|
Name |
Accession |
Description |
Interval |
E-value |
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
151-585 |
8.17e-170 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 488.55 E-value: 8.17e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 151 PPFFRALVDYAQDGSYSWHCPGHSGGVAFLKSPVGQMFHQFFGENMLRADVCNAVDELGQLLDHSGPVAKAERNAARIFN 230
Cdd:pfam01276 1 PPLYKALFKYVRRGNYTFHCPGHQGGAGFQKHPAGRFFYDFFGENLLRIDVCIEDVELGDLLDHEGAIKEAQKYAARVFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 231 ADHCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIPVFLTPTRNHLGIIGPIPLDEFKPESIRRRI 310
Cdd:pfam01276 81 ADKSYFVVNGTSGSNKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGATPVYLEPSRNAYGIIGGIPLHEFQEETLKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 311 EANPFAreaksKKPRILTITQSTYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYKDMHAIGKDrpRSKDSLIS 390
Cdd:pfam01276 161 AEVPDA-----KGPRLAVITNPTYDGVLYNAKEIVDTLHHLSDPILFDSAWVGYEQFIPIYADASPMGGE--NENGPGIF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 391 ATHSVHKLLAGLSQASQILVQEGetRKLDRHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTALVEESITEALDFR 470
Cdd:pfam01276 234 VTQSVHKLLAALSQASYIHKKEG--HIVNHDRFNEAFMMHATTSPSYPIFASLDVAAKMLEGNSGRRLWNECVERAIEFR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 471 RAMRKVDDEWGkdwwFKVWGPtnlaaEGMGKREDWMLRANEKWHGFGNLAPGFNMLDPIKATVITPGLDVSGKFAKTGIP 550
Cdd:pfam01276 312 KAIDTLNNCEF----FRPWNP-----EIVDGKECWPFHPGETWHGFEGYADNQYFLDPCKLTILTPGMDEDGEYSEFGVP 382
|
410 420 430
....*....|....*....|....*....|....*
gi 1671290574 551 ASIVTKYLAEHGVIVEKTGLYSFFIMFTIGITKGR 585
Cdd:pfam01276 383 ATIVAKWLRENGIVPEKTDLNNILFLFTPGEDRTK 417
|
|
| PRK15399 |
PRK15399 |
lysine decarboxylase; |
24-585 |
1.59e-166 |
|
lysine decarboxylase;
Pssm-ID: 185297 [Multi-domain] Cd Length: 713 Bit Score: 490.79 E-value: 1.59e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 24 IRALAGAIEKEGLEILGVTSYYDLSQYAQQQSRASAFILSIDDEefgtgtaaeteaalkSLRAFvEEIRFKNAEIPIYLY 103
Cdd:PRK15399 19 IKELESALQAQGFQTIWPQNSVDLLKFIEHNPRICGVIFDWDEY---------------SLDLC-SDINQLNEYLPLYAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 104 GETrtsrHIPNDI-LRELHGFIHTFE---DTPEFVARHIVREARAYLDSLAPPFFRALVDYAQDGSYSWHCPGHSGGVAF 179
Cdd:PRK15399 83 INT----HSTMDVsVQDMRMALWFFEyalGAAEDIAIRIRQYTNEYLDNITPPFTKALFTYVKEGKYTFCTPGHMGGTAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 180 LKSPVGQMFHQFFGENMLRADVCNAVDELGQLLDHSGPVAKAERNAARIFNADHCFFVTNGTSTSNKMVWHANVAPGDIV 259
Cdd:PRK15399 159 QKSPVGCLFYDFFGGNTLKADVSISVTELGSLLDHTGPHLEAEEYIARTFGAEQSYIVTNGTSTSNKIVGMYAAPAGSTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 260 VVDRNCHVSILHAITMTGAIPVFLTPTRNHLGIIGPIPLDEFKPESIRRRIEANPFAreaksKKPRILTITQSTYDGVVY 339
Cdd:PRK15399 239 LIDRNCHKSLAHLLMMSDVVPIWLKPTRNALGILGGIPRREFTRDSIEEKVAATTQA-----QWPVHAVITNSTYDGLLY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 340 NVEMLKQTLNgtIETLHFDEAWLPHAAFHDFYKDMHAIGKDRPRSKdsLISATHSVHKLLAGLSQASQILVQeGEtrkLD 419
Cdd:PRK15399 314 NTDWIKQTLD--VPSIHFDSAWVPYTHFHPIYQGKSGMSGERVPGK--VIFETQSTHKMLAAFSQASLIHIK-GE---YD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 420 RHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTALVEESITEALDFRRAMRKVDDEWGkDWWFKVWGPtnlaaEGM 499
Cdd:PRK15399 386 EETFNEAFMMHTSTSPSYPIVASVETAAAMLRGNPGKRLINRSVERALHFRKEVQRLREESD-GWFFDIWQP-----ENV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 500 GKREDWMLRANEKWHGFGNLAPGFNMLDPIKATVITPGLDVSGKFAKTGIPASIVTKYLAEHGVIVEKTGLYSFFIMFTI 579
Cdd:PRK15399 460 DEAECWPVAPGEQWHGFKDADADHMFLDPVKVTILTPGMDEQGNMSEEGIPAALVAKFLDERGIVVEKTGPYNLLFLFSI 539
|
....*.
gi 1671290574 580 GITKGR 585
Cdd:PRK15399 540 GIDKTK 545
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
145-584 |
1.12e-142 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 421.83 E-value: 1.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 145 YLDSLAPPFFRALVDYAQDGSYSWHCPGHSGGVAFlkspvGQMFHQFFGENMLRADVCNaVDELGQLLDHSGPVAKAERN 224
Cdd:COG1982 1 YMDQLLTPLFDALKKYAERGPVSFHVPGHKGGRGF-----GREFYDFFGENVFRLDLTE-LPGLDDLHDPEGVIKEAQEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 225 AARIFNADHCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIPVFLTPT-RNHLGIIGPIPldefkP 303
Cdd:COG1982 75 AAEAFGADRTFFLVNGTSSGNKAMILAVCGPGDKVLVPRNCHKSVIHGLILSGAIPVYLNPEiDNELGIIGGIT-----P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 304 ESIRRRIEANPfareakskKPRILTITQSTYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYK--------DMh 375
Cdd:COG1982 150 EAVEEALIEHP--------DAKAVLITNPTYYGVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLPrsameagaDL- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 376 aigkdrprskdslisATHSVHKLLAGLSQASQILVQEGetrKLDRHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPgG 455
Cdd:COG1982 221 ---------------VVQSTHKTLGALTQSSMLHVKGG---RVDHERVNEALMLLQSTSPSYLLMASLDVARRQMAGE-G 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 456 TALVEESITEALDFRRAMRKVddewgkdWWFKVWGPTNLAaegmgkredwmlranekwhgfgnlAPGFNMLDPIKATVIT 535
Cdd:COG1982 282 EELLDEALELAIEARKEINKI-------PGLYVFGPEDLG------------------------APGVYDLDPTKLTIDV 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1671290574 536 PGLdvsgkfaktGIPASIVTKYLAEH-GVIVEKTGLYSFFIMFTIGITKG 584
Cdd:COG1982 331 PGL---------GISGYEVAEYLREEyGIQVELADLYNILFLLSLGDTKE 371
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
152-475 |
2.03e-105 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 319.19 E-value: 2.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 152 PFFRALVDYAQDGSYSWHCPGHSGGVAFLKSpvgqmFHQFFGENMLRADVCNaVDELGQLLDHSGPVAKAERNAARIFNA 231
Cdd:cd00615 1 PLFEALKEYAKRGIISFHVPGHKGGRGFRKS-----FYEFYGENLFKADVTE-LTGLDDLLDPTGPIKEAQELAARAFGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 232 DHCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIPVFLTPTRN-HLGIIGPIPLDEFKPESIRRRi 310
Cdd:cd00615 75 KHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNpYYGIAGGIPPETFKKALIEHP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 311 eanpfareakskKPRILTITQSTYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYkdmhaigkdrPRS--KDSL 388
Cdd:cd00615 154 ------------DAKAAVITNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPIL----------PSSaaMAGA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 389 ISATHSVHKLLAGLSQASQILVQEGetrKLDRHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTaLVEESITEALD 468
Cdd:cd00615 212 DIVVQSTHKTLPALTQGSMIHVKGD---LVNPDRVNEALNLHQSTSPSYLILASLDVARAMMALEGKE-LVEELIELALY 287
|
....*..
gi 1671290574 469 FRRAMRK 475
Cdd:cd00615 288 ARQEINK 294
|
|
| OKR_DC_1_N |
pfam03709 |
Orn/Lys/Arg decarboxylase, N-terminal domain; This domain has a flavodoxin-like fold, and is ... |
19-145 |
2.47e-35 |
|
Orn/Lys/Arg decarboxylase, N-terminal domain; This domain has a flavodoxin-like fold, and is termed the "wing" domain because of its position in the overall 3D structure.
Pssm-ID: 427454 [Multi-domain] Cd Length: 111 Bit Score: 128.51 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 19 ASGLGIRALAGAIEKEGLEILGVTSYYDLSQYAQQQSRASAFILSIDDEefgtgtaaeteaalksLRAFVEEIRFKNAEI 98
Cdd:pfam03709 1 LKIAASRELAEALERTGREVVDATSTDDLLAAIETFTDIAAVVLSWDDY----------------AAGLLDEIRRRNFDL 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1671290574 99 PIYLYGETRTSRHIPNDILRELHGFIHTFEDTPEFVARHIVREARAY 145
Cdd:pfam03709 65 PVFLLGETHTSEDVPADVLRLIDGFIELAEDTPEFIARQIEAAAKKY 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
151-585 |
8.17e-170 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 488.55 E-value: 8.17e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 151 PPFFRALVDYAQDGSYSWHCPGHSGGVAFLKSPVGQMFHQFFGENMLRADVCNAVDELGQLLDHSGPVAKAERNAARIFN 230
Cdd:pfam01276 1 PPLYKALFKYVRRGNYTFHCPGHQGGAGFQKHPAGRFFYDFFGENLLRIDVCIEDVELGDLLDHEGAIKEAQKYAARVFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 231 ADHCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIPVFLTPTRNHLGIIGPIPLDEFKPESIRRRI 310
Cdd:pfam01276 81 ADKSYFVVNGTSGSNKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGATPVYLEPSRNAYGIIGGIPLHEFQEETLKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 311 EANPFAreaksKKPRILTITQSTYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYKDMHAIGKDrpRSKDSLIS 390
Cdd:pfam01276 161 AEVPDA-----KGPRLAVITNPTYDGVLYNAKEIVDTLHHLSDPILFDSAWVGYEQFIPIYADASPMGGE--NENGPGIF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 391 ATHSVHKLLAGLSQASQILVQEGetRKLDRHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTALVEESITEALDFR 470
Cdd:pfam01276 234 VTQSVHKLLAALSQASYIHKKEG--HIVNHDRFNEAFMMHATTSPSYPIFASLDVAAKMLEGNSGRRLWNECVERAIEFR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 471 RAMRKVDDEWGkdwwFKVWGPtnlaaEGMGKREDWMLRANEKWHGFGNLAPGFNMLDPIKATVITPGLDVSGKFAKTGIP 550
Cdd:pfam01276 312 KAIDTLNNCEF----FRPWNP-----EIVDGKECWPFHPGETWHGFEGYADNQYFLDPCKLTILTPGMDEDGEYSEFGVP 382
|
410 420 430
....*....|....*....|....*....|....*
gi 1671290574 551 ASIVTKYLAEHGVIVEKTGLYSFFIMFTIGITKGR 585
Cdd:pfam01276 383 ATIVAKWLRENGIVPEKTDLNNILFLFTPGEDRTK 417
|
|
| PRK15399 |
PRK15399 |
lysine decarboxylase; |
24-585 |
1.59e-166 |
|
lysine decarboxylase;
Pssm-ID: 185297 [Multi-domain] Cd Length: 713 Bit Score: 490.79 E-value: 1.59e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 24 IRALAGAIEKEGLEILGVTSYYDLSQYAQQQSRASAFILSIDDEefgtgtaaeteaalkSLRAFvEEIRFKNAEIPIYLY 103
Cdd:PRK15399 19 IKELESALQAQGFQTIWPQNSVDLLKFIEHNPRICGVIFDWDEY---------------SLDLC-SDINQLNEYLPLYAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 104 GETrtsrHIPNDI-LRELHGFIHTFE---DTPEFVARHIVREARAYLDSLAPPFFRALVDYAQDGSYSWHCPGHSGGVAF 179
Cdd:PRK15399 83 INT----HSTMDVsVQDMRMALWFFEyalGAAEDIAIRIRQYTNEYLDNITPPFTKALFTYVKEGKYTFCTPGHMGGTAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 180 LKSPVGQMFHQFFGENMLRADVCNAVDELGQLLDHSGPVAKAERNAARIFNADHCFFVTNGTSTSNKMVWHANVAPGDIV 259
Cdd:PRK15399 159 QKSPVGCLFYDFFGGNTLKADVSISVTELGSLLDHTGPHLEAEEYIARTFGAEQSYIVTNGTSTSNKIVGMYAAPAGSTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 260 VVDRNCHVSILHAITMTGAIPVFLTPTRNHLGIIGPIPLDEFKPESIRRRIEANPFAreaksKKPRILTITQSTYDGVVY 339
Cdd:PRK15399 239 LIDRNCHKSLAHLLMMSDVVPIWLKPTRNALGILGGIPRREFTRDSIEEKVAATTQA-----QWPVHAVITNSTYDGLLY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 340 NVEMLKQTLNgtIETLHFDEAWLPHAAFHDFYKDMHAIGKDRPRSKdsLISATHSVHKLLAGLSQASQILVQeGEtrkLD 419
Cdd:PRK15399 314 NTDWIKQTLD--VPSIHFDSAWVPYTHFHPIYQGKSGMSGERVPGK--VIFETQSTHKMLAAFSQASLIHIK-GE---YD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 420 RHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTALVEESITEALDFRRAMRKVDDEWGkDWWFKVWGPtnlaaEGM 499
Cdd:PRK15399 386 EETFNEAFMMHTSTSPSYPIVASVETAAAMLRGNPGKRLINRSVERALHFRKEVQRLREESD-GWFFDIWQP-----ENV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 500 GKREDWMLRANEKWHGFGNLAPGFNMLDPIKATVITPGLDVSGKFAKTGIPASIVTKYLAEHGVIVEKTGLYSFFIMFTI 579
Cdd:PRK15399 460 DEAECWPVAPGEQWHGFKDADADHMFLDPVKVTILTPGMDEQGNMSEEGIPAALVAKFLDERGIVVEKTGPYNLLFLFSI 539
|
....*.
gi 1671290574 580 GITKGR 585
Cdd:PRK15399 540 GIDKTK 545
|
|
| PRK15029 |
PRK15029 |
arginine decarboxylase; Provisional |
7-585 |
2.53e-160 |
|
arginine decarboxylase; Provisional
Pssm-ID: 184989 [Multi-domain] Cd Length: 755 Bit Score: 476.64 E-value: 2.53e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 7 IVIIDEDFRSENAS-GLGIRALAGAIEKEGLEILGVTSYYDLSQYAQQQSRASAFILSiddeefgtgTAAETEAALKSLR 85
Cdd:PRK15029 3 VLIVESEFLHQDTWvGNAVERLADALSQQNVTVIKSTSFDDGFAILSSNEAIDCLMFS---------YQMEHPDEHQNVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 86 AFVEEIRFKNAEIPIYLYGET-RTSRHIPNDILRELHGFIHTFEDTPEFVARHIVREARAYLDSLAPPFFRALVDYAQDG 164
Cdd:PRK15029 74 QLIGKLHERQQNVPVFLLGDReKALAAMDRDLLELVDEFAWILEDTADFIAGRAVAAMTRYRQQLLPPLFSALMKYSDIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 165 SYSWHCPGHSGGVAFLKSPVGQMFHQFFGENMLRADVCNAVDELGQLLDHSGPVAKAERNAARIFNADHCFFVTNGTSTS 244
Cdd:PRK15029 154 EYSWAAPGHQGGVGFTKTPAGRFYHDYYGENLFRTDMGIERTSLGSLLDHTGAFGESEKYAARVFGADRSWSVVVGTSGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 245 NKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIPVFLTPTRNHLGIIGPIPLDEFKPESIRRRIEANPFAREAKSKKP 324
Cdd:PRK15029 234 NRTIMQACMTDNDVVVVDRNCHKSIEQGLILTGAKPVYMVPSRNRYGIIGPIYPQEMQPETLQKKISESPLTKDKAGQKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 325 RILTITQSTYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYKDMHAIGKDRPRSKDSLISATHSVHKLLAGLSQ 404
Cdd:PRK15029 314 SYCVVTNCTYDGVCYNAKEAQDLLEKTSDRLHFDEAWYGYARFNPIYADHYAMRGEPGDHNGPTVFATHSTHKLLNALSQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 405 ASQILVQEGEtRKLDRHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTALVEESITEALDFRRAMRKVDDEWGK-- 482
Cdd:PRK15029 394 ASYIHVREGR-GAINFSRFNQAYMMHATTSPLYAICASNDVAVSMMDGNSGLSLTQEVIDEAVDFRQAMARLYKEFTAdg 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 483 DWWFKVWGPTNLAAEGMGKRED---------------WMLRANEKWHGFGNLAPGFNMLDPIKATVITPGLDVSGKFAKT 547
Cdd:PRK15029 473 SWFFKPWNKEVVTDPQTGKTYDfadaptkllttvqdcWVMHPGESWHGFKDLPDNWSMLDPIKVSILAPGMGEDGELEET 552
|
570 580 590
....*....|....*....|....*....|....*...
gi 1671290574 548 GIPASIVTKYLAEHGVIVEKTGLYSFFIMFTIGITKGR 585
Cdd:PRK15029 553 GVPAALVTAWLGRHGIVPTRTTDFQIMFLFSMGVTRGK 590
|
|
| PRK15400 |
PRK15400 |
lysine decarboxylase; |
24-585 |
1.16e-149 |
|
lysine decarboxylase;
Pssm-ID: 185298 [Multi-domain] Cd Length: 714 Bit Score: 447.76 E-value: 1.16e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 24 IRALAGAIEKEGLEILGVTSYYDLSQYAQQQSRASAFILSIDdeefgtgtaaeteaalKSLRAFVEEIRFKNAEIPIYLY 103
Cdd:PRK15400 19 IRELHRALERLNFQIVYPNDRDDLLKLIENNARLCGVIFDWD----------------KYNLELCEEISKMNENLPLYAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 104 GETRTSRHIP-NDILRELHGFIHTFeDTPEFVARHIVREARAYLDSLAPPFFRALVDYAQDGSYSWHCPGHSGGVAFLKS 182
Cdd:PRK15400 83 ANTYSTLDVSlNDLRLQVSFFEYAL-GAADDIANKIKQTTDEYIDTILPPLTKALFKYVREGKYTFCTPGHMGGTAFQKS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 183 PVGQMFHQFFGENMLRADVCNAVDELGQLLDHSGPVAKAERNAARIFNADHCFFVTNGTSTSNKMVWHANVAPGDIVVVD 262
Cdd:PRK15400 162 PVGSLFYDFFGPNTMKSDISISVSELGSLLDHSGPHKEAEEYIARVFNADRSYMVTNGTSTANKIVGMYSAPAGSTVLID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 263 RNCHVSILHAITMTGAIPVFLTPTRNHLGIIGPIPLDEFKPESIRRRIEANPFAreaksKKPRILTITQSTYDGVVYNVE 342
Cdd:PRK15400 242 RNCHKSLTHLMMMSDVTPIYFRPTRNAYGILGGIPQSEFQHATIAKRVKETPNA-----TWPVHAVITNSTYDGLLYNTD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 343 MLKQTLNgtIETLHFDEAWLPHAAFHDFYKDMHAIGKDRPRSKdsLISATHSVHKLLAGLSQASQILVQeGEtrkLDRHI 422
Cdd:PRK15400 317 FIKKTLD--VKSIHFDSAWVPYTNFSPIYEGKCGMSGGRVEGK--VIYETQSTHKLLAAFSQASMIHVK-GD---VNEET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 423 FNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTALVEESITEALDFRRAMRKVDDEwGKDWWFKVWGPTNLaaegmGKR 502
Cdd:PRK15400 389 FNEAYMMHTTTSPHYGIVASTETAAAMMKGNAGKRLINGSIERAIKFRKEIKRLRTE-SDGWFFDVWQPDHI-----DTT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 503 EDWMLRANEKWHGFGNLAPGFNMLDPIKATVITPGLDVSGKFAKTGIPASIVTKYLAEHGVIVEKTGLYSFFIMFTIGIT 582
Cdd:PRK15400 463 ECWPLRSDSTWHGFKNIDNEHMYLDPIKVTLLTPGMKKDGTMSDFGIPASIVAKYLDEHGIVVEKTGPYNLLFLFSIGID 542
|
...
gi 1671290574 583 KGR 585
Cdd:PRK15400 543 KTK 545
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
145-584 |
1.12e-142 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 421.83 E-value: 1.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 145 YLDSLAPPFFRALVDYAQDGSYSWHCPGHSGGVAFlkspvGQMFHQFFGENMLRADVCNaVDELGQLLDHSGPVAKAERN 224
Cdd:COG1982 1 YMDQLLTPLFDALKKYAERGPVSFHVPGHKGGRGF-----GREFYDFFGENVFRLDLTE-LPGLDDLHDPEGVIKEAQEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 225 AARIFNADHCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIPVFLTPT-RNHLGIIGPIPldefkP 303
Cdd:COG1982 75 AAEAFGADRTFFLVNGTSSGNKAMILAVCGPGDKVLVPRNCHKSVIHGLILSGAIPVYLNPEiDNELGIIGGIT-----P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 304 ESIRRRIEANPfareakskKPRILTITQSTYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYK--------DMh 375
Cdd:COG1982 150 EAVEEALIEHP--------DAKAVLITNPTYYGVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLPrsameagaDL- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 376 aigkdrprskdslisATHSVHKLLAGLSQASQILVQEGetrKLDRHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPgG 455
Cdd:COG1982 221 ---------------VVQSTHKTLGALTQSSMLHVKGG---RVDHERVNEALMLLQSTSPSYLLMASLDVARRQMAGE-G 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 456 TALVEESITEALDFRRAMRKVddewgkdWWFKVWGPTNLAaegmgkredwmlranekwhgfgnlAPGFNMLDPIKATVIT 535
Cdd:COG1982 282 EELLDEALELAIEARKEINKI-------PGLYVFGPEDLG------------------------APGVYDLDPTKLTIDV 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1671290574 536 PGLdvsgkfaktGIPASIVTKYLAEH-GVIVEKTGLYSFFIMFTIGITKG 584
Cdd:COG1982 331 PGL---------GISGYEVAEYLREEyGIQVELADLYNILFLLSLGDTKE 371
|
|
| PRK13578 |
PRK13578 |
ornithine decarboxylase; Provisional |
61-577 |
8.53e-106 |
|
ornithine decarboxylase; Provisional
Pssm-ID: 237434 [Multi-domain] Cd Length: 720 Bit Score: 334.24 E-value: 8.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 61 ILSIDDEEFgTGTAAETEAALKSLRAFVEEIRFKNAEIPIYLYgeTRTSRHIPNDILRELHGFIHTFEDTPEFVARHIVR 140
Cdd:PRK13578 22 VVALDQTDF-TDVAAVVLSVADSRSGILALIKRTGFGIPVFVA--TEEEEEVPAEVLPRISGVFELCESNNEFYGRQLET 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 141 EARAYLDSLAPPFFRALVDYAQDGSYSWHCPGHSGGVAFLKSPVGQMFHQFFGENMLRADVCNAVDELGQLLDHSGPVAK 220
Cdd:PRK13578 99 AASKYEENLLPPFFDTLTDYVEMGNSTFDCPGHQGGQFFRKHPAGRQFYDFFGENLFRADMCNADVKLGDLLIHEGAAKD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 221 AERNAARIFNADHCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILH-AITMTGAIPVFLTPTRNHLGIIGPIPLD 299
Cdd:PRK13578 179 AQKHAAKVFNADKTYFVLNGTSASNKVVTNALLTPGDLVLFDRNNHKSNHHgALIQAGATPVYLETARNPFGFIGGIDAH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 300 EFKPESIRRRI-EANPfaREAKSKKPRILTITQ-STYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYKD---- 373
Cdd:PRK13578 259 CFDEEYLREQIrEVAP--ERADEARPFRLAVIQlGTYDGTIYNARQVVDKIGHLCDYILFDSAWVGYEQFIPMMADcspl 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 374 MHAIGKDRPRskdslISATHSVHKLLAGLSQASQIlvqegetRKLDRHI-----------FNEAYLMHTSTSPQYAIIAS 442
Cdd:PRK13578 337 LLELNENDPG-----IFVTQSVHKQQAGFSQTSQI-------HKKDNHIkgqarycphkrLNNAFMLHASTSPFYPLFAA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 443 CDVAAAMMEPPGGTALVEESITEALDFRRAMRK------------VDdewGKDWWFkvwGPTNLAAEgmgKREDWMLRAN 510
Cdd:PRK13578 405 LDVNAKMHEGESGRRLWMECVKLGIEARKLILArcklirpfippvVD---GKPWQD---YPTEQIAS---DLRFFSFEPG 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1671290574 511 EKWHGFGNLAPGFNMLDPIKATVITPGLDV-SGKFAKTGIPASIVTKYLAEHGVIVEKTGLYSffIMF 577
Cdd:PRK13578 476 EKWHGFEGYAEDQYFVDPCKLLLTTPGIDAeTGEYEDFGIPATILANYLRENGIVPEKCDLNS--ILF 541
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
152-475 |
2.03e-105 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 319.19 E-value: 2.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 152 PFFRALVDYAQDGSYSWHCPGHSGGVAFLKSpvgqmFHQFFGENMLRADVCNaVDELGQLLDHSGPVAKAERNAARIFNA 231
Cdd:cd00615 1 PLFEALKEYAKRGIISFHVPGHKGGRGFRKS-----FYEFYGENLFKADVTE-LTGLDDLLDPTGPIKEAQELAARAFGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 232 DHCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIPVFLTPTRN-HLGIIGPIPLDEFKPESIRRRi 310
Cdd:cd00615 75 KHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNpYYGIAGGIPPETFKKALIEHP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 311 eanpfareakskKPRILTITQSTYDGVVYNVEMLKQTLNGTIETLHFDEAWLPHAAFHDFYkdmhaigkdrPRS--KDSL 388
Cdd:cd00615 154 ------------DAKAAVITNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPIL----------PSSaaMAGA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 389 ISATHSVHKLLAGLSQASQILVQEGetrKLDRHIFNEAYLMHTSTSPQYAIIASCDVAAAMMEPPGGTaLVEESITEALD 468
Cdd:cd00615 212 DIVVQSTHKTLPALTQGSMIHVKGD---LVNPDRVNEALNLHQSTSPSYLILASLDVARAMMALEGKE-LVEELIELALY 287
|
....*..
gi 1671290574 469 FRRAMRK 475
Cdd:cd00615 288 ARQEINK 294
|
|
| OKR_DC_1_N |
pfam03709 |
Orn/Lys/Arg decarboxylase, N-terminal domain; This domain has a flavodoxin-like fold, and is ... |
19-145 |
2.47e-35 |
|
Orn/Lys/Arg decarboxylase, N-terminal domain; This domain has a flavodoxin-like fold, and is termed the "wing" domain because of its position in the overall 3D structure.
Pssm-ID: 427454 [Multi-domain] Cd Length: 111 Bit Score: 128.51 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 19 ASGLGIRALAGAIEKEGLEILGVTSYYDLSQYAQQQSRASAFILSIDDEefgtgtaaeteaalksLRAFVEEIRFKNAEI 98
Cdd:pfam03709 1 LKIAASRELAEALERTGREVVDATSTDDLLAAIETFTDIAAVVLSWDDY----------------AAGLLDEIRRRNFDL 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1671290574 99 PIYLYGETRTSRHIPNDILRELHGFIHTFEDTPEFVARHIVREARAY 145
Cdd:pfam03709 65 PVFLLGETHTSEDVPADVLRLIDGFIELAEDTPEFIARQIEAAAKKY 111
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
218-345 |
9.16e-07 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 51.18 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 218 VAKAERNAARIFNADHCFFVTNGTStSNKMVWHANVAPGDIVVVDRNCHVSILHAitmtGAIpvfltptrNHLGIIGPIP 297
Cdd:cd06502 34 TAKLEARAAELFGKEAALFVPSGTA-ANQLALAAHTQPGGSVICHETAHIYTDEA----GAP--------EFLSGVKLLP 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1671290574 298 LD----EFKPESIRRRIEANPFAREAkskKPRILTITQSTYDGVVYNVEMLK 345
Cdd:cd06502 101 VPgengKLTPEDLEAAIRPRDDIHFP---PPSLVSLENTTEGGTVYPLDELK 149
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
218-346 |
8.79e-05 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 45.06 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 218 VAKAERNAARIFNADHCFFVTNGTstsnkMvwhANVA-------PGDIVVVDRNCHVsILH---AITMTGAIPVFLTPTR 287
Cdd:COG2008 37 VNRLEERVAELFGKEAALFVPSGT-----M---ANQLalrahtrPGDEVICHETAHI-YVDeggAPEALSGVKLLPVPGE 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1671290574 288 NhlgiiGPIPldefkPESIRRRIEANPFAREakskKPRILTITQSTYDGVVYNVEMLKQ 346
Cdd:COG2008 108 D-----GKLT-----PEDLEAAIRPGDVHFP----QPGLVSLENTTEGGTVYPLEELRA 152
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
217-410 |
1.21e-04 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 43.14 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 217 PVAKAERNAARIFN--ADHCFFVTNGTStSNKMVWHANVAPGDIVVVDRNCHVSIL-HAITMTGAIPVFLTPTRNHLGII 293
Cdd:cd01494 1 KLEELEEKLARLLQpgNDKAVFVPSGTG-ANEAALLALLGPGDEVIVDANGHGSRYwVAAELAGAKPVPVPVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 294 GPIPLDEfkpesirrrieanpfarEAKSKKPRILTITQSTYDGVVYNVEMLKQTL---NGTIetLHFDEAwlpHAAFHdf 370
Cdd:cd01494 80 DVAILEE-----------------LKAKPNVALIVITPNTTSGGVLVPLKEIRKIakeYGIL--LLVDAA---SAGGA-- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1671290574 371 ykdMHAIGKDRPRSKdsLISATHSVHKLLAGlSQASQILV 410
Cdd:cd01494 136 ---SPAPGVLIPEGG--ADVVTFSLHKNLGG-EGGGVVIV 169
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
216-282 |
3.84e-04 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 43.13 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1671290574 216 GP-VAKAERNAARIFNADHCFFVTNGTStSNKMVWHA-NVAPGDIVVVDRNCHVSILHAITMTGAIPVF 282
Cdd:COG0399 29 GPeVKEFEEEFAAYLGVKHAVAVSSGTA-ALHLALRAlGIGPGDEVITPAFTFVATANAILYVGATPVF 96
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
218-347 |
1.65e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 40.66 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 218 VAKAERNAARIFNADHCFFVTNGTStSNKMVWHANVAPGDIVVVDRNCHvsilhaitmtgaipVFLTPTRNH--LGIIGP 295
Cdd:pfam01212 34 VNRLEDRVAELFGKEAALFVPSGTA-ANQLALMAHCQRGDEVICGEPAH--------------IHFDETGGHaeLGGVQP 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1671290574 296 IPLD-----EFKPESIRRRIeanpfAREAKSKKPRI----LTITQSTYDGVVYNVEMLKQT 347
Cdd:pfam01212 99 RPLDgdeagNMDLEDLEAAI-----REVGADIFPPTglisLENTHNSAGGQVVSLENLREI 154
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
217-334 |
3.78e-03 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 39.68 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 217 PVAKAERNAARIFNADhCFFVTNGTSTSNKMVWHANVAPGDIVVVDRNCHVSILHAITMTGAIpVFLTPTRNHlgiigpi 296
Cdd:cd06452 45 PIKDFHHDLAEFLGMD-EARVTPGAREGKFAVMHSLCEKGDWVVVDGLAHYTSYVAAERAGLN-VREVPNTGH------- 115
|
90 100 110
....*....|....*....|....*....|....*...
gi 1671290574 297 PLDEFKPESIRRRIEAnpfAREAKSKKPRILTITQSTY 334
Cdd:cd06452 116 PEYHITPEGYAEVIEE---VKDEFGKPPALALLTHVDG 150
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
198-282 |
6.58e-03 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 39.19 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671290574 198 RADVCNAVDELGQLLdhSGP-VAKAERNAARIFNADHCFFVTNGTSTsNKMVWHA-NVAPGDIVVVDRNCHVSILHAITM 275
Cdd:pfam01041 7 ELAAVREVLKSGWLT--TGPyVREFERAFAAYLGVKHAIAVSSGTAA-LHLALRAlGVGPGDEVITPSFTFVATANAALR 83
|
....*..
gi 1671290574 276 TGAIPVF 282
Cdd:pfam01041 84 LGAKPVF 90
|
|
| |
