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 135 VKCNQDRFIIEDIVEFGsgfrFGLEAGSKPEILLAMSCLCKgnPEAFLVcngfkDSEYISLALFGRKLELNTVIVLEQEE 214
Cdd:cd06836 34 VKANPLVPVLRLLAEAG----AGAEVASPGELELALAAGFP--PERIVF-----DSPAKTRAELREALELGVAINIDNFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 215 ELDlVID--LSQKMNVRPVIGLRAKLRTKhSGHFG--STSGEKGKFG--LTTVQILRVVRKLSQVGMLDCLqllHFHIGS 288
Cdd:cd06836 103 ELE-RIDalVAEFKEASSRIGLRVNPQVG-AGKIGalSTATATSKFGvaLEDGARDEIIDAFARRPWLNGL---HVHVGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 289 QIPSTALLSDGVAEAAQLYCELVRLGAHMKV--IDIGGGLGIDYDGSksgesdlSVAYSLEEYAAAVVASV-RFVCDQKS 365
Cdd:cd06836 178 QGCELSLLAEGIRRVVDLAEEINRRVGRRQItrIDIGGGLPVNFESE-------DITPTFADYAAALKAAVpELFDGRYQ 250
|
250 260
....*....|....*....|..
gi 15227223 366 VKhpvicSESGRAIVSHHSVLI 387
Cdd:cd06836 251 LV-----TEFGRSLLAKCGTIV 267
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
96-330 |
3.53e-10 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.
Pssm-ID: 143509 [Multi-domain] Cd Length: 423 Bit Score: 62.66 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 96 PLIVRFPDVLKNRLECLQSAFD-YAIQSQGYdshyqgvYPVKCNQDRFIIEDIVEFGsgfrFGLEAGSKPEILLAMSCLC 174
Cdd:cd06842 11 PLNVLFPQTFRENIAALRAVLDrHGVDGRVY-------FARKANKSLALVRAAAAAG----IGVDVASLAELRQALAAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 175 KGNPeafLVCNG-FKDSEYISLALfgrklELNTVIVLEQEEELDLVIDLSQKMNVRPV-IGLRAklrtkhsGHFGSTSge 252
Cdd:cd06842 80 RGDR---IVATGpAKTDEFLWLAV-----RHGATIAVDSLDELDRLLALARGYTTGPArVLLRL-------SPFPASL-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15227223 253 KGKFGLTTVQILRVVRKLSQVGMLDCLQLLHFHI-GSQIPSTALLsdgVAEAAQLYCELVRLGAHMKVIDIGGGLGIDY 330
Cdd:cd06842 143 PSRFGMPAAEVRTALERLAQLRERVRLVGFHFHLdGYSAAQRVAA---LQECLPLIDRARALGLAPRFIDIGGGFPVSY 218
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
130-387 |
9.54e-09 |
|
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: 57.83 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 130 QGVYPVKCNQDRFIIEDIVEFGsgfrFGLEAGSKPEILLAMSCLCKGNPEAFLVCNGFKD-SEYISLALFGRKLELNTVI 208
Cdd:cd06840 37 SLFYAIKANPHPDVLRTLEEAG----LGFECVSIGELDLVLKLFPDLDPRRVLFTPNFAArSEYEQALELGVNVTVDNLH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 209 VLEQ------EEELDLVIDLSQKMNvrpviglraklrtkHSGHFgSTSGEKGKFGLTTVQILRVVRKLSQVGMLdcLQLL 282
Cdd:cd06840 113 PLREwpelfrGREVILRIDPGQGEG--------------HHKHV-RTGGPESKFGLDVDELDEARDLAKKAGII--VIGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 283 HFHIGSQIPSTALLsdgvaeaAQLYCELVRLGAHM---KVIDIGGGLGIDYdgsKSGESDLSVAySLEEYAAAVVAsvrf 359
Cdd:cd06840 176 HAHSGSGVEDTDHW-------ARHGDYLASLARHFpavRILNVGGGLGIPE---APGGRPIDLD-ALDAALAAAKA---- 240
|
250 260 270
....*....|....*....|....*....|
gi 15227223 360 vcdqksvKHP--VICSESGRAIVSHHSVLI 387
Cdd:cd06840 241 -------AHPqyQLWMEPGRFIVAESGVLL 263
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
133-334 |
7.06e-08 |
|
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: 53.48 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 133 YPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAMSclcKGNPEAFLVCNG-FKDSEYISLALfgrklELNT-VIVL 210
Cdd:cd06808 20 AVVKANANPEVARTLAALGTGF----DVASLGEALLLRA---AGIPPEPILFLGpCKQVSELEDAA-----EQGViVVTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 211 EQEEELDLVIDLSQKMNvrpvIGLRAKLRTkhsghfgSTSGEKGKFGLTtVQILRVVrkLSQVGMLDCLQL--LHFHIGS 288
Cdd:cd06808 88 DSLEELEKLEEAALKAG----PPARVLLRI-------DTGDENGKFGVR-PEELKAL--LERAKELPHLRLvgLHTHFGS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15227223 289 QIPSTALLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSK 334
Cdd:cd06808 154 ADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQEL 199
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
123-330 |
3.20e-05 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 46.71 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 123 QGYDSHYQGV-----YPVKCNQDRFIIEDIVEFGSG--------FRFGLEAGSKPEillamSCLCKGNPEAFlvcngfkd 189
Cdd:PLN02537 33 EAYKEALEGLrsiigYAIKANNNLKILEHLRELGCGavlvsgneLRLALRAGFDPT-----RCIFNGNGKLL-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 190 sEYISLALfgrklELNTVIVLEQEEELDLVIDLSQKMNVRPVIGLRAKLRTKHSGH-FGSTSGEKGKFGLTTVQI---LR 265
Cdd:PLN02537 100 -EDLVLAA-----QEGVFVNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHpYVATGNKNSKFGIRNEKLqwfLD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227223 266 VVRK----LSQVGMldclqllHFHIGSQIPSTALLSDgvaeAAQLYCELVRL----GAHMKVIDIGGGLGIDY 330
Cdd:PLN02537 174 AVKAhpneLKLVGA-------HCHLGSTITKVDIFRD----AAVLMVNYVDEiraqGFELSYLNIGGGLGIDY 235
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
248-387 |
4.00e-05 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 47.00 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 248 STSGEKGKFGLTTVQILRVVRKLSQVGMLdcLQLLHFHIGSQIpstaLLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLG 327
Cdd:PRK08961 634 RTGGKESKFGLSQTRIDEFVDLAKTLGIT--VVGLHAHLGSGI----ETGEHWRRMADELASFARRFPDVRTIDLGGGLG 707
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227223 328 IDYdgsKSGESDLSVaysleEYAAAVVASVrfvcdqKSVkHP--VICSESGRAIVSHHSVLI 387
Cdd:PRK08961 708 IPE---SAGDEPFDL-----DALDAGLAEV------KAQ-HPgyQLWIEPGRYLVAEAGVLL 754
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|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
133-397 |
1.82e-04 |
|
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: 44.19 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 133 YPVKCNQDRFIIEDIVEFGSGFrfglEAGSKPEILLAMSClckgNPEAFLVCNG--FKDSEyISLALfGRKLELntvIVL 210
Cdd:cd06843 31 YAIKANSDPPILRALAPHVDGF----EVASGGEIAHVRAA----VPDAPLIFGGpgKTDSE-LAQAL-AQGVER---IHV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 211 EQEEELDLVIDLSQKMNVRPVIGLRAKLrtkHSGHFGSTS----GEKGKFGLTTVQILRVVRKLSQvgmLDCLQL--LHF 284
Cdd:cd06843 98 ESELELRRLNAVARRAGRTAPVLLRVNL---ALPDLPSSTltmgGQPTPFGIDEADLPDALELLRD---LPNIRLrgFHF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227223 285 HigsqipstaLLSDGVAEAAQL-----YCELVR-----LGAHMKVIDIGGGLGIDY-DGSKSGESDLSVAYsLEEYAAAV 353
Cdd:cd06843 172 H---------LMSHNLDAAAHLalvkaYLETARqwaaeHGLDLDVVNVGGGIGVNYaDPEEQFDWAGFCEG-LDQLLAEY 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15227223 354 VASVRFVcdqksvkhpvicSESGRAIVSHHSVLIFEAVSAGQQH 397
Cdd:cd06843 242 EPGLTLR------------FECGRYISAYCGYYVTEVLDLKRSH 273
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