|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
22-658 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 1144.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 22 MQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAELVKAREAQGQRLPALFCFPQILQHRLR 101
Cdd:PRK05354 1 MQEVAMSDWSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGD-PGASIDLAELVKELRERGLRLPLLLRFPDILQDRVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 102 SINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:PRK05354 80 SLNAAFKKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPynLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 180 IRLALVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILRA 259
Cdd:PRK05354 160 IRLALIGRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 260 AGHLESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNI 339
Cdd:PRK05354 240 AGLLDCLQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRSQSDSSVNYSLQEYANDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 340 IWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTEATPPAEDAARPLQSMWETWLEMhetgNRRSLRE 419
Cdd:PRK05354 320 VYTLKEICEEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYEEPPAPAEDAPPLLQNLWETYQEI----SERNLQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 420 WLHDSQMDLHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQKQLDPSNRaHRPIIDELQERMADKIYVNFSLFQSMPDAW 499
Cdd:PRK05354 396 IYHDAQQDLEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNR-HPPELDELQERLADKYYVNFSLFQSLPDAW 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 500 GIDQLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLF 579
Cdd:PRK05354 475 AIDQLFPIMPLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 580 GDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQ-VKNTGLDDALQQQFLEEFEAGLYGYTYLEDE 658
Cdd:PRK05354 555 GDTNAVHVRVDEDGGYEIEHVIEGDTVADVLEYVQYDPKELLERLREKaVKEGKLSPEERQQLLEELEAGLRGYTYLEDE 634
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
26-657 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 1086.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 26 AMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAELVKAREAQGQRLPALFCFPQILQHRLRSINA 105
Cdd:COG1166 1 PMMDWTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD-PGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 106 AFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLA 183
Cdd:COG1166 80 AFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPynFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 184 LVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILRAAGHL 263
Cdd:COG1166 160 LLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 264 ESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAI 343
Cdd:COG1166 240 DCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSNSDSSMNYSLQEYANDVVYAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 344 GDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTEA-TPPAEDAARPLQSMWETWLEMhetgNRRSLREWLH 422
Cdd:COG1166 320 KEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPpPAPPEDAHELLRNLWETYESL----TPRNLQECYH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 423 DSQMDLHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQKQLDPSNRaHRPIIDELQERMADKIYVNFSLFQSMPDAWGID 502
Cdd:COG1166 396 DALQYKEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEY-HPEELDELNEKLADKYFCNFSLFQSLPDSWAID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 503 QLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDT 582
Cdd:COG1166 475 QLFPIMPIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDT 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496081949 583 EAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQ----VKNTGLDDALQQQFLEEFEAGLYGYTYLED 657
Cdd:COG1166 555 NAVHVRLDEDGGYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQaeqaVRAGRLTPEERQRLLEEYEAGLRGYTYLED 633
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
30-656 |
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: 1028.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 30 QEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAELVKAREAQGQRLPALFCFPQILQHRLRSINAAFKR 109
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTLQRIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 110 ARESYGYNGDYFLVYPIKVNQHRRVIESLIHSG--EPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALVGE 187
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGkgEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 188 KMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILRAAGHLESLQ 267
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 268 LLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDAC 347
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSSSSDCSVNYGLEEYANDIVQALREIC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 348 EENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTEATPPAEDAARPLQsmweTWLEMHETGNRRSLREWLHDSQMD 427
Cdd:TIGR01273 321 EEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEYDPDPKIAEDAPPLVR----TLRELYGPIDRRSAIEILHDAQHL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 428 LHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQkQLDPSNRAHRPIIDELQERMADKIYVNFSLFQSMPDAWGIDQLFPV 507
Cdd:TIGR01273 397 KEEAHEGFKLGYLDLEERAWAEQLYLSICHKVH-QLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 508 MPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:TIGR01273 476 MPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRV 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496081949 588 FVFPDGSVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQVKNTGLDDALQQQFLEEFEAGLYGYTYLE 656
Cdd:TIGR01273 556 VFDGDGGYEVELIREGDTTEDMLRYVQYDPKELLTLYRDKVANNKLDAEEKKQFLEELEAGLSGYPYLS 624
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
82-587 |
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: 639.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 82 QGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVL 159
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRynIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 160 AHAGMTRSVIVCNGYKDREYIRLALVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGE 239
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 240 KSKFGLAATQVLQLVEILRAAGHLESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEG 319
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 320 TRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVerneyteatppaedaarplq 399
Cdd:cd06830 241 SRSSSDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGV-------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 400 smwetwlemhetgnrrslrewlhdsqmdlhdihigyssgtfnlqerawaeqlylnmchevqkqldpsnrahrpiidelqE 479
Cdd:cd06830 301 -------------------------------------------------------------------------------K 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 480 RMADKIYVNFSLFQSMPDAWGIDQLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPM 559
Cdd:cd06830 302 RLADWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYY 381
|
490 500
....*....|....*....|....*...
gi 496081949 560 LGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:cd06830 382 LGFFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
100-367 |
1.27e-74 |
|
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: 239.49 E-value: 1.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 100 LRSINAAFKRARESYGyngDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:pfam02784 1 LGSIERRHRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELG--TGFDCASKGELERVLAAGVPPERIIFANPCKQRSF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 180 IRLALVGEKMghkvYLVIEKMSEIAIVLEEAERlnvvPRLGVRARL-ASQGSGKWqssggeKSKFGLAatqVLQLVEILR 258
Cdd:pfam02784 76 LRYALEVGVG----CVTVDNVDELEKLARLAPE----ARVLLRIKPdDSAATCPL------SSKFGAD---LDEDVEALL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 259 AAGHLESLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvnygLNEYA 336
Cdd:pfam02784 139 EAAKLLNLQVvgVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD------FEEYA 212
|
250 260 270
....*....|....*....|....*....|.
gi 496081949 337 NNIIWAIGDACEenGLPHPTVITESGRAVTA 367
Cdd:pfam02784 213 NVINEALEEYFP--GDPGVTIIAEPGRYFVA 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
22-658 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 1144.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 22 MQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAELVKAREAQGQRLPALFCFPQILQHRLR 101
Cdd:PRK05354 1 MQEVAMSDWSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGD-PGASIDLAELVKELRERGLRLPLLLRFPDILQDRVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 102 SINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:PRK05354 80 SLNAAFKKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPynLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 180 IRLALVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILRA 259
Cdd:PRK05354 160 IRLALIGRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 260 AGHLESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNI 339
Cdd:PRK05354 240 AGLLDCLQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRSQSDSSVNYSLQEYANDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 340 IWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTEATPPAEDAARPLQSMWETWLEMhetgNRRSLRE 419
Cdd:PRK05354 320 VYTLKEICEEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYEEPPAPAEDAPPLLQNLWETYQEI----SERNLQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 420 WLHDSQMDLHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQKQLDPSNRaHRPIIDELQERMADKIYVNFSLFQSMPDAW 499
Cdd:PRK05354 396 IYHDAQQDLEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNR-HPPELDELQERLADKYYVNFSLFQSLPDAW 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 500 GIDQLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLF 579
Cdd:PRK05354 475 AIDQLFPIMPLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 580 GDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQ-VKNTGLDDALQQQFLEEFEAGLYGYTYLEDE 658
Cdd:PRK05354 555 GDTNAVHVRVDEDGGYEIEHVIEGDTVADVLEYVQYDPKELLERLREKaVKEGKLSPEERQQLLEELEAGLRGYTYLEDE 634
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
26-657 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 1086.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 26 AMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAELVKAREAQGQRLPALFCFPQILQHRLRSINA 105
Cdd:COG1166 1 PMMDWTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD-PGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 106 AFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLA 183
Cdd:COG1166 80 AFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPynFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 184 LVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILRAAGHL 263
Cdd:COG1166 160 LLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 264 ESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAI 343
Cdd:COG1166 240 DCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSNSDSSMNYSLQEYANDVVYAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 344 GDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTEA-TPPAEDAARPLQSMWETWLEMhetgNRRSLREWLH 422
Cdd:COG1166 320 KEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPpPAPPEDAHELLRNLWETYESL----TPRNLQECYH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 423 DSQMDLHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQKQLDPSNRaHRPIIDELQERMADKIYVNFSLFQSMPDAWGID 502
Cdd:COG1166 396 DALQYKEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEY-HPEELDELNEKLADKYFCNFSLFQSLPDSWAID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 503 QLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDT 582
Cdd:COG1166 475 QLFPIMPIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDT 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496081949 583 EAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQ----VKNTGLDDALQQQFLEEFEAGLYGYTYLED 657
Cdd:COG1166 555 NAVHVRLDEDGGYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQaeqaVRAGRLTPEERQRLLEEYEAGLRGYTYLED 633
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
30-656 |
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: 1028.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 30 QEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAELVKAREAQGQRLPALFCFPQILQHRLRSINAAFKR 109
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTLQRIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 110 ARESYGYNGDYFLVYPIKVNQHRRVIESLIHSG--EPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALVGE 187
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGkgEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 188 KMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILRAAGHLESLQ 267
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 268 LLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDAC 347
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSSSSDCSVNYGLEEYANDIVQALREIC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 348 EENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTEATPPAEDAARPLQsmweTWLEMHETGNRRSLREWLHDSQMD 427
Cdd:TIGR01273 321 EEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEYDPDPKIAEDAPPLVR----TLRELYGPIDRRSAIEILHDAQHL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 428 LHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQkQLDPSNRAHRPIIDELQERMADKIYVNFSLFQSMPDAWGIDQLFPV 507
Cdd:TIGR01273 397 KEEAHEGFKLGYLDLEERAWAEQLYLSICHKVH-QLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 508 MPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:TIGR01273 476 MPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRV 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496081949 588 FVFPDGSVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQVKNTGLDDALQQQFLEEFEAGLYGYTYLE 656
Cdd:TIGR01273 556 VFDGDGGYEVELIREGDTTEDMLRYVQYDPKELLTLYRDKVANNKLDAEEKKQFLEELEAGLSGYPYLS 624
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
82-587 |
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: 639.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 82 QGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVL 159
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRynIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 160 AHAGMTRSVIVCNGYKDREYIRLALVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGE 239
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 240 KSKFGLAATQVLQLVEILRAAGHLESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEG 319
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 320 TRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVerneyteatppaedaarplq 399
Cdd:cd06830 241 SRSSSDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGV-------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 400 smwetwlemhetgnrrslrewlhdsqmdlhdihigyssgtfnlqerawaeqlylnmchevqkqldpsnrahrpiidelqE 479
Cdd:cd06830 301 -------------------------------------------------------------------------------K 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 480 RMADKIYVNFSLFQSMPDAWGIDQLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGIATTMPMPEYDPENPPM 559
Cdd:cd06830 302 RLADWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYY 381
|
490 500
....*....|....*....|....*...
gi 496081949 560 LGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:cd06830 382 LGFFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
89-657 |
3.28e-159 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 469.55 E-value: 3.28e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 89 LFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAEL---MAVLAHaG 163
Cdd:PLN02439 2 IVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPfrFGLEAGSKPELllaMSCLCK-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 164 MTRSVIVCNGYKDREYIRLALVGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKF 243
Cdd:PLN02439 81 SPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 244 GLAATQVLQLVEILRAAGHLESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRS- 322
Cdd:PLN02439 161 GLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 323 QSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNeytEATPPAEDAARPLQSMW 402
Cdd:PLN02439 241 SSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASKR---GVPAADDDDQYLLLGLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 403 E----TWLEMHETGNRRSLREWLHDSQMDLHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQKQlDPSNRAHrpiidelq 478
Cdd:PLN02439 318 EelraDYENLYAAADRGDYEECLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVGAS-DPVATYH-------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 479 ermadkiyVNFSLFQSMPDAWGIDQLFPVMPLEGLNKSPERRAVLLDITCDSDGAIDHYVDGDGiatTMPMPEYDPEN-- 556
Cdd:PLN02439 389 --------INLSVFTSIPDFWAIGQLFPIVPLHRLDERPTVRGILSDLTCDSDGKIDKFIGGEG---SLPLHELEKNGgg 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 557 PPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVfPDG--SVEVELSDEGDTVADMLQYVQLDPNTLLTQFRDQVKNTGLD 634
Cdd:PLN02439 458 PYYLGMFLGGAYQEALGSLHNLFGGPSVVRVSQ-SDGpgGFAVTRAVPGQSCADVLRAMQHEPELMFETLKHRAEEYVHK 536
|
570 580
....*....|....*....|...
gi 496081949 635 DALQQQFLEEFEAGLYGYTYLED 657
Cdd:PLN02439 537 GGLSGAVAANLARSFHNMPYLSA 559
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
100-367 |
1.27e-74 |
|
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: 239.49 E-value: 1.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 100 LRSINAAFKRARESYGyngDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:pfam02784 1 LGSIERRHRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELG--TGFDCASKGELERVLAAGVPPERIIFANPCKQRSF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 180 IRLALVGEKMghkvYLVIEKMSEIAIVLEEAERlnvvPRLGVRARL-ASQGSGKWqssggeKSKFGLAatqVLQLVEILR 258
Cdd:pfam02784 76 LRYALEVGVG----CVTVDNVDELEKLARLAPE----ARVLLRIKPdDSAATCPL------SSKFGAD---LDEDVEALL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 259 AAGHLESLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvnygLNEYA 336
Cdd:pfam02784 139 EAAKLLNLQVvgVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD------FEEYA 212
|
250 260 270
....*....|....*....|....*....|.
gi 496081949 337 NNIIWAIGDACEenGLPHPTVITESGRAVTA 367
Cdd:pfam02784 213 NVINEALEEYFP--GDPGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
87-582 |
2.32e-46 |
|
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: 168.25 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 87 PALFCFPQILQHRLRSINAAFKraresygynGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLaHAGMTR 166
Cdd:cd06810 2 PFYVYDLDIIRAHYAALKEALP---------SGVKLFYAVKANPNPHVLRTLAEAG--TGFDVASKGELALAL-AAGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 167 SVIVCNGY-KDREYIRLALvgeKMGHKVyLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGL 245
Cdd:cd06810 70 ERIIFTGPaKSVSEIEAAL---ASGVDH-IVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLKSKFGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 246 AATQVLQLVEILRAAGhlESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGtrsqsd 325
Cdd:cd06810 146 SLSEARAALERAKELD--LRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 326 csVNYGLNEYANNIIWAIGDACEEngLPHPTVITESGRAVTAHHTVLVSNIIGVERNEyteatppaedaarplqsmwetw 405
Cdd:cd06810 218 --QPLDFEEYAALINPLLKKYFPN--DPGVTLILEPGRYIVAQAGVLVTRVVAVKVNG---------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 406 lemhetgnrrslrewlhdsqmdlhDIHIgyssgtfnlqerawaeqlylnmchevqkqldpsnrahrpiidelqermadkI 485
Cdd:cd06810 272 ------------------------GRFF---------------------------------------------------A 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 486 YVNFSLFQSMPDAWGIDQLFPVMPLEGLN-KSPERRAVLLDITCDSdgaidhyvdGDGIATTMPMPEydPENPPMLGFFM 564
Cdd:cd06810 277 VVDGGMNHSFRPALAYDAYHPITPLKAPGpDEPLVPATLAGPLCDS---------GDVIGRDRLLPE--LEVGDLLVFED 345
|
490
....*....|....*...
gi 496081949 565 VGAYQEILGNMHNLFGDT 582
Cdd:cd06810 346 MGAYGFSESSNFNSHPRP 363
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
103-386 |
4.90e-31 |
|
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: 124.90 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 103 INAAFKRARESYGYNgDYFLVYPIKVNQHRRVIEsLIHSgEPLGLEAGSKAELMAVLAhAGMTRSVIV--CNGyKDREYI 180
Cdd:cd06828 13 IRENYRRLKEAFSGP-GFKICYAVKANSNLAILK-LLAE-EGLGADVVSGGELYRALK-AGFPPERIVftGNG-KSDEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 181 RLALvgeKMGhKVYLVIEKMSEIAIVLEEAERLNVVPRLGVR------ArlasqGSGKWQSSGGEKSKFGLAATQVLQLV 254
Cdd:cd06828 88 ELAL---ELG-ILRINVDSLSELERLGEIAPELGKGAPVALRvnpgvdA-----GTHPYISTGGKDSKFGIPLEQALEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 255 EILRAAGHLEsLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvnygLNE 334
Cdd:cd06828 159 RRAKELPGLK-LVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEDEPLD------IEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 496081949 335 YANNIIWAIGDACEenGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTE 386
Cdd:cd06828 232 YAEAIAEALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKT 281
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
124-379 |
2.07e-29 |
|
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: 119.51 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 124 YPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTRSVIVCNG-YKDREYIRLALvgekmGHKVYLV-IEKMS 201
Cdd:pfam00278 28 YAVKANPNPAVLRLLAELG--AGFDVASGGELERALA-AGVDPERIVFAGpGKTDSEIRYAL-----EAGVLCFnVDSED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 202 EIAIVLEEAERLnvVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVEILRAAGhlesLQL--LHFHLGSQMAN 279
Cdd:pfam00278 100 ELEKIAKLAPEL--VARVALRINPDVDAGTHKISTGGLSSKFGIDLEDAPELLALAKELG----LNVvgVHFHIGSQITD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 280 IRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSdcsvnygLNEYANNIIwaigDACEENGLPHPTVIT 359
Cdd:pfam00278 174 LEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPPD-------FEEYAAAIR----EALDEYFPPDLEIIA 242
|
250 260
....*....|....*....|
gi 496081949 360 ESGRAVTAHHTVLVSNIIGV 379
Cdd:pfam00278 243 EPGRYLVANAGVLVTRVIAV 262
|
|
| Arg_decarb_HB |
pfam17810 |
Arginine decarboxylase helical bundle domain; This entry represents a helical bundle domain ... |
391-478 |
1.51e-26 |
|
Arginine decarboxylase helical bundle domain; This entry represents a helical bundle domain that is found between the two enzymatic domains of the arginine decarboxylases.
Pssm-ID: 436060 [Multi-domain] Cd Length: 84 Bit Score: 103.42 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 391 AEDAARPLQSMWETWLEMhetgNRRSLREWLHDSQMDLHDIHIGYSSGTFNLQERAWAEQLYLNMCHEVQKQLDPSNRAH 470
Cdd:pfam17810 1 DEDAPLLLQNLWELLENL----SQRNLLESYHDALHYLDEAHTLFNHGYLSLEQRALAEQLYWAICRRIRALLDPLKRVH 76
|
....*...
gi 496081949 471 RPIIDELQ 478
Cdd:pfam17810 77 REILDELN 84
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
96-383 |
5.79e-26 |
|
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: 111.01 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 96 LQHRLRSINAAFKRAresygyngDYFLVYPIKVNQHRRVIEsLIHSgEPLGLEAGSKAELMAVLAhAGMTRSVIV--CNG 173
Cdd:COG0019 36 LRRNLRALREAFPGS--------GAKVLYAVKANSNLAVLR-LLAE-EGLGADVVSGGELRLALA-AGFPPERIVfsGNG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 174 YKDREyIRLALvgekmGHKVY-LVIEKMSEIAIVLEEAERLNVVPRLGVRAR--LASQGSGKwQSSGGEKSKFGLAATQV 250
Cdd:COG0019 105 KSEEE-LEEAL-----ELGVGhINVDSLSELERLAELAAELGKRAPVGLRVNpgVDAGTHEY-ISTGGKDSKFGIPLEDA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 251 LQLVEILRAAGHLEsLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvny 330
Cdd:COG0019 178 LEAYRRAAALPGLR-LVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYTEGDEPPD----- 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 496081949 331 gLNEYANniiwAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNE 383
Cdd:COG0019 252 -LEELAA----AIKEALEELCGLGPELILEPGRALVGNAGVLLTRVLDVKENG 299
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
148-381 |
2.23e-21 |
|
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: 96.56 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 148 EAGSKAELMAV----LA-HAGMTRSVIVCNG-YKDREYIRLALVgekmgHKVYLVIEKMSEIAIVLEEAERLNVVPRLGV 221
Cdd:cd06841 55 EEGGYAEVVSAmeyeLAlKLGVPGKRIIFNGpYKSKEELEKALE-----EGALINIDSFDELERILEIAKELGRVAKVGI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 222 RARLASqGSGKWqssggekSKFGLAATQVLQLVEILRAAGHLESLQL--LHFHLGSQMANIRDIATGVRESARFYVELHk 299
Cdd:cd06841 130 RLNMNY-GNNVW-------SRFGFDIEENGEALAALKKIQESKNLSLvgLHCHVGSNILNPEAYSAAAKKLIELLDRLF- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 300 lGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEeNGLPHPTVITESGRAVTAHHTVLVSNIIGV 379
Cdd:cd06841 201 -GLELEYLDLGGGFPAKTPLSLAYPQEDTVPDPEDYAEAIASTLKEYYA-NKENKPKLILEPGRALVDDAGYLLGRVVAV 278
|
..
gi 496081949 380 ER 381
Cdd:cd06841 279 KN 280
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
103-385 |
2.59e-20 |
|
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: 93.89 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 103 INAAFKRARESYGyngDYFLV-YPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTRSVIVCNGY-KDREYI 180
Cdd:TIGR01048 35 IRRRFRAYKEAFG---GRSLVcYAVKANSNLAVLRLLAELG--SGFDVVSGGELYRALA-AGFPPEKIVFSGNgKSRAEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 181 RLALvgekmGHKVYLVIEKMSEIaivleeaERLN-VVPRLGVRARLA-------SQGSGKWQSSGGEKSKFGLAATQVLQ 252
Cdd:TIGR01048 109 ERAL-----ELGICINVDSFSEL-------ERLNeIAPELGKKARISlrvnpgvDAKTHPYISTGLKDSKFGIDVEEALE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 253 LVeilRAAGHLESLQL--LHFHLGSQMANIRDIATGVRESARFYVELhKLGVNIQCFDVGGGLGVDYEgtrsQSDCSVNy 330
Cdd:TIGR01048 177 AY---LYALQLPHLELvgIHCHIGSQITDLSPFVEAAEKVVKLAESL-AEGIDLEFLDLGGGLGIPYT----PEEEPPD- 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 496081949 331 gLNEYANNIIWAIGDACEENglPHPTVITESGRAVTAHHTVLVSNIIGVERNEYT 385
Cdd:TIGR01048 248 -LSEYAQAILNALEGYADLG--LDPKLILEPGRSIVANAGVLLTRVGFVKETGSR 299
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
87-379 |
1.93e-17 |
|
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: 84.47 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 87 PALFCFPQILQHRLRSINAAFKRAResygyngdyfLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTR 166
Cdd:cd00622 3 PFLVVDLGDVVRKYRRWKKALPRVR----------PFYAVKCNPDPAVLRTLAALG--AGFDCASKGEIELVLG-LGVSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 167 SVIVC-NGYKDREYIRLALvgeKMGHKVYLV-----IEKMSEIAivleeaerlnvvPRLGVRARLASQGSG-KWQSSGge 239
Cdd:cd00622 70 ERIIFaNPCKSISDIRYAA---ELGVRLFTFdsedeLEKIAKHA------------PGAKLLLRIATDDSGaLCPLSR-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 240 ksKFGLAATQVLQLVEILRAAGhlesLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDY 317
Cdd:cd00622 133 --KFGADPEEARELLRRAKELG----LNVvgVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSY 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496081949 318 EGtrsqsdcsVNYGLNEYANniiwAIGDACEEN-GLPHPTVITESGRAVTAHHTVLVSNIIGV 379
Cdd:cd00622 207 DG--------VVPSFEEIAA----VINRALDEYfPDEGVRIIAEPGRYLVASAFTLAVNVIAK 257
|
|
| Arg_decarbox_C |
pfam17944 |
Arginine decarboxylase C-terminal helical extension; This small three helical domain is found ... |
606-655 |
5.44e-16 |
|
Arginine decarboxylase C-terminal helical extension; This small three helical domain is found at the C-terminus of the arginine decarboxylase enzyme.
Pssm-ID: 436163 [Multi-domain] Cd Length: 50 Bit Score: 72.18 E-value: 5.44e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496081949 606 VADMLQYVQLDPNTLLTQFRDQVKNTGLDDALQQQFLEEFEAGLYGYTYL 655
Cdd:pfam17944 1 VADVLRYVQYDPEELLERYRRQVEAARLSAEERRALLEELEAGLKGYTYL 50
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
122-382 |
8.89e-16 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.
Pssm-ID: 143510 [Multi-domain] Cd Length: 377 Bit Score: 79.63 E-value: 8.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 122 LVYPIKVNQHRRVIESLIHSGEplGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREyIRLALVGekmghKVYLV-IEKM 200
Cdd:cd06843 29 LFYAIKANSDPPILRALAPHVD--GFEVASGGEIAHVRAAVPDAPLIFGGPGKTDSE-LAQALAQ-----GVERIhVESE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 201 SEIAIVLEEAERLNVVPRLGVRARLASQGSgkwQSS----GGEKSKFGLAATQVLQLVEILRAAGHLEsLQLLHFHLgsq 276
Cdd:cd06843 101 LELRRLNAVARRAGRTAPVLLRVNLALPDL---PSStltmGGQPTPFGIDEADLPDALELLRDLPNIR-LRGFHFHL--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 277 MANIRDIATGVR------ESARFYVELHKLGVNIqcFDVGGGLGVDYEGTRSQSDCSvnyGLNEYANNIIWAIGDAceen 350
Cdd:cd06843 174 MSHNLDAAAHLAlvkaylETARQWAAEHGLDLDV--VNVGGGIGVNYADPEEQFDWA---GFCEGLDQLLAEYEPG---- 244
|
250 260 270
....*....|....*....|....*....|..
gi 496081949 351 glphPTVITESGRAVTAHHTVLVSNIIGVERN 382
Cdd:cd06843 245 ----LTLRFECGRYISAYCGYYVTEVLDLKRS 272
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
93-388 |
2.71e-14 |
|
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: 75.12 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 93 PQILQHRLRSINAAFKRARESYGynGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTRSVIVCN 172
Cdd:cd06836 3 PAVGLYDLDGFRALVARLTAAFP--APVLHTFAVKANPLVPVLRLLAEAG--AGAEVASPGELELALA-AGFPPERIVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 173 G-YKDREYIRLALvgekmGHKVYLVIEKMSEIAiVLEE--AERLNVVPRLGVRARLASqGSGKWQ--SSGGEKSKFGLAA 247
Cdd:cd06836 78 SpAKTRAELREAL-----ELGVAINIDNFQELE-RIDAlvAEFKEASSRIGLRVNPQV-GAGKIGalSTATATSKFGVAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 248 TQVlQLVEILRAAGHLESLQLLHFHLGSQMANIRDIATGVRESARFYVELHKL-GVN-IQCFDVGGGLGVDYEGTrsqsd 325
Cdd:cd06836 151 EDG-ARDEIIDAFARRPWLNGLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRvGRRqITRIDIGGGLPVNFESE----- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496081949 326 cSVNYGLNEYANNIIWAIGDACEENglphPTVITESGRAVTAHHTVLVSniigveRNEYTEAT 388
Cdd:cd06836 225 -DITPTFADYAAALKAAVPELFDGR----YQLVTEFGRSLLAKCGTIVS------RVEYTKSS 276
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
124-381 |
3.42e-14 |
|
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: 74.55 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 124 YPIKVNQHRRVIESLihSGEPLGLEAGSKAELMAVLAhAGMTRSVIVCNGY-KDREYIRLALvgekmGHKVY-LVIEKMS 201
Cdd:cd06839 36 YSLKANPNPALVAHL--RQLGDGAEVASAGELALALE-AGVPPEKILFAGPgKSDAELRRAI-----EAGIGtINVESLE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 202 EIAIVLEEAERLNVVPRLGVR--ARLASQGSGkwQSSGGEKSKFGLAATQVLQLVEILRAAGHLEsLQLLHFHLGSQMAN 279
Cdd:cd06839 108 ELERIDALAEEHGVVARVALRinPDFELKGSG--MKMGGGPSQFGIDVEELPAVLARIAALPNLR-FVGLHIYPGTQILD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 280 IRDIATGVRESARFYVEL-HKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvnygLNEYANNIIWAIGDACEEngLPHPTVI 358
Cdd:cd06839 185 ADALIEAFRQTLALALRLaEELGLPLEFLDLGGGFGIPYFPGETPLD------LEALGAALAALLAELGDR--LPGTRVV 256
|
250 260
....*....|....*....|...
gi 496081949 359 TESGRAVTAHHTVLVSNIIGVER 381
Cdd:cd06839 257 LELGRYLVGEAGVYVTRVLDRKV 279
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
75-317 |
5.11e-12 |
|
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: 68.44 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 75 LVKAREAQGQrlPALFCFPQILQHRLRSINAAFKRaresygYNGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAE 154
Cdd:cd06842 1 LVALVEAYGS--PLNVLFPQTFRENIAALRAVLDR------HGVDGRVYFARKANKSLALVRAAAAAG--IGVDVASLAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 155 LMAVLAhAGMTRSVIVCNG-YKDREYIRLALvgekmGHKVYLVIEKMSEIAIVLEEAERLnvvprLGVRARLASQGSGKW 233
Cdd:cd06842 71 LRQALA-AGVRGDRIVATGpAKTDEFLWLAV-----RHGATIAVDSLDELDRLLALARGY-----TTGPARVLLRLSPFP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 234 QSSggeKSKFGLAATQVLQLVEilRAAGHLESLQL--LHFHLGSQMANIRDIAtgVRESARFYVELHKLGVNIQCFDVGG 311
Cdd:cd06842 140 ASL---PSRFGMPAAEVRTALE--RLAQLRERVRLvgFHFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGG 212
|
....*.
gi 496081949 312 GLGVDY 317
Cdd:cd06842 213 GFPVSY 218
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
122-324 |
2.24e-11 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 63.88 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 122 LVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMaVLAHAGMTRSVIVCNG-YKDREYIRLALvgekmGHKVYLVIekm 200
Cdd:cd06808 18 LFAVVKANANPEVARTLAALG--TGFDVASLGEAL-LLRAAGIPPEPILFLGpCKQVSELEDAA-----EQGVIVVT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 201 seiAIVLEEAERLN-VVPRLGVRARLASQgsgkwQSSGGEKSKFGLAATQVLQLVEILRAAGHLEsLQLLHFHLGSQMAN 279
Cdd:cd06808 87 ---VDSLEELEKLEeAALKAGPPARVLLR-----IDTGDENGKFGVRPEELKALLERAKELPHLR-LVGLHTHFGSADED 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496081949 280 IRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQS 324
Cdd:cd06808 158 YSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLG 202
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
109-317 |
5.58e-08 |
|
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: 55.52 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 109 RARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLA---HAGMTRSVIVCNGYKDREYIRLALV 185
Cdd:cd06840 25 RARQVSALKAVDSLFYAIKANPHPDVLRTLEEAG--LGFECVSIGELDLVLKlfpDLDPRRVLFTPNFAARSEYEQALEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 186 GekmghkVYLVIEKMSeiaiVLEEAERLNVVPRLGVRARLAsQGSGKWQ--SSGGEKSKFGLAATQVLQLVEILRAAGhl 263
Cdd:cd06840 103 G------VNVTVDNLH----PLREWPELFRGREVILRIDPG-QGEGHHKhvRTGGPESKFGLDVDELDEARDLAKKAG-- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 264 ESLQLLHFHLGSqmanirdiatGVRES---ARFYVELHKLGVN---IQCFDVGGGLGVDY 317
Cdd:cd06840 170 IIVIGLHAHSGS----------GVEDTdhwARHGDYLASLARHfpaVRILNVGGGLGIPE 219
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
89-382 |
3.22e-07 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 53.26 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 89 LFCFPQILQHRlrsinAAFKRARESYgyngDYFLVYPIKVNQHRRVIESLIHSGEPLGLEAGSKAELmAVLAHAGMTRSV 168
Cdd:PLN02537 22 LYSKPQITRNY-----EAYKEALEGL----RSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRL-ALRAGFDPTRCI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 169 IVCNGyKDREYIRLAlvgEKMGhkVYLVIEKMSEIAIVLEEA----ERLNVVPRLG--VRARLASqgsgkWQSSGGEKSK 242
Cdd:PLN02537 92 FNGNG-KLLEDLVLA---AQEG--VFVNVDSEFDLENIVEAAriagKKVNVLLRINpdVDPQVHP-----YVATGNKNSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 243 FGLAATQVLQLVEILRAagHLESLQLL--HFHLGSQMANI---RDIATGVREsarFYVELHKLGVNIQCFDVGGGLGVDY 317
Cdd:PLN02537 161 FGIRNEKLQWFLDAVKA--HPNELKLVgaHCHLGSTITKVdifRDAAVLMVN---YVDEIRAQGFELSYLNIGGGLGIDY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496081949 318 EGTRSqsdcsvnygLNEYANNIIWAIGDACEENGLphpTVITESGRAVTAHHTVLVSNIIGVERN 382
Cdd:PLN02537 236 YHAGA---------VLPTPRDLIDTVRELVLSRDL---TLIIEPGRSLIANTCCFVNRVTGVKTN 288
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
124-317 |
9.16e-07 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 52.39 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 124 YPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAH--AGMTRSVIVCNGYKDR-EYIRLALVGekmghkVYLVIEKM 200
Cdd:PRK08961 531 YAIKANPHPAILRTLEEEG--FGFECVSIGELRRVFELfpELSPERVLFTPNFAPRaEYEAAFALG------VTVTLDNV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081949 201 SEiaivLEEAERLNVVPRLGVRARLAsQGSG--KWQSSGGEKSKFGLAATQVLQLVEILRAAGhlesLQL--LHFHLGSq 276
Cdd:PRK08961 603 EP----LRNWPELFRGREVWLRIDPG-HGDGhhEKVRTGGKESKFGLSQTRIDEFVDLAKTLG----ITVvgLHAHLGS- 672
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496081949 277 manirDIATGV--RESARFYVELHKLGVNIQCFDVGGGLGVDY 317
Cdd:PRK08961 673 -----GIETGEhwRRMADELASFARRFPDVRTIDLGGGLGIPE 710
|
|
| |
