|
Name |
Accession |
Description |
Interval |
E-value |
| Bna5 |
COG3844 |
Kynureninase [Amino acid transport and metabolism]; |
1-416 |
0e+00 |
|
Kynureninase [Amino acid transport and metabolism];
Pssm-ID: 443054 [Multi-domain] Cd Length: 420 Bit Score: 669.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 1 MITREQCLYWDQEDELKKFKDEFALPE-GVIYLDGNSLGARPKKSLAVAQHIISQEWGEDLINSWNKADWWGLPTRLGDK 79
Cdd:COG3844 2 ETTRAFARALDAADPLAAFRDRFHLPDdGVIYLDGNSLGLLPKAAAARLAEVLEEEWGELLIRGWNEAPWFDLPERLGDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 80 VAKLIGAEQGEVVISDSTTLNLFKVLSAAVKIQadkfPEHKIIVAEKDAFPTDIYIIEGFIDLIQKGYQVELIDG----- 154
Cdd:COG3844 82 LARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPR----PGRTKILSEADNFPTDRYALEGQARLHGLDEELRLVEPrdget 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 155 --VEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTYKYLNGG 232
Cdd:COG3844 158 lrPEDIEAALDDDVALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLHDWGVDFAVGCTYKYLNGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 233 PGSPALLWVNEKHRDQFWQPLSGWWSHKKPFDMAQHYEPANSIRRYLCGTQPVISMSLIECGVDIFLHADMQKIREKSLK 312
Cdd:COG3844 238 PGAPAFLYVHERHQDRLLQPLAGWWGHATPFAMEPGYEPAPGARRFQLGTPPILSMAALEASLDLFEEAGMDALRAKSLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 313 LTDLFIQLVHQECSEFGFELITPLDHNHRGSHVSYRHEFGYEIIQALIARGVIGDYREPAVLRFGITPLYLGFEDIWNAV 392
Cdd:COG3844 318 LTDYLIFLVEERLAPLGLELITPRDPARRGSQVSLRHPEAYAIFQALIERGVIGDFREPDVIRFGPTPLYTSFEDVWRAV 397
|
410 420
....*....|....*....|....
gi 1661071830 393 QHLKETMLNSEWKNKQyLVRGEVT 416
Cdd:COG3844 398 EILREILEEGEWEKFE-NERGAVT 420
|
|
| kynureninase |
TIGR01814 |
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ... |
7-399 |
1.51e-139 |
|
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130873 [Multi-domain] Cd Length: 406 Bit Score: 404.50 E-value: 1.51e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 7 CLYWDQEDELKKFKDEFALPEG-----VIYLDGNSLGARPKkSLAVAQHIISQEWGEDLINSWNKAD--WWGLPTRLGDk 79
Cdd:TIGR01814 1 ALELDEADPLRALRDEFHLPKIgdenaVIYLDGNSLGLMPK-AARNALKEELDKWAKIAIRGHNTGKapWFTLDESLLK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 80 vAKLIGAEQGEVVISDSTTLNLFKVLSAAVKIQadkfPEHKIIVAEKDAFPTDIYIIEGfIDLIQKGY------QVELID 153
Cdd:TIGR01814 79 -LRLVGAKEDEVVVMNTLTINLHLLLASFYKPT----PKRYKILLEAKAFPSDHYAIES-QLQLHGLTveesmvQIEPRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 154 G----VEDLSRALEK---DVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTY 226
Cdd:TIGR01814 153 EetlrLEDILDTIEKngdDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDFACWCTY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 227 KYLNGGPGSPALLWVNEKHRDQFWQPlsGWWSHKKPFDMAQHY--EPANSIRRyLCgTQPVISMSLIECGVDIFLHADMQ 304
Cdd:TIGR01814 233 KYLNAGPGAGAFVHEKHAHTERPRLA--GWWGHARPTRFKMDNtlGLIPCGFR-IS-NPPILSVAALRGSLDIFDQAGME 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 305 KIREKSLKLTDLFIQLVHQECSE-FGFELITPLDHNHRGSHVSYRHEF-GYEIIQALIARGVIGDYREPAVLRFGITPLY 382
Cdd:TIGR01814 309 ALRKKSLLLTDYLEELIKARCGGpPVLTIITPRDHAQRGCQLSLTHPVpGKAVFQALIKRGVIGDKREPSVIRVAPVPLY 388
|
410
....*....|....*..
gi 1661071830 383 LGFEDIWNAVQHLKETM 399
Cdd:TIGR01814 389 NTFVDVYDAVNVLEEIL 405
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
78-234 |
3.13e-07 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 51.91 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 78 DKVAKLIGAEQGEVVI-SDSTTLNLFKVLSAAVKiqadkfPEHKIIVAEKDAFPtdiyiiEGFID-LIQKGYQVELIDG- 154
Cdd:cd06451 39 EGLRYVFQTENGLTFLlSGSGTGAMEAALSNLLE------PGDKVLVGVNGVFG------DRWADmAERYGADVDVVEKp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 155 ------VEDLSRALEK-DVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTYK 227
Cdd:cd06451 107 wgeavsPEEIAEALEQhDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQK 186
|
....*..
gi 1661071830 228 YLNGGPG 234
Cdd:cd06451 187 ALGAPPG 193
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
79-255 |
6.88e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 44.65 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 79 KVAKLIGAEQGEVVISDSTTLNLFKVLSAAVKIQADKFP-------EHKIIVAEKDAfptdiyiiegfidLIQKGYQVEL 151
Cdd:PLN02651 51 QVAALIGADPKEIIFTSGATESNNLAIKGVMHFYKDKKKhvittqtEHKCVLDSCRH-------------LQQEGFEVTY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 152 I----DGV---EDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGC 224
Cdd:PLN02651 118 LpvksDGLvdlDELAAAIRPDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSIS 197
|
170 180 190
....*....|....*....|....*....|.
gi 1661071830 225 TYKYlnGGPGSPALLWVNEKHRDQFWQPLSG 255
Cdd:PLN02651 198 GHKI--YGPKGVGALYVRRRPRVRLEPLMSG 226
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
78-316 |
8.20e-05 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 44.55 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 78 DKVAKLIGAEQG-EVVISDSTT--LNLFkVLSAAVKIQA-DKF----PEH----------------KIIVAEKDAfptdi 133
Cdd:pfam00266 50 EKVAEFINAPSNdEIIFTSGTTeaINLV-ALSLGRSLKPgDEIviteMEHhanlvpwqelakrtgaRVRVLPLDE----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 134 yiiEGFIDLiqkgyqvelidgvEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHL 213
Cdd:pfam00266 124 ---DGLLDL-------------DELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 214 NQTDSDFAIGCTYKYLngGPGSPALLWVNEKHRDQFWQPLSGwwSHKKPFDMAQHYEPANSIRRYLCGTQPVISMSLIEC 293
Cdd:pfam00266 188 QKLGVDFLAFSGHKLY--GPTGIGVLYGRRDLLEKMPPLLGG--GGMIETVSLQESTFADAPWKFEAGTPNIAGIIGLGA 263
|
250 260
....*....|....*....|...
gi 1661071830 294 GVDIFLHADMQKIREKSLKLTDL 316
Cdd:pfam00266 264 ALEYLSEIGLEAIEKHEHELAQY 286
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Bna5 |
COG3844 |
Kynureninase [Amino acid transport and metabolism]; |
1-416 |
0e+00 |
|
Kynureninase [Amino acid transport and metabolism];
Pssm-ID: 443054 [Multi-domain] Cd Length: 420 Bit Score: 669.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 1 MITREQCLYWDQEDELKKFKDEFALPE-GVIYLDGNSLGARPKKSLAVAQHIISQEWGEDLINSWNKADWWGLPTRLGDK 79
Cdd:COG3844 2 ETTRAFARALDAADPLAAFRDRFHLPDdGVIYLDGNSLGLLPKAAAARLAEVLEEEWGELLIRGWNEAPWFDLPERLGDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 80 VAKLIGAEQGEVVISDSTTLNLFKVLSAAVKIQadkfPEHKIIVAEKDAFPTDIYIIEGFIDLIQKGYQVELIDG----- 154
Cdd:COG3844 82 LARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPR----PGRTKILSEADNFPTDRYALEGQARLHGLDEELRLVEPrdget 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 155 --VEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTYKYLNGG 232
Cdd:COG3844 158 lrPEDIEAALDDDVALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLHDWGVDFAVGCTYKYLNGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 233 PGSPALLWVNEKHRDQFWQPLSGWWSHKKPFDMAQHYEPANSIRRYLCGTQPVISMSLIECGVDIFLHADMQKIREKSLK 312
Cdd:COG3844 238 PGAPAFLYVHERHQDRLLQPLAGWWGHATPFAMEPGYEPAPGARRFQLGTPPILSMAALEASLDLFEEAGMDALRAKSLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 313 LTDLFIQLVHQECSEFGFELITPLDHNHRGSHVSYRHEFGYEIIQALIARGVIGDYREPAVLRFGITPLYLGFEDIWNAV 392
Cdd:COG3844 318 LTDYLIFLVEERLAPLGLELITPRDPARRGSQVSLRHPEAYAIFQALIERGVIGDFREPDVIRFGPTPLYTSFEDVWRAV 397
|
410 420
....*....|....*....|....
gi 1661071830 393 QHLKETMLNSEWKNKQyLVRGEVT 416
Cdd:COG3844 398 EILREILEEGEWEKFE-NERGAVT 420
|
|
| kynureninase |
TIGR01814 |
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ... |
7-399 |
1.51e-139 |
|
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130873 [Multi-domain] Cd Length: 406 Bit Score: 404.50 E-value: 1.51e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 7 CLYWDQEDELKKFKDEFALPEG-----VIYLDGNSLGARPKkSLAVAQHIISQEWGEDLINSWNKAD--WWGLPTRLGDk 79
Cdd:TIGR01814 1 ALELDEADPLRALRDEFHLPKIgdenaVIYLDGNSLGLMPK-AARNALKEELDKWAKIAIRGHNTGKapWFTLDESLLK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 80 vAKLIGAEQGEVVISDSTTLNLFKVLSAAVKIQadkfPEHKIIVAEKDAFPTDIYIIEGfIDLIQKGY------QVELID 153
Cdd:TIGR01814 79 -LRLVGAKEDEVVVMNTLTINLHLLLASFYKPT----PKRYKILLEAKAFPSDHYAIES-QLQLHGLTveesmvQIEPRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 154 G----VEDLSRALEK---DVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTY 226
Cdd:TIGR01814 153 EetlrLEDILDTIEKngdDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDFACWCTY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 227 KYLNGGPGSPALLWVNEKHRDQFWQPlsGWWSHKKPFDMAQHY--EPANSIRRyLCgTQPVISMSLIECGVDIFLHADMQ 304
Cdd:TIGR01814 233 KYLNAGPGAGAFVHEKHAHTERPRLA--GWWGHARPTRFKMDNtlGLIPCGFR-IS-NPPILSVAALRGSLDIFDQAGME 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 305 KIREKSLKLTDLFIQLVHQECSE-FGFELITPLDHNHRGSHVSYRHEF-GYEIIQALIARGVIGDYREPAVLRFGITPLY 382
Cdd:TIGR01814 309 ALRKKSLLLTDYLEELIKARCGGpPVLTIITPRDHAQRGCQLSLTHPVpGKAVFQALIKRGVIGDKREPSVIRVAPVPLY 388
|
410
....*....|....*..
gi 1661071830 383 LGFEDIWNAVQHLKETM 399
Cdd:TIGR01814 389 NTFVDVYDAVNVLEEIL 405
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
78-364 |
2.29e-15 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 77.10 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 78 DKVAKLIGAEQ-GEVVISDSTT--LNLfkVLSAAVKIQADKfpehKIIVAEKDaFPTDIYIIEGFIDliQKGYQVELI-- 152
Cdd:COG0520 66 EKVARFIGAASpDEIIFTRGTTeaINL--VAYGLGRLKPGD----EILITEME-HHSNIVPWQELAE--RTGAEVRVIpl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 153 --DG---VEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTYK 227
Cdd:COG0520 137 deDGeldLEALEALLTPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 228 yLnGGPGSPALLWVNEKHRDQFWQPLSGWwshkkpfDMA-----QHYEPANSIRRYLCGTQPVI-SMSLIECgVDIFLHA 301
Cdd:COG0520 217 -L-YGPTGIGVLYGKRELLEALPPFLGGG-------GMIewvsfDGTTYADLPRRFEAGTPNIAgAIGLGAA-IDYLEAI 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1661071830 302 DMQKIREKSLKLTDLFiqlvHQECSEF-GFELITPLDHNHRGSHVSYRHEfG---YEIIQALIARGV 364
Cdd:COG0520 287 GMEAIEARERELTAYA----LEGLAAIpGVRILGPADPEDRSGIVSFNVD-GvhpHDVAALLDDEGI 348
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
78-234 |
3.13e-07 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 51.91 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 78 DKVAKLIGAEQGEVVI-SDSTTLNLFKVLSAAVKiqadkfPEHKIIVAEKDAFPtdiyiiEGFID-LIQKGYQVELIDG- 154
Cdd:cd06451 39 EGLRYVFQTENGLTFLlSGSGTGAMEAALSNLLE------PGDKVLVGVNGVFG------DRWADmAERYGADVDVVEKp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 155 ------VEDLSRALEK-DVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTYK 227
Cdd:cd06451 107 wgeavsPEEIAEALEQhDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQK 186
|
....*..
gi 1661071830 228 YLNGGPG 234
Cdd:cd06451 187 ALGAPPG 193
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
79-255 |
6.88e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 44.65 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 79 KVAKLIGAEQGEVVISDSTTLNLFKVLSAAVKIQADKFP-------EHKIIVAEKDAfptdiyiiegfidLIQKGYQVEL 151
Cdd:PLN02651 51 QVAALIGADPKEIIFTSGATESNNLAIKGVMHFYKDKKKhvittqtEHKCVLDSCRH-------------LQQEGFEVTY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 152 I----DGV---EDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGC 224
Cdd:PLN02651 118 LpvksDGLvdlDELAAAIRPDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSIS 197
|
170 180 190
....*....|....*....|....*....|.
gi 1661071830 225 TYKYlnGGPGSPALLWVNEKHRDQFWQPLSG 255
Cdd:PLN02651 198 GHKI--YGPKGVGALYVRRRPRVRLEPLMSG 226
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
78-316 |
8.20e-05 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 44.55 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 78 DKVAKLIGAEQG-EVVISDSTT--LNLFkVLSAAVKIQA-DKF----PEH----------------KIIVAEKDAfptdi 133
Cdd:pfam00266 50 EKVAEFINAPSNdEIIFTSGTTeaINLV-ALSLGRSLKPgDEIviteMEHhanlvpwqelakrtgaRVRVLPLDE----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 134 yiiEGFIDLiqkgyqvelidgvEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHL 213
Cdd:pfam00266 124 ---DGLLDL-------------DELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 214 NQTDSDFAIGCTYKYLngGPGSPALLWVNEKHRDQFWQPLSGwwSHKKPFDMAQHYEPANSIRRYLCGTQPVISMSLIEC 293
Cdd:pfam00266 188 QKLGVDFLAFSGHKLY--GPTGIGVLYGRRDLLEKMPPLLGG--GGMIETVSLQESTFADAPWKFEAGTPNIAGIIGLGA 263
|
250 260
....*....|....*....|...
gi 1661071830 294 GVDIFLHADMQKIREKSLKLTDL 316
Cdd:pfam00266 264 ALEYLSEIGLEAIEKHEHELAQY 286
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
78-240 |
1.34e-04 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 43.97 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 78 DKVAKLIGAEQ-GEVVISDSTT--LNLFK--------------VLSAAvkiqadkfpEHKI------IVAEKDAfptdiy 134
Cdd:PLN02855 83 KKVAAFINASTsREIVFTRNATeaINLVAytwglanlkpgdevILSVA---------EHHSnivpwqLVAQKTG------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 135 IIEGFIDLIQKgyqvELIDgVEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLN 214
Cdd:PLN02855 148 AVLKFVGLTPD----EVLD-VEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQ 222
|
170 180
....*....|....*....|....*.
gi 1661071830 215 QTDSDFAIGCTYKYLngGPGSPALLW 240
Cdd:PLN02855 223 TLGADFLVASSHKMC--GPTGIGFLW 246
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
140-213 |
1.40e-03 |
|
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440172 [Multi-domain] Cd Length: 442 Bit Score: 40.78 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1661071830 140 IDLIQKGYQVELIDgVEDLSRALEKDVAVVVLSHVNYrTGYFYDMATINEQIHSKDALVIwdlchsVGAVPMHL 213
Cdd:COG0403 181 IEVVEVPDEDGVTD-LEALKALLDDDVAGVLVQYPNF-FGVIEDLRAIAEAAHAAGALVI------VAADPLSL 246
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
155-227 |
3.42e-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: 39.30 E-value: 3.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1661071830 155 VEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTYK 227
Cdd:cd06452 129 IEEVKDEFGKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHK 201
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
30-219 |
3.48e-03 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 39.33 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 30 IYLDGNSLGARPKKSLAVAQHIISQEWGedliNSWNKADWWGLPTRL----GDKVAKLI-GAEQGEVVISDSTTLNLFKV 104
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFG----NESSLHDIGGTASSLlqvcRKTFAEMIgGEEQGIYFTSGGTESNYLAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 105 LSAAVKIQADKfpEHKIIVAEKDAfptDIYIIegFIDLIQKGYQVELID-------GVEDLSRALEKDVAVVVLSHVNYR 177
Cdd:PRK02948 78 QSLLNALPQNK--KHIITTPMEHA---SIHSY--FQSLESQGYTVTEIPvdksgliRLVDLERAITPDTVLASIQHANSE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1661071830 178 TGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSD 219
Cdd:PRK02948 151 IGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGID 192
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
140-199 |
8.24e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 38.20 E-value: 8.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 140 IDLIQKGYQVELIDgVEDLSRALEKDVAVVVLSHVNYRtGYFYDMATINEQIHSKDALVI 199
Cdd:PRK00451 180 IEVVEVPYEDGVTD-LEALEAAVDDDTAAVVVQYPNFF-GVIEDLEEIAEIAHAGGALFI 237
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
151-236 |
8.72e-03 |
|
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: 36.98 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1661071830 151 LIDGVEDLSRALEKDVAVVVLSHVNYRTGYFYDMATINEQIHSKDALVIWDLCHSVGAVPMHLNQTDSDFAIGCTY---K 227
Cdd:cd01494 78 GLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFslhK 157
|
....*....
gi 1661071830 228 YLNGGPGSP 236
Cdd:cd01494 158 NLGGEGGGV 166
|
|
| |
