|
Name |
Accession |
Description |
Interval |
E-value |
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
19-651 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 1080.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 19 WSIERAAQYYNVSGWGAGFFSINEKGHVAVHPMGQPGPTIDLMDVVEDIRERNIGFPCVVRFQDVLRARVKQINEAFGKA 98
Cdd:COG1166 5 WTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGDPGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNEAFAKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 99 VAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLALLGRK 178
Cdd:COG1166 85 IAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLALLGRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 179 LGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAKL 258
Cdd:COG1166 165 LGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGMLDCLQL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 259 LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTNdFTSSVNYSMDEYVGDVVYNVQRVC 338
Cdd:COG1166 245 LHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSN-SDSSMNYSLQEYANDVVYAIKEVC 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 339 MNEGVPEPHIVSESGRAVTAHHSCIIIPVFGHIEIGSVEEIAkasEPEPNEAKVVREMREIVSSLTPRNRAETYHDAAAK 418
Cdd:COG1166 324 DEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPPP---APPEDAHELLRNLWETYESLTPRNLQECYHDALQY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 419 KEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNRGKKRPPRETKDLGDKIADQYMANFSLFQSAPDHWAFDQLFPIV 498
Cdd:COG1166 401 KEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEYHPEELDELNEKLADKYFCNFSLFQSLPDSWAIDQLFPIM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 499 PLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYYLGMFMTGAYQDIMGDMHNLFGRVNEIHVF 578
Cdd:COG1166 481 PIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDTNAVHVR 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501518076 579 VDDEDpeDFYIEEVIPGDTIEKVLSRVQYEPADLFRRVKAALDQKVKEGAIRPKEGVSLQDFYEAVMKGYTYL 651
Cdd:COG1166 561 LDEDG--GYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQAEQAVRAGRLTPEERQRLLEEYEAGLRGYTYL 631
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
19-651 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 1053.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 19 WSIERAAQYYNVSGWGAGFFSINEKGHVAVHPMGQPGPTIDLMDVVEDIRERNIGFPCVVRFQDVLRARVKQINEAFGKA 98
Cdd:PRK05354 9 WSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGDPGASIDLAELVKELRERGLRLPLLLRFPDILQDRVRSLNAAFKKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 99 VAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLALLGRK 178
Cdd:PRK05354 89 IEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPYNLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREYIRLALIGRK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 179 LGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAKL 258
Cdd:PRK05354 169 LGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLREAGLLDCLQL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 259 LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTNdFTSSVNYSMDEYVGDVVYNVQRVC 338
Cdd:PRK05354 249 LHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRSQ-SDSSVNYSLQEYANDVVYTLKEIC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 339 MNEGVPEPHIVSESGRAVTAHHSCIIIPVFGHIEIGSVEEIakasEPEPNEAKVVREMREIVSSLTPRNRAETYHDAAAK 418
Cdd:PRK05354 328 EEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYEEPP----APAEDAPPLLQNLWETYQEISERNLQEIYHDAQQD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 419 KEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNRGKKRPPRETKDLGDKIADQYMANFSLFQSAPDHWAFDQLFPIV 498
Cdd:PRK05354 404 LEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNRHPPELDELQERLADKYYVNFSLFQSLPDAWAIDQLFPIM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 499 PLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYYLGMFMTGAYQDIMGDMHNLFGRVNEIHVF 578
Cdd:PRK05354 484 PLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLFGDTNAVHVR 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501518076 579 VDDEdpEDFYIEEVIPGDTIEKVLSRVQYEPADLFRRVKaalDQKVKEGAIRPKEGVSLQDFYEAVMKGYTYL 651
Cdd:PRK05354 564 VDED--GGYEIEHVIEGDTVADVLEYVQYDPKELLERLR---EKAVKEGKLSPEERQQLLEELEAGLRGYTYL 631
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
19-652 |
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: 736.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 19 WSIERAAQYYNVSGWGAGFFSINEKGHVAVHPMGQPGPT-IDLMDVVEDIRERNIGFPCVVRFQDVLRARVKQINEAFGK 97
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTLQrIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 98 AVAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLALLGR 177
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGKGEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 178 KLGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAK 257
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 258 LLHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTNDFtSSVNYSMDEYVGDVVYNVQRV 337
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSSSSD-CSVNYGLEEYANDIVQALREI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 338 CMNEGVPEPHIVSESGRAVTAHHSCIIIPVfghIEIGSVEEiAKASEPEPNEAKVVREMREIVSSLTPRNRAETYHDAAA 417
Cdd:TIGR01273 320 CEEKGVPHPVIITESGRAITAHHAVLITNV---LGVERHEY-DPDPKIAEDAPPLVRTLRELYGPIDRRSAIEILHDAQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 418 KKEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNRGKKRPPRETKDLGDKIADQYMANFSLFQSAPDHWAFDQLFPI 497
Cdd:TIGR01273 396 LKEEAHEGFKLGYLDLEERAWAEQLYLSICHKVHQLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 498 VPLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYYLGMFMTGAYQDIMGDMHNLFGRVNEIHV 577
Cdd:TIGR01273 476 MPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRV 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501518076 578 FVDDEDpeDFYIEEVIPGDTIEKVLSRVQYEPADLFRRVKaaldQKVKEGAIRPKEGVSLQDFYEAVMKGYTYLG 652
Cdd:TIGR01273 556 VFDGDG--GYEVELIREGDTTEDMLRYVQYDPKELLTLYR----DKVANNKLDAEEKKQFLEELEAGLSGYPYLS 624
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
70-577 |
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: 619.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 70 RNIGFPCVVRFQDVLRARVKQINEAFGKAVAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVL 149
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 150 GMNADPDALTICNGYKDEEYLRLALLGRKLGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGD 229
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 230 FAKFGLTVPELIQAVRILKEAGKEHCAKLLHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVG 309
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 310 TRTNdFTSSVNYSMDEYVGDVVYNVQRVCMNEGVPEPHIVSESGRAVTAHHSCIIIPVFGhieigsveeiakasepepne 389
Cdd:cd06830 241 SRSS-SDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLG-------------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 390 akvvremreivssltprnraetyhdaaakkeealqmfklgilgleeravVESLfwklvrgiadmnrgkkrppretkdlgd 469
Cdd:cd06830 300 -------------------------------------------------VKRL--------------------------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 470 kiADQYMANFSLFQSAPDHWAFDQLFPIVPLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYY 549
Cdd:cd06830 304 --ADWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYY 381
|
490 500
....*....|....*....|....*...
gi 501518076 550 LGMFMTGAYQDIMGDMHNLFGRVNEIHV 577
Cdd:cd06830 382 LGFFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
90-358 |
5.93e-39 |
|
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: 143.58 E-value: 5.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 90 QINEAFGKAVAEMGygaSYFGVYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNADPDALTICNGYKDEEY 169
Cdd:pfam02784 3 SIERRHRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELGT----GFDCASKGELERVLAAGVPPERIIFANPCKQRSF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 170 LRLALLGRKlgrkVIVVIEKLSELPQLLRLGEEmgvdPMIGLRSKLT-TRGTGKWEgssgdfAKFGLTvpeLIQAVRILK 248
Cdd:pfam02784 76 LRYALEVGV----GCVTVDNVDELEKLARLAPE----ARVLLRIKPDdSAATCPLS------SKFGAD---LDEDVEALL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 249 EAGKEHCAKL--LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTR----TNDFTSSVNYS 322
Cdd:pfam02784 139 EAAKLLNLQVvgVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEepldFEEYANVINEA 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 501518076 323 MDEYVgdvvynvqrvcmnEGVPEPHIVSESGRAVTA 358
Cdd:pfam02784 219 LEEYF-------------PGDPGVTIIAEPGRYFVA 241
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
19-651 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 1080.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 19 WSIERAAQYYNVSGWGAGFFSINEKGHVAVHPMGQPGPTIDLMDVVEDIRERNIGFPCVVRFQDVLRARVKQINEAFGKA 98
Cdd:COG1166 5 WTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGDPGPSIDLYELVEELRERGLSLPVLLRFPDILRDRVERLNEAFAKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 99 VAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLALLGRK 178
Cdd:COG1166 85 IAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALLDDPGSLIICNGYKDREYIRLALLGRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 179 LGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAKL 258
Cdd:COG1166 165 LGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERLKEAGMLDCLQL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 259 LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTNdFTSSVNYSMDEYVGDVVYNVQRVC 338
Cdd:COG1166 245 LHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSN-SDSSMNYSLQEYANDVVYAIKEVC 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 339 MNEGVPEPHIVSESGRAVTAHHSCIIIPVFGHIEIGSVEEIAkasEPEPNEAKVVREMREIVSSLTPRNRAETYHDAAAK 418
Cdd:COG1166 324 DEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPPP---APPEDAHELLRNLWETYESLTPRNLQECYHDALQY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 419 KEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNRGKKRPPRETKDLGDKIADQYMANFSLFQSAPDHWAFDQLFPIV 498
Cdd:COG1166 401 KEEARSLFNLGYLSLEERALAEQLYWAICRKIRELLDPLEYHPEELDELNEKLADKYFCNFSLFQSLPDSWAIDQLFPIM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 499 PLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYYLGMFMTGAYQDIMGDMHNLFGRVNEIHVF 578
Cdd:COG1166 481 PIHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGVKSTLPLHPLKPGEPYYLGVFLVGAYQEILGDLHNLFGDTNAVHVR 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501518076 579 VDDEDpeDFYIEEVIPGDTIEKVLSRVQYEPADLFRRVKAALDQKVKEGAIRPKEGVSLQDFYEAVMKGYTYL 651
Cdd:COG1166 561 LDEDG--GYEIEHVVEGDTVAEVLSYVQYDPEDLLERYRRQAEQAVRAGRLTPEERQRLLEEYEAGLRGYTYL 631
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
19-651 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 1053.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 19 WSIERAAQYYNVSGWGAGFFSINEKGHVAVHPMGQPGPTIDLMDVVEDIRERNIGFPCVVRFQDVLRARVKQINEAFGKA 98
Cdd:PRK05354 9 WSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGDPGASIDLAELVKELRERGLRLPLLLRFPDILQDRVRSLNAAFKKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 99 VAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLALLGRK 178
Cdd:PRK05354 89 IEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPYNLGLEAGSKPELMAVLALAGDPGALIVCNGYKDREYIRLALIGRK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 179 LGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAKL 258
Cdd:PRK05354 169 LGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERLREAGLLDCLQL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 259 LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTNdFTSSVNYSMDEYVGDVVYNVQRVC 338
Cdd:PRK05354 249 LHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRSQ-SDSSVNYSLQEYANDVVYTLKEIC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 339 MNEGVPEPHIVSESGRAVTAHHSCIIIPVFGHIEIGSVEEIakasEPEPNEAKVVREMREIVSSLTPRNRAETYHDAAAK 418
Cdd:PRK05354 328 EEHGVPHPTIISESGRALTAHHAVLVFNVLGVESQEYEEPP----APAEDAPPLLQNLWETYQEISERNLQEIYHDAQQD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 419 KEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNRGKKRPPRETKDLGDKIADQYMANFSLFQSAPDHWAFDQLFPIV 498
Cdd:PRK05354 404 LEEALTLFALGYLSLQERAWAEQLYWAICRKIQKLLDPKNRHPPELDELQERLADKYYVNFSLFQSLPDAWAIDQLFPIM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 499 PLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYYLGMFMTGAYQDIMGDMHNLFGRVNEIHVF 578
Cdd:PRK05354 484 PLHRLDEEPTRRAVLADITCDSDGKIDQFIDGQGIKTTLPLHELDPGEPYYLGFFLVGAYQEILGDMHNLFGDTNAVHVR 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501518076 579 VDDEdpEDFYIEEVIPGDTIEKVLSRVQYEPADLFRRVKaalDQKVKEGAIRPKEGVSLQDFYEAVMKGYTYL 651
Cdd:PRK05354 564 VDED--GGYEIEHVIEGDTVADVLEYVQYDPKELLERLR---EKAVKEGKLSPEERQQLLEELEAGLRGYTYL 631
|
|
| speA |
TIGR01273 |
arginine decarboxylase, biosynthetic; Two alternative pathways can convert arginine to ... |
19-652 |
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: 736.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 19 WSIERAAQYYNVSGWGAGFFSINEKGHVAVHPMGQPGPT-IDLMDVVEDIRERNIGFPCVVRFQDVLRARVKQINEAFGK 97
Cdd:TIGR01273 1 WSASESRKTYNIAGWGAGYFAVNKLGNVSVRPGGDDTLQrIDLLELVKQVEARGLQLPLLVRFPDILQHRIRSLNAAFKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 98 AVAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLALLGR 177
Cdd:TIGR01273 81 AIEEYQYAGHYQGVYPIKVNQHRRVVEDIVASGKGEPYGLEAGSKPELMAAMAYATKPGAPIVCNGYKDREYIELALIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 178 KLGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAK 257
Cdd:TIGR01273 161 KLGHNVFIVIEKLSELDLVIDEAKKLGVKPKLGLRARLASKGSGKWASSGGEKSKFGLSATQVLEVVRLLEQNGLLDSLQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 258 LLHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTNDFtSSVNYSMDEYVGDVVYNVQRV 337
Cdd:TIGR01273 241 LLHFHIGSQISNIDDIKKGVREAARFYCELRKLGVKITYVDVGGGLGVDYDGTSSSSD-CSVNYGLEEYANDIVQALREI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 338 CMNEGVPEPHIVSESGRAVTAHHSCIIIPVfghIEIGSVEEiAKASEPEPNEAKVVREMREIVSSLTPRNRAETYHDAAA 417
Cdd:TIGR01273 320 CEEKGVPHPVIITESGRAITAHHAVLITNV---LGVERHEY-DPDPKIAEDAPPLVRTLRELYGPIDRRSAIEILHDAQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 418 KKEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNRGKKRPPRETKDLGDKIADQYMANFSLFQSAPDHWAFDQLFPI 497
Cdd:TIGR01273 396 LKEEAHEGFKLGYLDLEERAWAEQLYLSICHKVHQLSAKNKDHRPILDELQERLADKYFVNFSVFQSLPDAWGIDQLFPI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 498 VPLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYYLGMFMTGAYQDIMGDMHNLFGRVNEIHV 577
Cdd:TIGR01273 476 MPLERLDEKPTRRAVLLDITCDSDGKIDQFIGGQGITSTLPLHELDPDEGYFLGFFLVGAYQEILGDMHNLFGDTSAVRV 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501518076 578 FVDDEDpeDFYIEEVIPGDTIEKVLSRVQYEPADLFRRVKaaldQKVKEGAIRPKEGVSLQDFYEAVMKGYTYLG 652
Cdd:TIGR01273 556 VFDGDG--GYEVELIREGDTTEDMLRYVQYDPKELLTLYR----DKVANNKLDAEEKKQFLEELEAGLSGYPYLS 624
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
70-577 |
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: 619.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 70 RNIGFPCVVRFQDVLRARVKQINEAFGKAVAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVL 149
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 150 GMNADPDALTICNGYKDEEYLRLALLGRKLGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGD 229
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 230 FAKFGLTVPELIQAVRILKEAGKEHCAKLLHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVG 309
Cdd:cd06830 161 RSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 310 TRTNdFTSSVNYSMDEYVGDVVYNVQRVCMNEGVPEPHIVSESGRAVTAHHSCIIIPVFGhieigsveeiakasepepne 389
Cdd:cd06830 241 SRSS-SDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLG-------------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 390 akvvremreivssltprnraetyhdaaakkeealqmfklgilgleeravVESLfwklvrgiadmnrgkkrppretkdlgd 469
Cdd:cd06830 300 -------------------------------------------------VKRL--------------------------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 470 kiADQYMANFSLFQSAPDHWAFDQLFPIVPLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGVDETLSLHALRPGEPYY 549
Cdd:cd06830 304 --ADWYFCNFSLFQSLPDSWAIDQLFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILPTLPLHPLRKDEPYY 381
|
490 500
....*....|....*....|....*...
gi 501518076 550 LGMFMTGAYQDIMGDMHNLFGRVNEIHV 577
Cdd:cd06830 382 LGFFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
77-651 |
0e+00 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 555.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 77 VVRFQDVLRARVKQINEAFGKAVAEMGYGASYFGVYPIKVNQMREVVDEIVDAGAPYHYGLEAGSKGELLVVLG--MNAD 154
Cdd:PLN02439 2 IVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPFRFGLEAGSKPELLLAMSclCKGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 155 PDALTICNGYKDEEYLRLALLGRKLGRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKFG 234
Cdd:PLN02439 82 PDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 235 LTVPELIQAVRILKEAGKEHCAKLLHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTND 314
Cdd:PLN02439 162 LTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 315 FTSSVNYSMDEYVGDVVYNVQRVCMNEGVPEPHIVSESGRAVTAHHSCIIIPVFGHIEIGsveeiakASEPEPNEAKVVR 394
Cdd:PLN02439 242 SDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASKRG-------VPAADDDDQYLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 395 EMREIVsSLTPRNRAET---------YHDAAAKKEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNrgkkrPPRetk 465
Cdd:PLN02439 315 GLTEEL-RADYENLYAAadrgdyeecLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVGASD-----PVA--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 466 dlgdkiadQYMANFSLFQSAPDHWAFDQLFPIVPLHRMGEAPTRDTTIVDITCDSDGKIDRFIEGEGvdeTLSLHALR-- 543
Cdd:PLN02439 386 --------TYHINLSVFTSIPDFWAIGQLFPIVPLHRLDERPTVRGILSDLTCDSDGKIDKFIGGEG---SLPLHELEkn 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 544 PGEPYYLGMFMTGAYQDIMGDMHNLFGRVNEIHVFVDDeDPEDFYIEEVIPGDTIEKVLSRVQYEPADLFRRVKAALDQK 623
Cdd:PLN02439 455 GGGPYYLGMFLGGAYQEALGSLHNLFGGPSVVRVSQSD-GPGGFAVTRAVPGQSCADVLRAMQHEPELMFETLKHRAEEY 533
|
570 580
....*....|....*....|....*...
gi 501518076 624 VKEGAIRPKEGVSLQDFYEAvmkgYTYL 651
Cdd:PLN02439 534 VHKGGLSGAVAANLARSFHN----MPYL 557
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
75-577 |
1.02e-48 |
|
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: 174.80 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 75 PCVVRFQDVLRARVKQINEAFGKAVAemgygasyfGVYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNAD 154
Cdd:cd06810 2 PFYVYDLDIIRAHYAALKEALPSGVK---------LFYAVKANPNPHVLRTLAEAGT----GFDVASKGELALALAAGVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 155 PDaLTICNGY-KDEEYLRLALlgrKLGRKVIVViEKLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTGKWEGSSGDFAKF 233
Cdd:cd06810 69 PE-RIIFTGPaKSVSEIEAAL---ASGVDHIVV-DSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLKSKF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 234 GLTVPELIQAVRILKEAGKEhcAKLLHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGtrtn 313
Cdd:cd06810 144 GLSLSEARAALERAKELDLR--LVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 314 dftssVNYSMDEYVGDVVYNVQRVCMNegVPEPHIVSESGRAVTAHHSCIIIPVfghieigsveeiakasepepneakvv 393
Cdd:cd06810 218 -----QPLDFEEYAALINPLLKKYFPN--DPGVTLILEPGRYIVAQAGVLVTRV-------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 394 remreivssltprnraetyhdaaakkeealqmfklgilgleeravveslfwklvrgiadmnrgkkrppRETKDLGDKiaD 473
Cdd:cd06810 265 --------------------------------------------------------------------VAVKVNGGR--F 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 474 QYMANFSLFQSAPDHWAFDQLFPIVPLHRMGE-APTRDTTIVDITCDSDgkiDRFIEGEGVDEtlslhaLRPGepYYLGM 552
Cdd:cd06810 275 FAVVDGGMNHSFRPALAYDAYHPITPLKAPGPdEPLVPATLAGPLCDSG---DVIGRDRLLPE------LEVG--DLLVF 343
|
490 500
....*....|....*....|....*
gi 501518076 553 FMTGAYQDIMGDMHNLFGRVNEIHV 577
Cdd:cd06810 344 EDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
90-358 |
5.93e-39 |
|
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: 143.58 E-value: 5.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 90 QINEAFGKAVAEMGygaSYFGVYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNADPDALTICNGYKDEEY 169
Cdd:pfam02784 3 SIERRHRRWKKALP---RIKPFYAVKCNSDPAVLRLLAELGT----GFDCASKGELERVLAAGVPPERIIFANPCKQRSF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 170 LRLALLGRKlgrkVIVVIEKLSELPQLLRLGEEmgvdPMIGLRSKLT-TRGTGKWEgssgdfAKFGLTvpeLIQAVRILK 248
Cdd:pfam02784 76 LRYALEVGV----GCVTVDNVDELEKLARLAPE----ARVLLRIKPDdSAATCPLS------SKFGAD---LDEDVEALL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 249 EAGKEHCAKL--LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTR----TNDFTSSVNYS 322
Cdd:pfam02784 139 EAAKLLNLQVvgVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEepldFEEYANVINEA 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 501518076 323 MDEYVgdvvynvqrvcmnEGVPEPHIVSESGRAVTA 358
Cdd:pfam02784 219 LEEYF-------------PGDPGVTIIAEPGRYFVA 241
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
64-358 |
6.78e-29 |
|
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439790 [Multi-domain] Cd Length: 417 Bit Score: 119.48 E-value: 6.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 64 VEDIRERnIGFPCVVRFQDVLRARVKQINEAFGKAVAEMgygasyfgVYPIKVNQMREVVDEIVDAGApyhyGLEAGSKG 143
Cdd:COG0019 17 LAELAEE-YGTPLYVYDEAALRRNLRALREAFPGSGAKV--------LYAVKANSNLAVLRLLAEEGL----GADVVSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 144 ELLVVLGMNADPDALTI-CNGYKDEEyLRLALlgrKLGRKVIVViEKLSELPQLLRLGEEMGVDPMIGLR---------- 212
Cdd:COG0019 84 ELRLALAAGFPPERIVFsGNGKSEEE-LEEAL---ELGVGHINV-DSLSELERLAELAAELGKRAPVGLRvnpgvdagth 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 213 SKLTTrgtgkwegsSGDFAKFGLTVPELIQAVRILKEAGKEHCaKLLHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGL 292
Cdd:COG0019 159 EYIST---------GGKDSKFGIPLEDALEAYRRAAALPGLRL-VGLHFHIGSQILDLEPFEEALERLLELAEELRELGI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501518076 293 PIEYFDVGGGLGVDYVGTRTndftssvNYSMDEYVGDVVYNVQRVCmnegVPEPHIVSESGRAVTA 358
Cdd:COG0019 229 DLEWLDLGGGLGIPYTEGDE-------PPDLEELAAAIKEALEELC----GLGPELILEPGRALVG 283
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
82-358 |
2.59e-26 |
|
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: 110.27 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 82 DVLRARVKQINEAFGKavaemgyGASYFgvYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNADPDALTIC 161
Cdd:pfam00278 7 ATLRRNYRRWKAALPP-------RVKIF--YAVKANPNPAVLRLLAELGA----GFDVASGGELERALAAGVDPERIVFA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 162 NGYKDEEYLRLALlgrKLGRKVIVViEKLSELPQLLRLGEEMGVDpmIGLR------SKLTTRGTGkwegssGDFAKFGL 235
Cdd:pfam00278 74 GPGKTDSEIRYAL---EAGVLCFNV-DSEDELEKIAKLAPELVAR--VALRinpdvdAGTHKISTG------GLSSKFGI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 236 TVPeliQAVRILKEAgKEHCAKL--LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTN 313
Cdd:pfam00278 142 DLE---DAPELLALA-KELGLNVvgVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPP 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 501518076 314 DFtssvnysmDEYVGdvvyNVQRVCMNEGVPEPHIVSESGRAVTA 358
Cdd:pfam00278 218 DF--------EEYAA----AIREALDEYFPPDLEIIAEPGRYLVA 250
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
75-364 |
4.16e-23 |
|
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: 101.41 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 75 PCVVRFQDVLRARVKQINEAFGKAVAEMgygasyfgVYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNAD 154
Cdd:cd06828 4 PLYVYDEATIRENYRRLKEAFSGPGFKI--------CYAVKANSNLAILKLLAEEGL----GADVVSGGELYRALKAGFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 155 PDalTI---CNGYKDEEyLRLALlgrKLGrKVIVVIEKLSELPQLLRLGEEMGVDPMIGLR---------SKLTTrgTGK 222
Cdd:cd06828 72 PE--RIvftGNGKSDEE-LELAL---ELG-ILRINVDSLSELERLGEIAPELGKGAPVALRvnpgvdagtHPYIS--TGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 223 WEgssgdfAKFGLTVPELIQAVRILKEAgkeHCAKL--LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVG 300
Cdd:cd06828 143 KD------SKFGIPLEQALEAYRRAKEL---PGLKLvgLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLG 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501518076 301 GGLGVDYV-GTRTNDFtssvnysmDEYVGDVVYNVQRVCmnEGVPEPHIVSESGRAVTAHHSCII 364
Cdd:cd06828 214 GGLGIPYRdEDEPLDI--------EEYAEAIAEALKELC--EGGPDLKLIIEPGRYIVANAGVLL 268
|
|
| Arg_decarb_HB |
pfam17810 |
Arginine decarboxylase helical bundle domain; This entry represents a helical bundle domain ... |
386-463 |
1.74e-18 |
|
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: 80.31 E-value: 1.74e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501518076 386 EPNEAKVVREMREIVSSLTPRNRAETYHDAAAKKEEALQMFKLGILGLEERAVVESLFWKLVRGIADMNRGKKRPPRE 463
Cdd:pfam17810 1 DEDAPLLLQNLWELLENLSQRNLLESYHDALHYLDEAHTLFNHGYLSLEQRALAEQLYWAICRRIRALLDPLKRVHRE 78
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
73-308 |
1.70e-15 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.
Pssm-ID: 143509 [Multi-domain] Cd Length: 423 Bit Score: 79.23 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 73 GFPCVVRFQDVLRARVKQINEAFgkavAEMGY-GASYFGVypiKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGM 151
Cdd:cd06842 9 GSPLNVLFPQTFRENIAALRAVL----DRHGVdGRVYFAR---KANKSLALVRAAAAAGI----GVDVASLAELRQALAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 152 NADPDALtICNG-YKDEEYLRLALLGRklgrkVIVVIEKLSELPQLLRLGEEMGVDPM-IGLRsklttrgtgkWEGSSGD 229
Cdd:cd06842 78 GVRGDRI-VATGpAKTDEFLWLAVRHG-----ATIAVDSLDELDRLLALARGYTTGPArVLLR----------LSPFPAS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 230 -FAKFGLTVPELIQAVRILKEAGKEHCAKLLHFHVGSQLTEIRVvkDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYV 308
Cdd:cd06842 142 lPSRFGMPAAEVRTALERLAQLRERVRLVGFHFHLDGYSAAQRV--AALQECLPLIDRARALGLAPRFIDIGGGFPVSYL 219
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
38-358 |
2.26e-15 |
|
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: 78.49 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 38 FSINEKGHVavhpmgqpgpTIDLMDVVEDIRErnIGFPCVVRFQDVLRARVKQINEAFGKA--VAemgygasyfgvYPIK 115
Cdd:TIGR01048 1 TVENEDGEL----------FIEGVPLLELAQE--FGTPLYVYDEDTIRRRFRAYKEAFGGRslVC-----------YAVK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 116 VNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLALlgrKLGrkVIVVIEKLSELPQ 195
Cdd:TIGR01048 58 ANSNLAVLRLLAELGS----GFDVVSGGELYRALAAGFPPEKIVFSGNGKSRAELERAL---ELG--ICINVDSFSELER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 196 LLRLGEEMGVDPMIGLR-SKLTTRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAKLlHFHVGSQLTEIRVVK 274
Cdd:TIGR01048 129 LNEIAPELGKKARISLRvNPGVDAKTHPYISTGLKDSKFGIDVEEALEAYLYALQLPHLELVGI-HCHIGSQITDLSPFV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 275 DAVNEGARVYAKLrKMGLPIEYFDVGGGLGVDYVGtrtndftSSVNYSMDEYVGDVVYNVQRVCmnEGVPEPHIVSESGR 354
Cdd:TIGR01048 208 EAAEKVVKLAESL-AEGIDLEFLDLGGGLGIPYTP-------EEEPPDLSEYAQAILNALEGYA--DLGLDPKLILEPGR 277
|
....
gi 501518076 355 AVTA 358
Cdd:TIGR01048 278 SIVA 281
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
112-358 |
1.55e-14 |
|
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: 75.61 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 112 YPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNADPDALTICNGYKDEEYLRLAllgRKLGRKVIVV----- 186
Cdd:cd00622 30 YAVKCNPDPAVLRTLAALGA----GFDCASKGEIELVLGLGVSPERIIFANPCKSISDIRYA---AELGVRLFTFdsede 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 187 IEKLSELPQ----LLRLgeemgvdpmiglrskLTTRGTGKWEGSsgdfAKFGLTVPEliqAVRILKEAgKEHCAKL--LH 260
Cdd:cd00622 103 LEKIAKHAPgaklLLRI---------------ATDDSGALCPLS----RKFGADPEE---ARELLRRA-KELGLNVvgVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 261 FHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTN--DFTSSVNYSMDEYVGDvvynvqrvc 338
Cdd:cd00622 160 FHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSfeEIAAVINRALDEYFPD--------- 230
|
250 260
....*....|....*....|
gi 501518076 339 mnegvPEPHIVSESGRAVTA 358
Cdd:cd00622 231 -----EGVRIIAEPGRYLVA 245
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
160-358 |
3.08e-14 |
|
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: 74.99 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 160 ICNG-YKDEEYLRLALLgrklgRKVIVVIEKLSELPQLLRLGEEMGVDPMIGLRSKLTTrGTGKWegssgdfAKFGLTVP 238
Cdd:cd06841 82 IFNGpYKSKEELEKALE-----EGALINIDSFDELERILEIAKELGRVAKVGIRLNMNY-GNNVW-------SRFGFDIE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 239 ELIQAVRILKEAGKEHCAKL--LHFHVGSQLTEIRV----VKDAVNEGARVYaklrkmGLPIEYFDVGGGLGVDYVgTRT 312
Cdd:cd06841 149 ENGEALAALKKIQESKNLSLvgLHCHVGSNILNPEAysaaAKKLIELLDRLF------GLELEYLDLGGGFPAKTP-LSL 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501518076 313 NDFTSSVNYSMDEYVgDVVYNVQRVCMNEGVPEPHIVSESGRAVTA 358
Cdd:cd06841 222 AYPQEDTVPDPEDYA-EAIASTLKEYYANKENKPKLILEPGRALVD 266
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
73-354 |
1.58e-11 |
|
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: 66.46 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 73 GFPCVVRFQDVLRARVKQINEAFGKAVAEMgygasyfgvYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMN 152
Cdd:cd06839 6 GTPFYVYDRDRVRERYAALRAALPPAIEIY---------YSLKANPNPALVAHLRQLGD----GAEVASAGELALALEAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 153 ADPDALTICNGYKDEEYLRLALlgrKLGRKVIVViEKLSELPQLLRLGEEMGVDPMIGLR---------SKLTTRGTGKw 223
Cdd:cd06839 73 VPPEKILFAGPGKSDAELRRAI---EAGIGTINV-ESLEELERIDALAEEHGVVARVALRinpdfelkgSGMKMGGGPS- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 224 egssgdfaKFGL---TVPELIQAVRilkeAGKEHCAKLLHFHVGSQLTE----IRVVKDAVNEGARVYAKLrkmGLPIEY 296
Cdd:cd06839 148 --------QFGIdveELPAVLARIA----ALPNLRFVGLHIYPGTQILDadalIEAFRQTLALALRLAEEL---GLPLEF 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 297 FDVGGGLGVDYV-GTRTNDFtssvnysmdEYVGDVVYN-VQRVCMNEgvPEPHIVSESGR 354
Cdd:cd06839 213 LDLGGGFGIPYFpGETPLDL---------EALGAALAAlLAELGDRL--PGTRVVLELGR 261
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
82-367 |
1.21e-10 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with similarity to Ornithine and Diaminopimelate Decarboxylases; This subfamily contains uncharacterized proteins with similarity to ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.
Pssm-ID: 143505 [Multi-domain] Cd Length: 379 Bit Score: 63.57 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 82 DVLRARVKQINEAFGKAVaemgygasyFGVYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNADPDALTIC 161
Cdd:cd06836 11 DGFRALVARLTAAFPAPV---------LHTFAVKANPLVPVLRLLAEAGA----GAEVASPGELELALAAGFPPERIVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 162 NGYKDEEYLRLALlgrKLGrkVIVVIEKLSELPQLLRL-GEEMGVDPMIGLRSKLTTrGTGKWEGSSGDFA--KFGLTVp 238
Cdd:cd06836 78 SPAKTRAELREAL---ELG--VAINIDNFQELERIDALvAEFKEASSRIGLRVNPQV-GAGKIGALSTATAtsKFGVAL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 239 ELIQAVRILKEAGKEHCAKLLHFHVGSQLTEIrvvkDAVNEGARVYAKL-----RKMG-LPIEYFDVGGGLGVDYVGT-R 311
Cdd:cd06836 151 EDGARDEIIDAFARRPWLNGLHVHVGSQGCEL----SLLAEGIRRVVDLaeeinRRVGrRQITRIDIGGGLPVNFESEdI 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501518076 312 TNDFTSSVNYsmdeyvgdvvynvqrvcMNEGVPE-----PHIVSESGRAVTAHHSCIIIPV 367
Cdd:cd06836 227 TPTFADYAAA-----------------LKAAVPElfdgrYQLVTEFGRSLLAKCGTIVSRV 270
|
|
| Arg_decarbox_C |
pfam17944 |
Arginine decarboxylase C-terminal helical extension; This small three helical domain is found ... |
598-651 |
2.46e-10 |
|
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: 56.00 E-value: 2.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 501518076 598 IEKVLSRVQYEPADLFRRVKAALDQKvkegAIRPKEGVSLQDFYEAVMKGYTYL 651
Cdd:pfam17944 1 VADVLRYVQYDPEELLERYRRQVEAA----RLSAEERRALLEELEAGLKGYTYL 50
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
112-360 |
5.70e-09 |
|
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: 58.45 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 112 YPIKVNQMREvvdeIVDAGAPYHYGLEAGSKGELLVVLGmnADPDALTICNG--YKDEEyLRLAllgrkLGRKVIVV-IE 188
Cdd:cd06843 31 YAIKANSDPP----ILRALAPHVDGFEVASGGEIAHVRA--AVPDAPLIFGGpgKTDSE-LAQA-----LAQGVERIhVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 189 KLSELPQLLRLGEEMGVDPMIGLRSKLTTRGTgkwEGSS----GDFAKFGLTVPELIQAVRILKEAGkehCAKL--LHFH 262
Cdd:cd06843 99 SELELRRLNAVARRAGRTAPVLLRVNLALPDL---PSSTltmgGQPTPFGIDEADLPDALELLRDLP---NIRLrgFHFH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 263 VGS-QL---TEIRVVKDAVnEGARVYAklRKMGLPIEYFDVGGGLGVDYV-GTRTNDFtssvnysmDEYvGDVVYNVQRv 337
Cdd:cd06843 173 LMShNLdaaAHLALVKAYL-ETARQWA--AEHGLDLDVVNVGGGIGVNYAdPEEQFDW--------AGF-CEGLDQLLA- 239
|
250 260
....*....|....*....|...
gi 501518076 338 cmnEGVPEPHIVSESGRAVTAHH 360
Cdd:cd06843 240 ---EYEPGLTLRFECGRYISAYC 259
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
84-307 |
2.33e-08 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 54.63 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 84 LRARVKQINEAFGKAVAEMgygasyfgvYPIKVNQMREVVDEIVDAGApyhyGLEAGSKGELLVVLGMNADPDALTICNG 163
Cdd:cd06808 1 IRHNYRRLREAAPAGITLF---------AVVKANANPEVARTLAALGT----GFDVASLGEALLLRAAGIPPEPILFLGP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 164 YKDEEYLRLALlgrKLGRKVIVVI--EKLSELPQL-LRLGEEMGVDPMIGlrsklttrgTGKWEGssgdfaKFGLTVPEL 240
Cdd:cd06808 68 CKQVSELEDAA---EQGVIVVTVDslEELEKLEEAaLKAGPPARVLLRID---------TGDENG------KFGVRPEEL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501518076 241 IQAVRILKEAgkeHCAKL--LHFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDY 307
Cdd:cd06808 130 KALLERAKEL---PHLRLvgLHTHFGSADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILY 195
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
60-307 |
1.07e-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: 54.36 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 60 LMDVVEDIRernigfPCVVRFQDVLRARVKQINeafgkavaemGYGASYFGVYPIKVNQMREVVDEIVDAGApyhyGLEA 139
Cdd:cd06840 4 LLRLAPDVG------PCYVYDLETVRARARQVS----------ALKAVDSLFYAIKANPHPDVLRTLEEAGL----GFEC 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 140 GSKGELLVVLGM--NADPD-ALTICNGYKDEEYLRLALLGRKLgrkVIVVIEKLSELPQLLRlGEE--MGVDPMIGlrsk 214
Cdd:cd06840 64 VSIGELDLVLKLfpDLDPRrVLFTPNFAARSEYEQALELGVNV---TVDNLHPLREWPELFR-GREviLRIDPGQG---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 215 lttRGTGKWEGSSGDFAKFGLTVPELIQAVRILKEAGKEHCAklLHFHVGSQLTEirvvkdaVNEGARVYAKLRKM--GL 292
Cdd:cd06840 136 ---EGHHKHVRTGGPESKFGLDVDELDEARDLAKKAGIIVIG--LHAHSGSGVED-------TDHWARHGDYLASLarHF 203
|
250
....*....|....*.
gi 501518076 293 P-IEYFDVGGGLGVDY 307
Cdd:cd06840 204 PaVRILNVGGGLGIPE 219
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
72-307 |
1.54e-05 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 48.15 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 72 IGFPCVVRFQDVLRARVKQINEAfgKAVAEmgygasyfGVYPIKVNQMREVVDEIVDAGapyhYGLEAGSKGELLVVLGM 151
Cdd:PRK08961 501 AGSPCYVYHLPTVRARARALAAL--AAVDQ--------RFYAIKANPHPAILRTLEEEG----FGFECVSIGELRRVFEL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 152 --NADPD-ALTICNGYKDEEYLRLALLGrklgrkVIVVI---EKLSELPQLLRlGEE--MGVDPMIGlrsklttRGTGKW 223
Cdd:PRK08961 567 fpELSPErVLFTPNFAPRAEYEAAFALG------VTVTLdnvEPLRNWPELFR-GREvwLRIDPGHG-------DGHHEK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 224 EGSSGDFAKFGLTVPELIQAVRILKEAGkehcAKL--LHFHVGSQLTEirvvKDAVNEGARVYAKL-RKMGlPIEYFDVG 300
Cdd:PRK08961 633 VRTGGKESKFGLSQTRIDEFVDLAKTLG----ITVvgLHAHLGSGIET----GEHWRRMADELASFaRRFP-DVRTIDLG 703
|
....*..
gi 501518076 301 GGLGVDY 307
Cdd:PRK08961 704 GGLGIPE 710
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
260-369 |
4.19e-05 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 46.32 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501518076 260 HFHVGSQLTEIRVVKDAVNEGARVYAKLRKMGLPIEYFDVGGGLGVDYVGTRTNDFTSSvnysmdeyvgDVVYNVQRVCM 339
Cdd:PLN02537 188 HCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDYYHAGAVLPTPR----------DLIDTVRELVL 257
|
90 100 110
....*....|....*....|....*....|
gi 501518076 340 NEGVpepHIVSESGRAVTAHHSCIIIPVFG 369
Cdd:PLN02537 258 SRDL---TLIIEPGRSLIANTCCFVNRVTG 284
|
|
| |
