|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
1-365 |
0e+00 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 631.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 1 MTNNNYLLLTPGPLTTSKTVKEAMLFDSCTWDDDYNLgVVQNIRQQLVALATDKKGYSSVLLQGSGSYAVEAVLGSAIGP 80
Cdd:PRK13479 1 MTENDPLLLTPGPLTTSRTVREAMLRDWGSWDDDFNA-LTASVRAKLVAIATGEEGYTCVPLQGSGTFSVEAAIGSLVPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 81 KEKILIISNGAYGARMAEMVQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPITHIAMVHCETTTGILNPIEKVAKLAKQ 160
Cdd:PRK13479 80 DGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETTTGILNPLDEIAAVAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 161 YQKRYIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGRSRSLSLDLYAQWRCMEDfQGKW 240
Cdd:PRK13479 160 HGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKGNSRSLSLDLYDQWAYMEK-TGQW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 241 RFTSPTHTVLAFAQALKELAQEGGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPNSPDYQFKQFYQN 320
Cdd:PRK13479 239 RFTPPTHVVAAFYQALLELEEEGGVPARGARYANNQRTLVAGMRALGFEPLLDAEIQSPIIVTFHAPADPAYDFKEFYER 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1327839759 321 LKSQGFVIYPGKVSQSDCFRIGNIGEVYEKDIDALLVAIEKAIYW 365
Cdd:PRK13479 319 LKEQGFVIYPGKLTQVDTFRIGCIGDVDAADIRRLVAAIAEALYW 363
|
|
| transamin_PhnW |
TIGR02326 |
2-aminoethylphosphonate--pyruvate transaminase; Members of this family are ... |
4-365 |
0e+00 |
|
2-aminoethylphosphonate--pyruvate transaminase; Members of this family are 2-aminoethylphosphonate--pyruvate transaminase. This enzyme acts on the most common type of naturally occurring phosphonate. It interconverts 2-aminoethylphosphonate plus pyruvate with 2-phosphonoacetaldehyde plus alanine. The enzyme phosphonoacetaldehyde hydrolase (EC 3.11.1.1), usually encoded by an adjacent gene, then cleaves the C-P bond of phosphonoacetaldehyde, adding water to yield acetaldehyde plus inorganic phosphate. Species with this pathway generally have an identified phosphonate ABC transporter but do not also have the multisubunit C-P lysase complex as found in Escherichia coli. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 131379 [Multi-domain] Cd Length: 363 Bit Score: 612.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 4 NNYLLLTPGPLTTSKTVKEAMLFDSCTWDDDYNLgVVQNIRQQLVALATDKKGYSSVLLQGSGSYAVEAVLGSAIGPKEK 83
Cdd:TIGR02326 2 RNYLLLTPGPLTTSRTVKEAMLFDWCTWDSDYNI-VVEQIRQQLLALATAEEGYTSVLLQGSGTFAVEAVIGSAVPKDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 84 ILIISNGAYGARMAEMVQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPITHIAMVHCETTTGILNPIEKVAKLAKQYQK 163
Cdd:TIGR02326 81 LLVVINGAYGARIVQIAEYLGIPHHVVDTGEVEPPDVVEVEAILAADPAITHIALVHCETTTGILNPIEAVAKLAHRHGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 164 RYIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGRSRSLSLDLYAQWRCMEDFQGKWRFT 243
Cdd:TIGR02326 161 VTIVDAMSSFGGIPIDIAELHIDYLISSANKCIQGVPGFGFVIARQAELAACKGNARSLSLDLYDQWRCMEDNHGKWRFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 244 SPTHTVLAFAQALKELAQEGGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPNSPDYQFKQFYQNLKS 323
Cdd:TIGR02326 241 SPTHVVHAFAQALLELEKEGGVAARHQRYQQNQKTLVAGMRALGFEPLLDDEIQSPIITSFYSPEDPDYRFADFYQRLKE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1327839759 324 QGFVIYPGKVSQSDCFRIGNIGEVYEKDIDALLVAIEKAIYW 365
Cdd:TIGR02326 321 QGFVIYPGKVSQVDCFRIGNIGEVDAADITRLLTAIGKAMYW 362
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
6-363 |
1.68e-124 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 363.26 E-value: 1.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 6 YLLLTPGPLTTSKTVKEAM-LFDSCTWDDDYNlGVVQNIRQQLVALA-TDKKgysSVLLQGSGSYAVEAVLGSAIGPKEK 83
Cdd:COG0075 1 RLLLTPGPTPVPPRVLRAMaRPMIGHRDPEFV-ELMDEVRELLKKVFgTEND---VVILTGSGTGAMEAALANLVSPGDK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 84 ILIISNGAYGARMAEMVQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPITHIAMVHCETTTGILNPIEKVAKLAKQYQK 163
Cdd:COG0075 77 VLVLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIGALAKEHGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 164 RYIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGR-SRSLSLDLYAQWRCMEDfqGKWRF 242
Cdd:COG0075 157 LLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARkLPSYYLDLKLWLKYWEK--GQTPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 243 TSPTHTVLAFAQALKELAQEgGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPNSPDyqFKQFYQNLK 322
Cdd:COG0075 235 TPPVSLLYALREALDLILEE-GLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVD--AAALRKRLK 311
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1327839759 323 SQ-GFVIYPGKVS-QSDCFRIGNIGEVYEKDIDALLVAIEKAI 363
Cdd:COG0075 312 ERyGIEIAGGLGPlKGKIFRIGHMGYVNPEDVLRTLAALEEAL 354
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
7-363 |
5.34e-52 |
|
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: 176.33 E-value: 5.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 7 LLLTPGPLTTSKTVKEAMLFDSCTWDDDYNLGVVQNIRQQLVALATDKKgYSSVLLQGSGSYAVEAVLGSAIGPKEKILI 86
Cdd:cd06451 1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTEN-GLTFLLSGSGTGAMEAALSNLLEPGDKVLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 87 ISNGAYGARMAEMVQ--GLGISHCIYDCGEVSLPDLQQIEQIlqqDNPITHIAMVHCETTTGILNPIEKVAKLAKQYQKR 164
Cdd:cd06451 80 GVNGVFGDRWADMAEryGADVDVVEKPWGEAVSPEEIAEALE---QHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 165 YIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGRSRSLS--LDLYAQWrcmeDFQGK--- 239
Cdd:cd06451 157 LIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKGfyFDLLLLL----KYWGEgys 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 240 WRFTSPTHTVLAFAQALKELAQEgGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPnsPDYQFKQFYQ 319
Cdd:cd06451 233 YPHTPPVNLLYALREALDLILEE-GLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVP--EGVDGDEVVR 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1327839759 320 NLKSQ-GFVIYPG------KVsqsdcFRIGNIGEVYEKDIDALLVAIEKAI 363
Cdd:cd06451 310 RLMKRyNIEIAGGlgptagKV-----FRIGHMGEATREDVLGVLSALEEAL 355
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
136-302 |
5.87e-13 |
|
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: 69.20 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 136 IAMVHCETTTGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANKcIQGVPGFAFVIARTEALERC 215
Cdd:pfam00266 143 VAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 216 K------GRSRSLSLDLYAqwrcmedFQGK-WRF---TSPTHTVLAFAQALKELaQEGGVAARFQRYQGNQYKLVSGMRK 285
Cdd:pfam00266 222 PpllgggGMIETVSLQEST-------FADApWKFeagTPNIAGIIGLGAALEYL-SEIGLEAIEKHEHELAQYLYERLLS 293
|
170
....*....|....*..
gi 1327839759 286 LGFTTLLEDSLHSPIIT 302
Cdd:pfam00266 294 LPGIRLYGPERRASIIS 310
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
1-365 |
0e+00 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 631.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 1 MTNNNYLLLTPGPLTTSKTVKEAMLFDSCTWDDDYNLgVVQNIRQQLVALATDKKGYSSVLLQGSGSYAVEAVLGSAIGP 80
Cdd:PRK13479 1 MTENDPLLLTPGPLTTSRTVREAMLRDWGSWDDDFNA-LTASVRAKLVAIATGEEGYTCVPLQGSGTFSVEAAIGSLVPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 81 KEKILIISNGAYGARMAEMVQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPITHIAMVHCETTTGILNPIEKVAKLAKQ 160
Cdd:PRK13479 80 DGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETTTGILNPLDEIAAVAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 161 YQKRYIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGRSRSLSLDLYAQWRCMEDfQGKW 240
Cdd:PRK13479 160 HGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKGNSRSLSLDLYDQWAYMEK-TGQW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 241 RFTSPTHTVLAFAQALKELAQEGGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPNSPDYQFKQFYQN 320
Cdd:PRK13479 239 RFTPPTHVVAAFYQALLELEEEGGVPARGARYANNQRTLVAGMRALGFEPLLDAEIQSPIIVTFHAPADPAYDFKEFYER 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1327839759 321 LKSQGFVIYPGKVSQSDCFRIGNIGEVYEKDIDALLVAIEKAIYW 365
Cdd:PRK13479 319 LKEQGFVIYPGKLTQVDTFRIGCIGDVDAADIRRLVAAIAEALYW 363
|
|
| transamin_PhnW |
TIGR02326 |
2-aminoethylphosphonate--pyruvate transaminase; Members of this family are ... |
4-365 |
0e+00 |
|
2-aminoethylphosphonate--pyruvate transaminase; Members of this family are 2-aminoethylphosphonate--pyruvate transaminase. This enzyme acts on the most common type of naturally occurring phosphonate. It interconverts 2-aminoethylphosphonate plus pyruvate with 2-phosphonoacetaldehyde plus alanine. The enzyme phosphonoacetaldehyde hydrolase (EC 3.11.1.1), usually encoded by an adjacent gene, then cleaves the C-P bond of phosphonoacetaldehyde, adding water to yield acetaldehyde plus inorganic phosphate. Species with this pathway generally have an identified phosphonate ABC transporter but do not also have the multisubunit C-P lysase complex as found in Escherichia coli. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 131379 [Multi-domain] Cd Length: 363 Bit Score: 612.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 4 NNYLLLTPGPLTTSKTVKEAMLFDSCTWDDDYNLgVVQNIRQQLVALATDKKGYSSVLLQGSGSYAVEAVLGSAIGPKEK 83
Cdd:TIGR02326 2 RNYLLLTPGPLTTSRTVKEAMLFDWCTWDSDYNI-VVEQIRQQLLALATAEEGYTSVLLQGSGTFAVEAVIGSAVPKDGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 84 ILIISNGAYGARMAEMVQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPITHIAMVHCETTTGILNPIEKVAKLAKQYQK 163
Cdd:TIGR02326 81 LLVVINGAYGARIVQIAEYLGIPHHVVDTGEVEPPDVVEVEAILAADPAITHIALVHCETTTGILNPIEAVAKLAHRHGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 164 RYIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGRSRSLSLDLYAQWRCMEDFQGKWRFT 243
Cdd:TIGR02326 161 VTIVDAMSSFGGIPIDIAELHIDYLISSANKCIQGVPGFGFVIARQAELAACKGNARSLSLDLYDQWRCMEDNHGKWRFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 244 SPTHTVLAFAQALKELAQEGGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPNSPDYQFKQFYQNLKS 323
Cdd:TIGR02326 241 SPTHVVHAFAQALLELEKEGGVAARHQRYQQNQKTLVAGMRALGFEPLLDDEIQSPIITSFYSPEDPDYRFADFYQRLKE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1327839759 324 QGFVIYPGKVSQSDCFRIGNIGEVYEKDIDALLVAIEKAIYW 365
Cdd:TIGR02326 321 QGFVIYPGKVSQVDCFRIGNIGEVDAADITRLLTAIGKAMYW 362
|
|
| PhnW-AepZ |
TIGR03301 |
2-aminoethylphosphonate aminotransferase; This family includes a number of ... |
7-362 |
2.67e-174 |
|
2-aminoethylphosphonate aminotransferase; This family includes a number of 2-aminoethylphosphonate aminotransferases, some of which are indicated to operate in the catabolism of 2-aminoethylphosphonate (AEP) and others which are involved in the biosynthesis of the same compound. The catabolic enzyme (PhnW) is known to use pyruvate:alanine as the transfer partner and is modeled by the equivalog-level model (TIGR02326). The PhnW family is apparently a branch of a larger tree including genes (AepZ) adjacent to others responsible for the biosynthesis of phosphonoacetaldehyde. The identity of the transfer partner is unknown for these enzymes and considering the reversed flux compared to PhnW, it may very well be different.
Pssm-ID: 274512 [Multi-domain] Cd Length: 355 Bit Score: 488.81 E-value: 2.67e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 7 LLLTPGPLTTSKTVKEAMLFDSCTWDDDYNlGVVQNIRQQLVALATDKKGYSSVLLQGSGSYAVEAVLGSAIGPKEKILI 86
Cdd:TIGR03301 1 ILLTPGPLSTSATVRDAMLVDWCHWDSEFN-DVTDQVRDRLLALAGGDDNHTCVLLQGSGTFAVEATIGSLVPRDGKLLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 87 ISNGAYGARMAEMVQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPITHIAMVHCETTTGILNPIEKVAKLAKQYQKRYI 166
Cdd:TIGR03301 80 LINGAYGERLAKICEYLGIPHTDLNFSEYEPPDLNRIEEALAADPDITHVATVHHETTTGILNPLEAIAKVARSHGAVLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 167 VDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGRSRSLSLDLYAQWRCMEDfQGKWRFTSPT 246
Cdd:TIGR03301 160 VDAMSSFGAIPIDIEELDVDALIASANKCLEGVPGFGFVIARRDLLEASAGNARSLYLDLYDQWAYMEK-TGKWRFTPPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 247 HTVLAFAQALKELAQEGGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPNSPDYQFKQFYQNLKSQGF 326
Cdd:TIGR03301 239 HTVYAFAQALEELEAEGGVPARIARYRRNRELLVDGLRALGFQPLLPERWQSPIIVSFLYPDDPDFDFDDFYQELKERGF 318
|
330 340 350
....*....|....*....|....*....|....*.
gi 1327839759 327 VIYPGKVSQSDCFRIGNIGEVYEKDIDALLVAIEKA 362
Cdd:TIGR03301 319 VIYPGKLTLADTFRIGTIGEIDAADIERLLEAIKDA 354
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
6-363 |
1.68e-124 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 363.26 E-value: 1.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 6 YLLLTPGPLTTSKTVKEAM-LFDSCTWDDDYNlGVVQNIRQQLVALA-TDKKgysSVLLQGSGSYAVEAVLGSAIGPKEK 83
Cdd:COG0075 1 RLLLTPGPTPVPPRVLRAMaRPMIGHRDPEFV-ELMDEVRELLKKVFgTEND---VVILTGSGTGAMEAALANLVSPGDK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 84 ILIISNGAYGARMAEMVQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPITHIAMVHCETTTGILNPIEKVAKLAKQYQK 163
Cdd:COG0075 77 VLVLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIGALAKEHGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 164 RYIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGR-SRSLSLDLYAQWRCMEDfqGKWRF 242
Cdd:COG0075 157 LLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARkLPSYYLDLKLWLKYWEK--GQTPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 243 TSPTHTVLAFAQALKELAQEgGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPNSPDyqFKQFYQNLK 322
Cdd:COG0075 235 TPPVSLLYALREALDLILEE-GLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVD--AAALRKRLK 311
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1327839759 323 SQ-GFVIYPGKVS-QSDCFRIGNIGEVYEKDIDALLVAIEKAI 363
Cdd:COG0075 312 ERyGIEIAGGLGPlKGKIFRIGHMGYVNPEDVLRTLAALEEAL 354
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
7-363 |
5.34e-52 |
|
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: 176.33 E-value: 5.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 7 LLLTPGPLTTSKTVKEAMLFDSCTWDDDYNLGVVQNIRQQLVALATDKKgYSSVLLQGSGSYAVEAVLGSAIGPKEKILI 86
Cdd:cd06451 1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTEN-GLTFLLSGSGTGAMEAALSNLLEPGDKVLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 87 ISNGAYGARMAEMVQ--GLGISHCIYDCGEVSLPDLQQIEQIlqqDNPITHIAMVHCETTTGILNPIEKVAKLAKQYQKR 164
Cdd:cd06451 80 GVNGVFGDRWADMAEryGADVDVVEKPWGEAVSPEEIAEALE---QHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 165 YIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIARTEALERCKGRSRSLS--LDLYAQWrcmeDFQGK--- 239
Cdd:cd06451 157 LIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKGfyFDLLLLL----KYWGEgys 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 240 WRFTSPTHTVLAFAQALKELAQEgGVAARFQRYQGNQYKLVSGMRKLGFTTLLEDSLHSPIITAFYSPnsPDYQFKQFYQ 319
Cdd:cd06451 233 YPHTPPVNLLYALREALDLILEE-GLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVP--EGVDGDEVVR 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1327839759 320 NLKSQ-GFVIYPG------KVsqsdcFRIGNIGEVYEKDIDALLVAIEKAI 363
Cdd:cd06451 310 RLMKRyNIEIAGGlgptagKV-----FRIGHMGEATREDVLGVLSALEEAL 355
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
54-360 |
1.18e-17 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 83.65 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 54 KKGYSsVLLQGSGSYAVEAVLGSAIGPKEKILIISNGAYGARMAEMVQGLGISHCIYDC--GEVSLPDLQQIEQILQQDN 131
Cdd:PLN02409 58 KSGTP-FIFPTTGTGAWESALTNTLSPGDKVVSFRIGQFSLLWIDQMQRLNFDVDVVESpwGQGADLDILKSKLRQDTNH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 132 PITHIAMVHCETTTGILNPIEKVAKLAKQYQKR--YIVDAMSSFGGVPMDIAELNIDFLISSANKCIQGVPGFAFVIART 209
Cdd:PLN02409 137 KIKAVCVVHNETSTGVTNDLAGVRKLLDCAQHPalLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 210 EALERCKgrsRSLSLDLYAQWRCMEDFQ---GKWRFTSPTHTVLAFAQALKeLAQEGGVAARFQRYQGNQYKLVSGMRKL 286
Cdd:PLN02409 217 KALEASK---TAKSPRVFFDWADYLKFYklgTYWPYTPSIQLLYGLRAALD-LIFEEGLENVIARHARLGEATRLAVEAW 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 287 GFTTLLE-DSLHSPIITAFYSPNSPDYQ--FKQFYQ--NLkSQGFVIYP--GKVsqsdcFRIGNIGEVYEKDIDALLVAI 359
Cdd:PLN02409 293 GLKLCTKkPEWRSDTVTAVVVPEGIDSAeiVKNAWKkyNL-SLGLGLNKvaGKV-----FRIGHLGNVNELQLLGALAGV 366
|
.
gi 1327839759 360 E 360
Cdd:PLN02409 367 E 367
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
136-302 |
5.87e-13 |
|
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: 69.20 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 136 IAMVHCETTTGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANKcIQGVPGFAFVIARTEALERC 215
Cdd:pfam00266 143 VAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 216 K------GRSRSLSLDLYAqwrcmedFQGK-WRF---TSPTHTVLAFAQALKELaQEGGVAARFQRYQGNQYKLVSGMRK 285
Cdd:pfam00266 222 PpllgggGMIETVSLQEST-------FADApWKFeagTPNIAGIIGLGAALEYL-SEIGLEAIEKHEHELAQYLYERLLS 293
|
170
....*....|....*..
gi 1327839759 286 LGFTTLLEDSLHSPIIT 302
Cdd:pfam00266 294 LPGIRLYGPERRASIIS 310
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
136-302 |
4.07e-12 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 66.70 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 136 IAMVHCETTTGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANKcIQGVPGFAFVIARTEALERC 215
Cdd:COG0520 158 VAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGKRELLEAL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 216 K-----GRSrslsldlyAQWRCMEDFQGK---WRF---TSPTHTVLAFAQALkELAQEGGVAARFQRYQGNQYKLVSGMR 284
Cdd:COG0520 237 PpflggGGM--------IEWVSFDGTTYAdlpRRFeagTPNIAGAIGLGAAI-DYLEAIGMEAIEARERELTAYALEGLA 307
|
170 180
....*....|....*....|.
gi 1327839759 285 KLGFTTLL---EDSLHSPIIT 302
Cdd:COG0520 308 AIPGVRILgpaDPEDRSGIVS 328
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
136-214 |
8.03e-10 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 59.79 E-value: 8.03e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327839759 136 IAMVHCETTTGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANKcIQGVPGFAFVIARTEALER 214
Cdd:cd06453 143 VAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHK-MLGPTGIGVLYGKEELLEE 220
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
145-285 |
4.43e-08 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 54.28 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 145 TGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANKcI---QGVpGFAFVIART--EAL------E 213
Cdd:COG1104 153 TGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHK-IygpKGV-GALYVRKGVrlEPLihgggqE 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327839759 214 RckGRsRSlsldlyaqwrcmedfqGkwrfTSPTHTVLAFAQALKELAQEggVAARFQRYQGNQYKLVSGMRK 285
Cdd:COG1104 231 R--GL-RS----------------G----TENVPGIVGLGKAAELAAEE--LEEEAARLRALRDRLEEGLLA 277
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
136-213 |
2.81e-07 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 52.06 E-value: 2.81e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327839759 136 IAMVHCETTTGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANK-CiqGVPGFAFVIARTEALE 213
Cdd:PLN02855 177 VATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKmC--GPTGIGFLWGKSDLLE 253
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
60-201 |
1.89e-06 |
|
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: 47.38 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 60 VLLQGSGSYAVEAVLGSAIGPKEKILIISNGAYG--ARMAEMvQGLGISHCIYDCGEVSLPDLQQIEQILQQDNPIThIA 137
Cdd:cd01494 20 AVFVPSGTGANEAALLALLGPGDEVIVDANGHGSryWVAAEL-AGAKPVPVPVDDAGYGGLDVAILEELKAKPNVAL-IV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327839759 138 MVHCETTTGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVP---MDIAELNIDFLISSANKCIQGVPG 201
Cdd:cd01494 98 ITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFSLHKNLGGEGG 164
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
140-194 |
1.33e-04 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 43.56 E-value: 1.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1327839759 140 HCETTTGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANK 194
Cdd:PRK02948 146 HANSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHK 200
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
136-194 |
2.25e-04 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 43.01 E-value: 2.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327839759 136 IAMVHCETttGILNPIEKVAKLAKQYQKRYIVDAMSSFGGVPMDIAELNIDFLISSANK 194
Cdd:PRK14012 150 IMHVNNEI--GVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHK 206
|
|
| PRK03080 |
PRK03080 |
phosphoserine transaminase; |
56-214 |
8.73e-03 |
|
phosphoserine transaminase;
Pssm-ID: 235103 Cd Length: 378 Bit Score: 37.86 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 56 GYSSVLLQGSGSYAVEAVLGSAIGPKeKILIISNGAYGARMAEMVQG---LGISHCI-YDCGEvsLPDLQQIeqilqqdN 131
Cdd:PRK03080 66 GYEVGIVPGSDTGAWEMALWSLLGAR-RVDHLAWESFGSKWATDVVKqlkLEDPRVLeADYGS--LPDLSAV-------D 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839759 132 PITHIAMVHCETTTGILNPIEKVAK-----LAkqyqkryIVDAMSSFGGVPMDIAELniDFLISSANKCIQGVPGFAFVI 206
Cdd:PRK03080 136 FDRDVVFTWNGTTTGVRVPVARWIGadregLT-------ICDATSAAFALPLDWSKL--DVYTFSWQKVLGGEGGHGMAI 206
|
....*...
gi 1327839759 207 ARTEALER 214
Cdd:PRK03080 207 LSPRAVER 214
|
|
| |
