|
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: 1154.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 22 MQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLR 101
Cdd:PRK05354 1 MQEVAMSDWSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGD-PGASIDLAELVKELRERGLRLPLLLRFPDILQDRVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 102 SINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:PRK05354 80 SLNAAFKKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPynLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 180 IRLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLRE 259
Cdd:PRK05354 160 IRLALIGRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 260 AGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNI 339
Cdd:PRK05354 240 AGLLDCLQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRSQSDSSVNYSLQEYANDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 340 IWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTVPTAPAEDAPRALQSMWETWQEMHEpgtrRSLRE 419
Cdd:PRK05354 320 VYTLKEICEEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYEEPPAPAEDAPPLLQNLWETYQEISE----RNLQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 420 WLHDSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRaHRPIIDELQERMADKMYVNFSLFQSMPDAW 499
Cdd:PRK05354 396 IYHDAQQDLEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNR-HPPELDELQERLADKYYVNFSLFQSLPDAW 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 500 GIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLF 579
Cdd:PRK05354 475 AIDQLFPIMPLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 580 GDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQ-VKKTDLDAELQQQFLEEFEAGLYGYTYLEDE 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: 1098.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 26 AMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLRSINA 105
Cdd:COG1166 1 PMMDWTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD-PGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 106 AFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLA 183
Cdd:COG1166 80 AFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPynFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 184 LIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLREAGRL 263
Cdd:COG1166 160 LLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 264 DSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAI 343
Cdd:COG1166 240 DCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSNSDSSMNYSLQEYANDVVYAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 344 GDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYT-VPTAPAEDAPRALQSMWETWQEMhepgTRRSLREWLH 422
Cdd:COG1166 320 KEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEpPPPAPPEDAHELLRNLWETYESL----TPRNLQECYH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 423 DSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRaHRPIIDELQERMADKMYVNFSLFQSMPDAWGID 502
Cdd:COG1166 396 DALQYKEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEY-HPEELDELNEKLADKYFCNFSLFQSLPDSWAID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 503 QLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDT 582
Cdd:COG1166 475 QLFPIMPIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDT 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130839 583 EAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQ----VKKTDLDAELQQQFLEEFEAGLYGYTYLED 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: 1050.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 30 QEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLRSINAAFKR 109
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTLQRIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 110 ARESYGYNGDYFLVYPIKVNQHRRVIESLIHSG--EPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALIGE 187
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGkgEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 188 KMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLREAGRLDSLQ 267
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 268 LLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDAC 347
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSSSSDCSVNYGLEEYANDIVQALREIC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 348 EENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTVPTAPAEDAPRALQsmweTWQEMHEPGTRRSLREWLHDSQMD 427
Cdd:TIGR01273 321 EEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEYDPDPKIAEDAPPLVR----TLRELYGPIDRRSAIEILHDAQHL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 428 LHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQkQLDPQNRAHRPIIDELQERMADKMYVNFSLFQSMPDAWGIDQLFPV 507
Cdd:TIGR01273 397 KEEAHEGFKLGYLDLEERAWAEQLYLSICHKVH-QLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 508 LPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:TIGR01273 476 MPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRV 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130839 588 FVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQVKKTDLDAELQQQFLEEFEAGLYGYTYLE 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: 647.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 82 QGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVL 159
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRynIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 160 AHAGMTRSVIVCNGYKDREYIRLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGE 239
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 240 KSKFGLAATQVLQLVETLREAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEG 319
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 320 TRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVerneytvptapaedapralq 399
Cdd:cd06830 241 SRSSSDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGV-------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 400 smwetwqemhepgtrrslrewlhdsqmdlhdihigyssgifslqerawaeqlylsmchevqkqldpqnrahrpiidelqE 479
Cdd:cd06830 301 -------------------------------------------------------------------------------K 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 480 RMADKMYVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPM 559
Cdd:cd06830 302 RLADWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYY 381
|
490 500
....*....|....*....|....*...
gi 16130839 560 LGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:cd06830 382 LGFFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
100-367 |
5.48e-78 |
|
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: 248.35 E-value: 5.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 100 LRSINAAFKRARESYGyngDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:pfam02784 1 LGSIERRHRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELG--TGFDCASKGELERVLAAGVPPERIIFANPCKQRSF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 180 IRLALIGEKMghkvYLVIEKMSEIAIVLDEAERlnvvPRLGVRARL-ASQGSGKWqssggeKSKFGLAatqVLQLVETLR 258
Cdd:pfam02784 76 LRYALEVGVG----CVTVDNVDELEKLARLAPE----ARVLLRIKPdDSAATCPL------SSKFGAD---LDEDVEALL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 259 EAGRLDSLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvnygLNEYA 336
Cdd:pfam02784 139 EAAKLLNLQVvgVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD------FEEYA 212
|
250 260 270
....*....|....*....|....*....|.
gi 16130839 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: 1154.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 22 MQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLR 101
Cdd:PRK05354 1 MQEVAMSDWSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGD-PGASIDLAELVKELRERGLRLPLLLRFPDILQDRVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 102 SINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:PRK05354 80 SLNAAFKKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPynLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 180 IRLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLRE 259
Cdd:PRK05354 160 IRLALIGRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 260 AGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNI 339
Cdd:PRK05354 240 AGLLDCLQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRSQSDSSVNYSLQEYANDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 340 IWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTVPTAPAEDAPRALQSMWETWQEMHEpgtrRSLRE 419
Cdd:PRK05354 320 VYTLKEICEEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYEEPPAPAEDAPPLLQNLWETYQEISE----RNLQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 420 WLHDSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRaHRPIIDELQERMADKMYVNFSLFQSMPDAW 499
Cdd:PRK05354 396 IYHDAQQDLEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNR-HPPELDELQERLADKYYVNFSLFQSLPDAW 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 500 GIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLF 579
Cdd:PRK05354 475 AIDQLFPIMPLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 580 GDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQ-VKKTDLDAELQQQFLEEFEAGLYGYTYLEDE 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: 1098.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 26 AMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDvPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLRSINA 105
Cdd:COG1166 1 PMMDWTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD-PGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 106 AFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLA 183
Cdd:COG1166 80 AFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPynFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 184 LIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLREAGRL 263
Cdd:COG1166 160 LLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 264 DSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAI 343
Cdd:COG1166 240 DCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSNSDSSMNYSLQEYANDVVYAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 344 GDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYT-VPTAPAEDAPRALQSMWETWQEMhepgTRRSLREWLH 422
Cdd:COG1166 320 KEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEpPPPAPPEDAHELLRNLWETYESL----TPRNLQECYH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 423 DSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRaHRPIIDELQERMADKMYVNFSLFQSMPDAWGID 502
Cdd:COG1166 396 DALQYKEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEY-HPEELDELNEKLADKYFCNFSLFQSLPDSWAID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 503 QLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDT 582
Cdd:COG1166 475 QLFPIMPIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDT 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130839 583 EAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQ----VKKTDLDAELQQQFLEEFEAGLYGYTYLED 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: 1050.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 30 QEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLRSINAAFKR 109
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTLQRIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 110 ARESYGYNGDYFLVYPIKVNQHRRVIESLIHSG--EPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALIGE 187
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGkgEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 188 KMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLREAGRLDSLQ 267
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 268 LLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDAC 347
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSSSSDCSVNYGLEEYANDIVQALREIC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 348 EENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTVPTAPAEDAPRALQsmweTWQEMHEPGTRRSLREWLHDSQMD 427
Cdd:TIGR01273 321 EEKGVPHPVIITESGRAITAHHAVLITNVLGVERHEYDPDPKIAEDAPPLVR----TLRELYGPIDRRSAIEILHDAQHL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 428 LHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQkQLDPQNRAHRPIIDELQERMADKMYVNFSLFQSMPDAWGIDQLFPV 507
Cdd:TIGR01273 397 KEEAHEGFKLGYLDLEERAWAEQLYLSICHKVH-QLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 508 LPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:TIGR01273 476 MPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRV 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130839 588 FVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQVKKTDLDAELQQQFLEEFEAGLYGYTYLE 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: 647.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 82 QGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAELMAVL 159
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRynIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 160 AHAGMTRSVIVCNGYKDREYIRLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGE 239
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 240 KSKFGLAATQVLQLVETLREAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEG 319
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 320 TRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVerneytvptapaedapralq 399
Cdd:cd06830 241 SRSSSDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGV-------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 400 smwetwqemhepgtrrslrewlhdsqmdlhdihigyssgifslqerawaeqlylsmchevqkqldpqnrahrpiidelqE 479
Cdd:cd06830 301 -------------------------------------------------------------------------------K 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 480 RMADKMYVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPM 559
Cdd:cd06830 302 RLADWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYY 381
|
490 500
....*....|....*....|....*...
gi 16130839 560 LGFFMVGAYQEILGNMHNLFGDTEAVDV 587
Cdd:cd06830 382 LGFFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
89-657 |
1.16e-161 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 475.71 E-value: 1.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 89 LFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEP--LGLEAGSKAEL---MAVLAHaG 163
Cdd:PLN02439 2 IVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPfrFGLEAGSKPELllaMSCLCK-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 164 MTRSVIVCNGYKDREYIRLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKF 243
Cdd:PLN02439 81 SPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 244 GLAATQVLQLVETLREAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRS- 322
Cdd:PLN02439 161 GLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 323 QSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEytvPTAPAEDAPRALQSMW 402
Cdd:PLN02439 241 SSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASKRG---VPAADDDDQYLLLGLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 403 E----TWQEMHEPGTRRSLREWLHDSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQlDPQNRAHrpiidelq 478
Cdd:PLN02439 318 EelraDYENLYAAADRGDYEECLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVGAS-DPVATYH-------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 479 ermadkmyVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGiatTMPMPEYDPEN-- 556
Cdd:PLN02439 389 --------INLSVFTSIPDFWAIGQLFPIVPLHRLDERPTVRGILSDLTCDSDGKIDKFIGGEG---SLPLHELEKNGgg 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 557 PPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVfPDG--SVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQVKKTDLD 634
Cdd:PLN02439 458 PYYLGMFLGGAYQEALGSLHNLFGGPSVVRVSQ-SDGpgGFAVTRAVPGQSCADVLRAMQHEPELMFETLKHRAEEYVHK 536
|
570 580
....*....|....*....|...
gi 16130839 635 AELQQQFLEEFEAGLYGYTYLED 657
Cdd:PLN02439 537 GGLSGAVAANLARSFHNMPYLSA 559
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
100-367 |
5.48e-78 |
|
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: 248.35 E-value: 5.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 100 LRSINAAFKRARESYGyngDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREY 179
Cdd:pfam02784 1 LGSIERRHRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELG--TGFDCASKGELERVLAAGVPPERIIFANPCKQRSF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 180 IRLALIGEKMghkvYLVIEKMSEIAIVLDEAERlnvvPRLGVRARL-ASQGSGKWqssggeKSKFGLAatqVLQLVETLR 258
Cdd:pfam02784 76 LRYALEVGVG----CVTVDNVDELEKLARLAPE----ARVLLRIKPdDSAATCPL------SSKFGAD---LDEDVEALL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 259 EAGRLDSLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvnygLNEYA 336
Cdd:pfam02784 139 EAAKLLNLQVvgVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD------FEEYA 212
|
250 260 270
....*....|....*....|....*....|.
gi 16130839 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 |
9.48e-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: 169.41 E-value: 9.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 87 PALFCFPQILQHRLRSINAAFKraresygynGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLaHAGMTR 166
Cdd:cd06810 2 PFYVYDLDIIRAHYAALKEALP---------SGVKLFYAVKANPNPHVLRTLAEAG--TGFDVASKGELALAL-AAGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 167 SVIVCNGY-KDREYIRLALigeKMGHKVyLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGL 245
Cdd:cd06810 70 ERIIFTGPaKSVSEIEAAL---ASGVDH-IVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLKSKFGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 246 AATQVLQLVETLREAGRldSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGtrsqsd 325
Cdd:cd06810 146 SLSEARAALERAKELDL--RLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 326 csVNYGLNEYANNIIWAIGDACEEngLPHPTVITESGRAVTAHHTVLVSNIIGVERNeytvptapaedapralqsmwetw 405
Cdd:cd06810 218 --QPLDFEEYAALINPLLKKYFPN--DPGVTLILEPGRYIVAQAGVLVTRVVAVKVN----------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 406 qemhepgtrrslrewlhdsqmdlhdihigyssgifslQERAWAeqlylsmchevqkqldpqnrahrpiidelqermadkm 485
Cdd:cd06810 271 -------------------------------------GGRFFA------------------------------------- 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 486 YVNFSLFQSMPDAWGIDQLFPVLPL-EGLDQVPERRAVLLDITCDSdgaidhyidGDGIATTMPMPEydPENPPMLGFFM 564
Cdd:cd06810 277 VVDGGMNHSFRPALAYDAYHPITPLkAPGPDEPLVPATLAGPLCDS---------GDVIGRDRLLPE--LEVGDLLVFED 345
|
490
....*....|....*...
gi 16130839 565 VGAYQEILGNMHNLFGDT 582
Cdd:cd06810 346 MGAYGFSESSNFNSHPRP 363
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
103-382 |
1.02e-29 |
|
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: 121.05 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 103 INAAFKRARESYGYNgDYFLVYPIKVNQHRRVIEsLIHSgEPLGLEAGSKAELMAVLAhAGMTRSVIV--CNGyKDREYI 180
Cdd:cd06828 13 IRENYRRLKEAFSGP-GFKICYAVKANSNLAILK-LLAE-EGLGADVVSGGELYRALK-AGFPPERIVftGNG-KSDEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 181 RLALigeKMGhKVYLVIEKMSEIaivldeaERLN-VVPRLGVRARLA--------SQGSGKwQSSGGEKSKFGLAATQVL 251
Cdd:cd06828 88 ELAL---ELG-ILRINVDSLSEL-------ERLGeIAPELGKGAPVAlrvnpgvdAGTHPY-ISTGGKDSKFGIPLEQAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 252 QLVetlREAGRLDSLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvn 329
Cdd:cd06828 156 EAY---RRAKELPGLKLvgLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEDEPLD---- 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 16130839 330 ygLNEYANNIIWAIGDACEenGLPHPTVITESGRAVTAHHTVLVSNIIGVERN 382
Cdd:cd06828 229 --IEEYAEAIAEALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKET 277
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
124-379 |
1.51e-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: 119.90 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 124 YPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTRSVIVCNG-YKDREYIRLALigekmGHKVYLV-IEKMS 201
Cdd:pfam00278 28 YAVKANPNPAVLRLLAELG--AGFDVASGGELERALA-AGVDPERIVFAGpGKTDSEIRYAL-----EAGVLCFnVDSED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 202 EIAIVLDEAERLnvVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLREAGrldsLQL--LHFHLGSQMAN 279
Cdd:pfam00278 100 ELEKIAKLAPEL--VARVALRINPDVDAGTHKISTGGLSSKFGIDLEDAPELLALAKELG----LNVvgVHFHIGSQITD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 280 IRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSdcsvnygLNEYANNIIwaigDACEENGLPHPTVIT 359
Cdd:pfam00278 174 LEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPPD-------FEEYAAAIR----EALDEYFPPDLEIIA 242
|
250 260
....*....|....*....|
gi 16130839 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 |
1.98e-28 |
|
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: 108.81 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 391 AEDAPRALQSMWETWQEMhepgTRRSLREWLHDSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRAH 470
Cdd:pfam17810 1 DEDAPLLLQNLWELLENL----SQRNLLESYHDALHYLDEAHTLFNHGYLSLEQRALAEQLYWAICRRIRALLDPLKRVH 76
|
....*...
gi 16130839 471 RPIIDELQ 478
Cdd:pfam17810 77 REILDELN 84
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
96-383 |
1.04e-24 |
|
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: 107.16 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 96 LQHRLRSINAAFKRAresygyngDYFLVYPIKVNQHRRVIEsLIHSgEPLGLEAGSKAELMAVLAhAGMTRSVIV--CNG 173
Cdd:COG0019 36 LRRNLRALREAFPGS--------GAKVLYAVKANSNLAVLR-LLAE-EGLGADVVSGGELRLALA-AGFPPERIVfsGNG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 174 YKDREyIRLAL---IGekmghkvYLVIEKMSEIAIVLDEAERLNVVPRLGVRAR--LASQGSGKwQSSGGEKSKFGLAAT 248
Cdd:COG0019 105 KSEEE-LEEALelgVG-------HINVDSLSELERLAELAAELGKRAPVGLRVNpgVDAGTHEY-ISTGGKDSKFGIPLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 249 QvlqLVETLREAGRLDSLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDc 326
Cdd:COG0019 176 D---ALEAYRRAAALPGLRLvgLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYTEGDEPPD- 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130839 327 svnygLNEYANniiwAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNE 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 |
5.25e-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: 95.41 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 148 EAGSKAELMAV----LA-HAGMTRSVIVCNG-YKDREYIRLALIgekmgHKVYLVIEKMSEIAIVLDEAERLNVVPRLGV 221
Cdd:cd06841 55 EEGGYAEVVSAmeyeLAlKLGVPGKRIIFNGpYKSKEELEKALE-----EGALINIDSFDELERILEIAKELGRVAKVGI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 222 RARLASqGSGKWqssggekSKFGLAATQVLQLVETLREAGRLDSLQL--LHFHLGSQMANIRDIATGVRESARFYVELHk 299
Cdd:cd06841 130 RLNMNY-GNNVW-------SRFGFDIEENGEALAALKKIQESKNLSLvgLHCHVGSNILNPEAYSAAAKKLIELLDRLF- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 300 lGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEeNGLPHPTVITESGRAVTAHHTVLVSNIIGV 379
Cdd:cd06841 201 -GLELEYLDLGGGFPAKTPLSLAYPQEDTVPDPEDYAEAIASTLKEYYA-NKENKPKLILEPGRALVDDAGYLLGRVVAV 278
|
..
gi 16130839 380 ER 381
Cdd:cd06841 279 KN 280
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
103-385 |
1.08e-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: 95.05 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 103 INAAFKRARESYGyngDYFLV-YPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTRSVIVCNGY-KDREYI 180
Cdd:TIGR01048 35 IRRRFRAYKEAFG---GRSLVcYAVKANSNLAVLRLLAELG--SGFDVVSGGELYRALA-AGFPPEKIVFSGNgKSRAEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 181 RLALigekmGHKVYLVIEKMSEIaivldeaERLN-VVPRLGVRARLA-------SQGSGKWQSSGGEKSKFGLAATQVLQ 252
Cdd:TIGR01048 109 ERAL-----ELGICINVDSFSEL-------ERLNeIAPELGKKARISlrvnpgvDAKTHPYISTGLKDSKFGIDVEEALE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 253 LVetlREAGRLDSLQL--LHFHLGSQMANIRDIATGVRESARFYVELhKLGVNIQCFDVGGGLGVDYEgtrsQSDCSVNy 330
Cdd:TIGR01048 177 AY---LYALQLPHLELvgIHCHIGSQITDLSPFVEAAEKVVKLAESL-AEGIDLEFLDLGGGLGIPYT----PEEEPPD- 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16130839 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 ... |
87-388 |
2.30e-18 |
|
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: 87.16 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 87 PALFCFPQILQHRLRSINAAFKRAResygyngdyfLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTR 166
Cdd:cd00622 3 PFLVVDLGDVVRKYRRWKKALPRVR----------PFYAVKCNPDPAVLRTLAALG--AGFDCASKGEIELVLG-LGVSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 167 SVIVC-NGYKDREYIRLALigeKMGHKVYLV-----IEKMSEIAivldeaerlnvvPRLGVRARLASQGSG-KWQSSGge 239
Cdd:cd00622 70 ERIIFaNPCKSISDIRYAA---ELGVRLFTFdsedeLEKIAKHA------------PGAKLLLRIATDDSGaLCPLSR-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 240 ksKFGLAATQVLQLVETLREAGrldsLQL--LHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDY 317
Cdd:cd00622 133 --KFGADPEEARELLRRAKELG----LNVvgVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSY 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130839 318 EGtrsqsdcsVNYGLNEYANniiwAIGDACEEN-GLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTVPT 388
Cdd:cd00622 207 DG--------VVPSFEEIAA----VINRALDEYfPDEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRE 266
|
|
| Arg_decarbox_C |
pfam17944 |
Arginine decarboxylase C-terminal helical extension; This small three helical domain is found ... |
606-655 |
4.06e-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: 72.56 E-value: 4.06e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 16130839 606 VADMLQYVQLDPKTLLTQFRDQVKKTDLDAELQQQFLEEFEAGLYGYTYL 655
Cdd:pfam17944 1 VADVLRYVQYDPEELLERYRRQVEAARLSAEERRALLEELEAGLKGYTYL 50
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
124-381 |
1.65e-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: 75.71 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 124 YPIKVNQHRRVIESLihSGEPLGLEAGSKAELMAVLAhAGMTRSVIVCNGY-KDREYIRLAL---IGEkmghkvyLVIEK 199
Cdd:cd06839 36 YSLKANPNPALVAHL--RQLGDGAEVASAGELALALE-AGVPPEKILFAGPgKSDAELRRAIeagIGT-------INVES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 200 MSEIAIVLDEAERLNVVPRLGVR--ARLASQGSGkwQSSGGEKSKFGLaatQVLQLVETLREAGRLDSLQL--LHFHLGS 275
Cdd:cd06839 106 LEELERIDALAEEHGVVARVALRinPDFELKGSG--MKMGGGPSQFGI---DVEELPAVLARIAALPNLRFvgLHIYPGT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 276 QMANIRDIATGVRESARFYVEL-HKLGVNIQCFDVGGGLGVDYEGTRSQSDcsvnygLNEYANNIIWAIGDACEEngLPH 354
Cdd:cd06839 181 QILDADALIEAFRQTLALALRLaEELGLPLEFLDLGGGFGIPYFPGETPLD------LEALGAALAALLAELGDR--LPG 252
|
250 260
....*....|....*....|....*..
gi 16130839 355 PTVITESGRAVTAHHTVLVSNIIGVER 381
Cdd:cd06839 253 TRVVLELGRYLVGEAGVYVTRVLDRKV 279
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
122-382 |
2.09e-14 |
|
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: 75.40 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 122 LVYPIKVNQHRRVIESLIHSGEplGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREyIRLALigekmGHKVYLV-IEKM 200
Cdd:cd06843 29 LFYAIKANSDPPILRALAPHVD--GFEVASGGEIAHVRAAVPDAPLIFGGPGKTDSE-LAQAL-----AQGVERIhVESE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 201 SEIAIVLDEAERLNVVPRLGVRARLASQGSgkwQSS----GGEKSKFGLAATQVLQLVETLREAGRLDsLQLLHFHLgsq 276
Cdd:cd06843 101 LELRRLNAVARRAGRTAPVLLRVNLALPDL---PSStltmGGQPTPFGIDEADLPDALELLRDLPNIR-LRGFHFHL--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 277 MANIRDIATGVR------ESARFYVELHKLGVNIqcFDVGGGLGVDYEGTRSQSDCSvnyGLNEYANNIIWAIGDAceen 350
Cdd:cd06843 174 MSHNLDAAAHLAlvkaylETARQWAAEHGLDLDV--VNVGGGIGVNYADPEEQFDWA---GFCEGLDQLLAEYEPG---- 244
|
250 260 270
....*....|....*....|....*....|..
gi 16130839 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 ... |
93-385 |
7.93e-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: 73.58 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 93 PQILQHRLRSINAAFKRARESYGynGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAhAGMTRSVIVCN 172
Cdd:cd06836 3 PAVGLYDLDGFRALVARLTAAFP--APVLHTFAVKANPLVPVLRLLAEAG--AGAEVASPGELELALA-AGFPPERIVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 173 G-YKDREYIRLALigekmGHKVYLVIEKMSEIAiVLDE--AERLNVVPRLGVRARLASqGSGKWQ--SSGGEKSKFGLAA 247
Cdd:cd06836 78 SpAKTRAELREAL-----ELGVAINIDNFQELE-RIDAlvAEFKEASSRIGLRVNPQV-GAGKIGalSTATATSKFGVAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 248 TQvlQLVETLREA-GRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKL-GVN-IQCFDVGGGLGVDYEGTrsqs 324
Cdd:cd06836 151 ED--GARDEIIDAfARRPWLNGLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRvGRRqITRIDIGGGLPVNFESE---- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130839 325 dcSVNYGLNEYANNIIWAIGDACEENglphPTVITESGRAVTAHHTVLVSniigveRNEYT 385
Cdd:cd06836 225 --DITPTFADYAAALKAAVPELFDGR----YQLVTEFGRSLLAKCGTIVS------RVEYT 273
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
72-317 |
3.96e-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: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 72 LAQLVktrEAQGQrlPALFCFPQILQHRLRSINAAFKRaresygYNGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGS 151
Cdd:cd06842 1 LVALV---EAYGS--PLNVLFPQTFRENIAALRAVLDR------HGVDGRVYFARKANKSLALVRAAAAAG--IGVDVAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 152 KAELMAVLAhAGMTRSVIVCNG-YKDREYIRLALigekmGHKVYLVIEKMSEIAIVLDEAERLnvvprLGVRARLASQGS 230
Cdd:cd06842 68 LAELRQALA-AGVRGDRIVATGpAKTDEFLWLAV-----RHGATIAVDSLDELDRLLALARGY-----TTGPARVLLRLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 231 GKWQSSggeKSKFGLAATQVLQLVETL-REAGRLDsLQLLHFHLGSQMANIRDIAtgVRESARFYVELHKLGVNIQCFDV 309
Cdd:cd06842 137 PFPASL---PSRFGMPAAEVRTALERLaQLRERVR-LVGFHFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDI 210
|
....*...
gi 16130839 310 GGGLGVDY 317
Cdd:cd06842 211 GGGFPVSY 218
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
122-324 |
9.77e-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: 61.95 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 122 LVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMaVLAHAGMTRSVIVCNG-YKDREYIRLALigekmGHKVYLVIekm 200
Cdd:cd06808 18 LFAVVKANANPEVARTLAALG--TGFDVASLGEAL-LLRAAGIPPEPILFLGpCKQVSELEDAA-----EQGVIVVT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 201 seiAIVLDEAERLN-VVPRLGVRARLASQgsgkwQSSGGEKSKFGLAATQVLQLVETLREagrLDSLQL--LHFHLGSQM 277
Cdd:cd06808 87 ---VDSLEELEKLEeAALKAGPPARVLLR-----IDTGDENGKFGVRPEELKALLERAKE---LPHLRLvgLHTHFGSAD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130839 278 ANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQS 324
Cdd:cd06808 156 EDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLG 202
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
124-317 |
2.65e-07 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 53.93 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 124 YPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLAH--AGMTRSVIVCNGYKDR-EYIRLALIGekmghkvylviekm 200
Cdd:PRK08961 531 YAIKANPHPAILRTLEEEG--FGFECVSIGELRRVFELfpELSPERVLFTPNFAPRaEYEAAFALG-------------- 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 201 seIAIVLDEAERLNVVPRL------GVRARLAsQGSG--KWQSSGGEKSKFGLAATQVLQLVETLREAGrldsLQL--LH 270
Cdd:PRK08961 595 --VTVTLDNVEPLRNWPELfrgrevWLRIDPG-HGDGhhEKVRTGGKESKFGLSQTRIDEFVDLAKTLG----ITVvgLH 667
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130839 271 FHLGSqmanirDIATGV--RESARFYVELHKLGVNIQCFDVGGGLGVDY 317
Cdd:PRK08961 668 AHLGS------GIETGEhwRRMADELASFARRFPDVRTIDLGGGLGIPE 710
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
109-317 |
4.47e-07 |
|
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: 52.44 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 109 RARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGepLGLEAGSKAELMAVLA---HAGMTRSVIVCNGYKDREYIRLALI 185
Cdd:cd06840 25 RARQVSALKAVDSLFYAIKANPHPDVLRTLEEAG--LGFECVSIGELDLVLKlfpDLDPRRVLFTPNFAARSEYEQALEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 186 GekmghkVYLVIEKMSeiaiVLDEAERLNVVPRLGVRARLAsQGSGKWQ--SSGGEKSKFGLAATQVLQLVETLREAGRl 263
Cdd:cd06840 103 G------VNVTVDNLH----PLREWPELFRGREVILRIDPG-QGEGHHKhvRTGGPESKFGLDVDELDEARDLAKKAGI- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 264 dSLQLLHFHLGSqmanirdiatGVRES---ARFYVELHKLGVN---IQCFDVGGGLGVDY 317
Cdd:cd06840 171 -IVIGLHAHSGS----------GVEDTdhwARHGDYLASLARHfpaVRILNVGGGLGIPE 219
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
235-382 |
1.62e-06 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 50.95 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130839 235 SSGGEKSKFGLAATQVLQLVETLREAGRLDSLQLLHFHLGSQMANI---RDIATGVREsarFYVELHKLGVNIQCFDVGG 311
Cdd:PLN02537 153 ATGNKNSKFGIRNEKLQWFLDAVKAHPNELKLVGAHCHLGSTITKVdifRDAAVLMVN---YVDEIRAQGFELSYLNIGG 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130839 312 GLGVDYEGTRSqsdcsvnygLNEYANNIIWAIGDACEENGLphpTVITESGRAVTAHHTVLVSNIIGVERN 382
Cdd:PLN02537 230 GLGIDYYHAGA---------VLPTPRDLIDTVRELVLSRDL---TLIIEPGRSLIANTCCFVNRVTGVKTN 288
|
|
| |
