|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
1-366 |
0e+00 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 671.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 1 MTSRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNLgVVQVIRQRLVELATPANGYTSVLLQGSGSYAVEAVLGSAIGA 80
Cdd:PRK13479 1 MTENDPLLLTPGPLTTSRTVREAMLRDWGSWDDDFNA-LTASVRAKLVAIATGEEGYTCVPLQGSGTFSVEAAIGSLVPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 81 QGKVLIISNGAYGARMIEMAKLMCIAHHPYDCGEVARPDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKR 160
Cdd:PRK13479 80 DGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETTTGILNPLDEIAAVAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 161 YDKRYIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVIAREAELANCQGRSRSLSLDLYAQWRCMEDNhGKW 240
Cdd:PRK13479 160 HGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKGNSRSLSLDLYDQWAYMEKT-GQW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 241 RFTSPTHTVLAFAQALKELAEEGGVRARHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIITAFYSPDAPQYRFKDFYQR 320
Cdd:PRK13479 239 RFTPPTHVVAAFYQALLELEEEGGVPARGARYANNQRTLVAGMRALGFEPLLDAEIQSPIIVTFHAPADPAYDFKEFYER 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 503993316 321 LKEQGFVIYPGKVSQSDCFRIGNIGEVYDADITALLAAIKNAMYWQ 366
Cdd:PRK13479 319 LKEQGFVIYPGKLTQVDTFRIGCIGDVDAADIRRLVAAIAEALYWM 364
|
|
| transamin_PhnW |
TIGR02326 |
2-aminoethylphosphonate--pyruvate transaminase; Members of this family are ... |
3-366 |
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: 664.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 3 SRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNLgVVQVIRQRLVELATPANGYTSVLLQGSGSYAVEAVLGSAIGAQG 82
Cdd:TIGR02326 1 ERNYLLLTPGPLTTSRTVKEAMLFDWCTWDSDYNI-VVEQIRQQLLALATAEEGYTSVLLQGSGTFAVEAVIGSAVPKDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 83 KVLIISNGAYGARMIEMAKLMCIAHHPYDCGEVARPDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYD 162
Cdd:TIGR02326 80 KLLVVINGAYGARIVQIAEYLGIPHHVVDTGEVEPPDVVEVEAILAADPAITHIALVHCETTTGILNPIEAVAKLAHRHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 163 KRYIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVIAREAELANCQGRSRSLSLDLYAQWRCMEDNHGKWRF 242
Cdd:TIGR02326 160 KVTIVDAMSSFGGIPIDIAELHIDYLISSANKCIQGVPGFGFVIARQAELAACKGNARSLSLDLYDQWRCMEDNHGKWRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 243 TSPTHTVLAFAQALKELAEEGGVRARHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIITAFYSPDAPQYRFKDFYQRLK 322
Cdd:TIGR02326 240 TSPTHVVHAFAQALLELEKEGGVAARHQRYQQNQKTLVAGMRALGFEPLLDDEIQSPIITSFYSPEDPDYRFADFYQRLK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503993316 323 EQGFVIYPGKVSQSDCFRIGNIGEVYDADITALLAAIKNAMYWQ 366
Cdd:TIGR02326 320 EQGFVIYPGKVSQVDCFRIGNIGEVDAADITRLLTAIGKAMYWT 363
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
6-363 |
2.86e-132 |
|
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: 382.90 E-value: 2.86e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 6 YLLLTPGPLTTSRTVKEAM-LFDSCTWDDDYNlGVVQVIRQRLVELATPANgyTSVLLQGSGSYAVEAVLGSAIGAQGKV 84
Cdd:COG0075 1 RLLLTPGPTPVPPRVLRAMaRPMIGHRDPEFV-ELMDEVRELLKKVFGTEN--DVVILTGSGTGAMEAALANLVSPGDKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 85 LIISNGAYGARMIEMAKLMCIAHHPYDCGEVARPDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYDKR 164
Cdd:COG0075 78 LVLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIGALAKEHGAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 165 YIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVIAREAELANCQGR-SRSLSLDLYAQWRCMEDnhGKWRFT 243
Cdd:COG0075 158 LIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARkLPSYYLDLKLWLKYWEK--GQTPYT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 244 SPTHTVLAFAQALKELAEEgGVRARHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIITAFYSPDApqYRFKDFYQRLKE 323
Cdd:COG0075 236 PPVSLLYALREALDLILEE-GLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEG--VDAAALRKRLKE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 503993316 324 Q-GFVIYPGKVS-QSDCFRIGNIGEVYDADITALLAAIKNAM 363
Cdd:COG0075 313 RyGIEIAGGLGPlKGKIFRIGHMGYVNPEDVLRTLAALEEAL 354
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
7-362 |
1.06e-55 |
|
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: 185.96 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 7 LLLTPGPLTTSRTVKEAMLFDSCTWDDDYNLGVVQVIRQRLVELATPANGYTsVLLQGSGSYAVEAVLGSAIGAQGKVLI 86
Cdd:cd06451 1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLT-FLLSGSGTGAMEAALSNLLEPGDKVLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 87 ISNGAYGARMIEMAKLMCIAHHPY--DCGEVARPDAaaIERILqTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYDKR 164
Cdd:cd06451 80 GVNGVFGDRWADMAERYGADVDVVekPWGEAVSPEE--IAEAL-EQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 165 YIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVI----AREAELANCQGRSRSLSLDLYAQ-WRCmednHGK 239
Cdd:cd06451 157 LIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAfserALERIKKKTKPKGFYFDLLLLLKyWGE----GYS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 240 WRFTSPTHTVLAFAQALKELAEEG--GVRARHQRYStnqQRLVAGMRALGFQPLLDDSLHSPIITAFYSPdaPQYRFKDF 317
Cdd:cd06451 233 YPHTPPVNLLYALREALDLILEEGleNRWARHRRLA---KALREGLEALGLKLLAKPELRSPTVTAVLVP--EGVDGDEV 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 503993316 318 YQRLKEQ-GFVIYPG------KVsqsdcFRIGNIGEVYDADITALLAAIKNA 362
Cdd:cd06451 308 VRRLMKRyNIEIAGGlgptagKV-----FRIGHMGEATREDVLGVLSALEEA 354
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
117-302 |
2.01e-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: 70.74 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 117 RPDAAAIERILQTDPAITHIAmvHSETTTGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANKcI 196
Cdd:pfam00266 126 LLDLDELEKLITPKTKLVAIT--HVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-L 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 197 QGVPGFAFVIAREAELANCQ------GRSRSLSLDLYAQwrcmedNHGKWRF---TSPTHTVLAFAQALKELaEEGGVRA 267
Cdd:pfam00266 203 YGPTGIGVLYGRRDLLEKMPpllgggGMIETVSLQESTF------ADAPWKFeagTPNIAGIIGLGAALEYL-SEIGLEA 275
|
170 180 190
....*....|....*....|....*....|....*
gi 503993316 268 RHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIIT 302
Cdd:pfam00266 276 IEKHEHELAQYLYERLLSLPGIRLYGPERRASIIS 310
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
1-366 |
0e+00 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 671.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 1 MTSRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNLgVVQVIRQRLVELATPANGYTSVLLQGSGSYAVEAVLGSAIGA 80
Cdd:PRK13479 1 MTENDPLLLTPGPLTTSRTVREAMLRDWGSWDDDFNA-LTASVRAKLVAIATGEEGYTCVPLQGSGTFSVEAAIGSLVPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 81 QGKVLIISNGAYGARMIEMAKLMCIAHHPYDCGEVARPDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKR 160
Cdd:PRK13479 80 DGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETTTGILNPLDEIAAVAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 161 YDKRYIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVIAREAELANCQGRSRSLSLDLYAQWRCMEDNhGKW 240
Cdd:PRK13479 160 HGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKGNSRSLSLDLYDQWAYMEKT-GQW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 241 RFTSPTHTVLAFAQALKELAEEGGVRARHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIITAFYSPDAPQYRFKDFYQR 320
Cdd:PRK13479 239 RFTPPTHVVAAFYQALLELEEEGGVPARGARYANNQRTLVAGMRALGFEPLLDAEIQSPIIVTFHAPADPAYDFKEFYER 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 503993316 321 LKEQGFVIYPGKVSQSDCFRIGNIGEVYDADITALLAAIKNAMYWQ 366
Cdd:PRK13479 319 LKEQGFVIYPGKLTQVDTFRIGCIGDVDAADIRRLVAAIAEALYWM 364
|
|
| transamin_PhnW |
TIGR02326 |
2-aminoethylphosphonate--pyruvate transaminase; Members of this family are ... |
3-366 |
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: 664.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 3 SRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNLgVVQVIRQRLVELATPANGYTSVLLQGSGSYAVEAVLGSAIGAQG 82
Cdd:TIGR02326 1 ERNYLLLTPGPLTTSRTVKEAMLFDWCTWDSDYNI-VVEQIRQQLLALATAEEGYTSVLLQGSGTFAVEAVIGSAVPKDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 83 KVLIISNGAYGARMIEMAKLMCIAHHPYDCGEVARPDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYD 162
Cdd:TIGR02326 80 KLLVVINGAYGARIVQIAEYLGIPHHVVDTGEVEPPDVVEVEAILAADPAITHIALVHCETTTGILNPIEAVAKLAHRHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 163 KRYIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVIAREAELANCQGRSRSLSLDLYAQWRCMEDNHGKWRF 242
Cdd:TIGR02326 160 KVTIVDAMSSFGGIPIDIAELHIDYLISSANKCIQGVPGFGFVIARQAELAACKGNARSLSLDLYDQWRCMEDNHGKWRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 243 TSPTHTVLAFAQALKELAEEGGVRARHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIITAFYSPDAPQYRFKDFYQRLK 322
Cdd:TIGR02326 240 TSPTHVVHAFAQALLELEKEGGVAARHQRYQQNQKTLVAGMRALGFEPLLDDEIQSPIITSFYSPEDPDYRFADFYQRLK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503993316 323 EQGFVIYPGKVSQSDCFRIGNIGEVYDADITALLAAIKNAMYWQ 366
Cdd:TIGR02326 320 EQGFVIYPGKVSQVDCFRIGNIGEVDAADITRLLTAIGKAMYWT 363
|
|
| PhnW-AepZ |
TIGR03301 |
2-aminoethylphosphonate aminotransferase; This family includes a number of ... |
7-363 |
0e+00 |
|
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: 516.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 7 LLLTPGPLTTSRTVKEAMLFDSCTWDDDYNlGVVQVIRQRLVELATPANGYTSVLLQGSGSYAVEAVLGSAIGAQGKVLI 86
Cdd:TIGR03301 1 ILLTPGPLSTSATVRDAMLVDWCHWDSEFN-DVTDQVRDRLLALAGGDDNHTCVLLQGSGTFAVEATIGSLVPRDGKLLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 87 ISNGAYGARMIEMAKLMCIAHHPYDCGEVARPDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYDKRYI 166
Cdd:TIGR03301 80 LINGAYGERLAKICEYLGIPHTDLNFSEYEPPDLNRIEEALAADPDITHVATVHHETTTGILNPLEAIAKVARSHGAVLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 167 VDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVIAREAELANCQGRSRSLSLDLYAQWRCMEDNhGKWRFTSPT 246
Cdd:TIGR03301 160 VDAMSSFGAIPIDIEELDVDALIASANKCLEGVPGFGFVIARRDLLEASAGNARSLYLDLYDQWAYMEKT-GKWRFTPPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 247 HTVLAFAQALKELAEEGGVRARHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIITAFYSPDAPQYRFKDFYQRLKEQGF 326
Cdd:TIGR03301 239 HTVYAFAQALEELEAEGGVPARIARYRRNRELLVDGLRALGFQPLLPERWQSPIIVSFLYPDDPDFDFDDFYQELKERGF 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 503993316 327 VIYPGKVSQSDCFRIGNIGEVYDADITALLAAIKNAM 363
Cdd:TIGR03301 319 VIYPGKLTLADTFRIGTIGEIDAADIERLLEAIKDAL 355
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
6-363 |
2.86e-132 |
|
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: 382.90 E-value: 2.86e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 6 YLLLTPGPLTTSRTVKEAM-LFDSCTWDDDYNlGVVQVIRQRLVELATPANgyTSVLLQGSGSYAVEAVLGSAIGAQGKV 84
Cdd:COG0075 1 RLLLTPGPTPVPPRVLRAMaRPMIGHRDPEFV-ELMDEVRELLKKVFGTEN--DVVILTGSGTGAMEAALANLVSPGDKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 85 LIISNGAYGARMIEMAKLMCIAHHPYDCGEVARPDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYDKR 164
Cdd:COG0075 78 LVLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIGALAKEHGAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 165 YIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVIAREAELANCQGR-SRSLSLDLYAQWRCMEDnhGKWRFT 243
Cdd:COG0075 158 LIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARkLPSYYLDLKLWLKYWEK--GQTPYT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 244 SPTHTVLAFAQALKELAEEgGVRARHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIITAFYSPDApqYRFKDFYQRLKE 323
Cdd:COG0075 236 PPVSLLYALREALDLILEE-GLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEG--VDAAALRKRLKE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 503993316 324 Q-GFVIYPGKVS-QSDCFRIGNIGEVYDADITALLAAIKNAM 363
Cdd:COG0075 313 RyGIEIAGGLGPlKGKIFRIGHMGYVNPEDVLRTLAALEEAL 354
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
7-362 |
1.06e-55 |
|
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: 185.96 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 7 LLLTPGPLTTSRTVKEAMLFDSCTWDDDYNLGVVQVIRQRLVELATPANGYTsVLLQGSGSYAVEAVLGSAIGAQGKVLI 86
Cdd:cd06451 1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLT-FLLSGSGTGAMEAALSNLLEPGDKVLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 87 ISNGAYGARMIEMAKLMCIAHHPY--DCGEVARPDAaaIERILqTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYDKR 164
Cdd:cd06451 80 GVNGVFGDRWADMAERYGADVDVVekPWGEAVSPEE--IAEAL-EQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 165 YIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFVI----AREAELANCQGRSRSLSLDLYAQ-WRCmednHGK 239
Cdd:cd06451 157 LIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAfserALERIKKKTKPKGFYFDLLLLLKyWGE----GYS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 240 WRFTSPTHTVLAFAQALKELAEEG--GVRARHQRYStnqQRLVAGMRALGFQPLLDDSLHSPIITAFYSPdaPQYRFKDF 317
Cdd:cd06451 233 YPHTPPVNLLYALREALDLILEEGleNRWARHRRLA---KALREGLEALGLKLLAKPELRSPTVTAVLVP--EGVDGDEV 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 503993316 318 YQRLKEQ-GFVIYPG------KVsqsdcFRIGNIGEVYDADITALLAAIKNA 362
Cdd:cd06451 308 VRRLMKRyNIEIAGGlgptagKV-----FRIGHMGEATREDVLGVLSALEEA 354
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
58-307 |
3.26e-15 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 76.33 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 58 TSVLLQGSGSYAVEAVLGSAIGAQGKVLIISNGAYGARMIEMAKlmciaHHPYDCGEVARP-----DAAAIERILQTDPA 132
Cdd:PLN02409 61 TPFIFPTTGTGAWESALTNTLSPGDKVVSFRIGQFSLLWIDQMQ-----RLNFDVDVVESPwgqgaDLDILKSKLRQDTN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 133 --ITHIAMVHSETTTGMLNPIeevAALAKRYDKR-----YIVDAMSSFGGIPMDVAALNIDYLISSANKCIQGVPGFAFV 205
Cdd:PLN02409 136 hkIKAVCVVHNETSTGVTNDL---AGVRKLLDCAqhpalLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 206 IAREAELANCQgrsRSLSLDLYAQWRCMEDNH---GKWRFTSPTHTVLAFAQALKELAEEG--GVRARHQRYSTnqqRLV 280
Cdd:PLN02409 213 CASPKALEASK---TAKSPRVFFDWADYLKFYklgTYWPYTPSIQLLYGLRAALDLIFEEGleNVIARHARLGE---ATR 286
|
250 260
....*....|....*....|....*...
gi 503993316 281 AGMRALGFQPLL-DDSLHSPIITAFYSP 307
Cdd:PLN02409 287 LAVEAWGLKLCTkKPEWRSDTVTAVVVP 314
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
117-302 |
2.01e-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: 70.74 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 117 RPDAAAIERILQTDPAITHIAmvHSETTTGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANKcI 196
Cdd:pfam00266 126 LLDLDELEKLITPKTKLVAIT--HVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-L 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 197 QGVPGFAFVIAREAELANCQ------GRSRSLSLDLYAQwrcmedNHGKWRF---TSPTHTVLAFAQALKELaEEGGVRA 267
Cdd:pfam00266 203 YGPTGIGVLYGRRDLLEKMPpllgggGMIETVSLQESTF------ADAPWKFeagTPNIAGIIGLGAALEYL-SEIGLEA 275
|
170 180 190
....*....|....*....|....*....|....*
gi 503993316 268 RHQRYSTNQQRLVAGMRALGFQPLLDDSLHSPIIT 302
Cdd:pfam00266 276 IEKHEHELAQYLYERLLSLPGIRLYGPERRASIIS 310
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
117-362 |
2.95e-13 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 70.17 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 117 RPDAAAIERILQTDPAIthIAMVHSETTTGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANKcI 196
Cdd:COG0520 141 ELDLEALEALLTPRTKL--VAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-L 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 197 QGVPGFAFVIAREAELANCQ-----GRSrslsldlyAQWRCMED---NHGKWRF---TSPTHTVLAFAQALkELAEEGGV 265
Cdd:COG0520 218 YGPTGIGVLYGKRELLEALPpflggGGM--------IEWVSFDGttyADLPRRFeagTPNIAGAIGLGAAI-DYLEAIGM 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 266 RARHQRYSTNQQRLVAGMRAL-GFQPL--LDDSLHSPIITaFYSPDAPQYrfkDFYQRLKEQGFVI---------YPGKV 333
Cdd:COG0520 289 EAIEARERELTAYALEGLAAIpGVRILgpADPEDRSGIVS-FNVDGVHPH---DVAALLDDEGIAVraghhcaqpLMRRL 364
|
250 260 270
....*....|....*....|....*....|.
gi 503993316 334 SQSDCFRIgNIGeVY--DADITALLAAIKNA 362
Cdd:COG0520 365 GVPGTVRA-SFH-LYntEEEIDRLVEALKKL 393
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
119-285 |
2.57e-12 |
|
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: 67.38 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 119 DAAAIERILQTDPAITHIAMVHSETttGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANKcIQG 198
Cdd:COG1104 129 DLEALEAALRPDTALVSVMHANNET--GTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHK-IYG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 199 VPGFAFVIAREaelancqgrsrslSLDLYAQWrcmednHG-----KWRF-TSPTHTVLAFAQALKELAEEggVRARHQRY 272
Cdd:COG1104 206 PKGVGALYVRK-------------GVRLEPLI------HGggqerGLRSgTENVPGIVGLGKAAELAAEE--LEEEAARL 264
|
170
....*....|...
gi 503993316 273 STNQQRLVAGMRA 285
Cdd:COG1104 265 RALRDRLEEGLLA 277
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
119-194 |
3.56e-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: 60.94 E-value: 3.56e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503993316 119 DAAAIERILQTDPAIthIAMVHSETTTGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANK 194
Cdd:cd06453 128 DLEALEKLLTERTKL--VAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHK 201
|
|
| PLN02452 |
PLN02452 |
phosphoserine transaminase |
50-271 |
1.11e-09 |
|
phosphoserine transaminase
Pssm-ID: 178071 Cd Length: 365 Bit Score: 59.32 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 50 LATPANgYTSVLLQGSGSYAVEAVLGSAIGAQGKVLIISNGAYGARMIEMAKLMCIAHHPY---DCGEVARPDAAAIERi 126
Cdd:PLN02452 65 LDIPDN-YEVLFLQGGASTQFAAIPLNLCKPGDKADFVVTGSWSKKAAKEAKKYCKTNVIAsgkDEKYTKIPSVSEWEL- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 127 lqtDPAITHIAMVHSETTTGMlnpieEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYliSSANKCIqGVPGFAFVI 206
Cdd:PLN02452 143 ---TPDAKFVHICANETIHGV-----EFKDYPDVGNVPLVADMSSNFLSKPVDVSKYGVIY--AGAQKNV-GPSGVTIVI 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503993316 207 AREAELANCQGRSRSLsLDlyaqWRCMEDNHGKWRfTSPTHTVLAFAQALKELAEEGGVRARHQR 271
Cdd:PLN02452 212 IRKDLIGNARPITPGM-LD----YKIHAENDSLYN-TPPCFGIYMCGLVFEDLLAQGGLKAMEKR 270
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
40-177 |
5.28e-09 |
|
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: 55.08 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 40 VQVIRQRLVELATPANGYtsVLLQGSGSYAVEAVLGSAIGAQGKVLIISNGAYG--ARMIEMAKLMcIAHHPYDcGEVAR 117
Cdd:cd01494 2 LEELEEKLARLLQPGNDK--AVFVPSGTGANEAALLALLGPGDEVIVDANGHGSryWVAAELAGAK-PVPVPVD-DAGYG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 118 PDAAAIERILQTDPAITHIAMVHSETTTGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIP 177
Cdd:cd01494 78 GLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASP 137
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
61-360 |
2.50e-07 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 51.96 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 61 LLQGSGSYAVEAVLGSAIGAQGKVLIISNGAYGArMIEMAKLMCIAHHPYDCGEVAR--PDAAAIERILQTDpaiTHIAM 138
Cdd:cd00609 62 IVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPG-YEAAARLAGAEVVPVPLDEEGGflLDLELLEAAKTPK---TKLLY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 139 VHSetttgMLNP---------IEEVAALAKRYDKRYIVD---AMSSFGGIPMDVAALNIDY----LISSANKCIqGVPGF 202
Cdd:cd00609 138 LNN-----PNNPtgavlseeeLEELAELAKKHGILIISDeayAELVYDGEPPPALALLDAYerviVLRSFSKTF-GLPGL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 203 --AFVIAREAELANcqgrsrslSLDLYAQWRCmednhgkwrFTSPTHTVLAFAQALKELAEEggVRARHQRYSTNQQRLV 280
Cdd:cd00609 212 riGYLIAPPEELLE--------RLKKLLPYTT---------SGPSTLSQAAAAAALDDGEEH--LEELRERYRRRRDALL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 281 AGMRALGFqplldDSLHSPIITAFYSPDAPQYRFKDFYQR-LKEQGFVIYPGK---VSQSDCFRIgNIGEVyDADITALL 356
Cdd:cd00609 273 EALKELGP-----LVVVKPSGGFFLWLDLPEGDDEEFLERlLLEAGVVVRPGSafgEGGEGFVRL-SFATP-EEELEEAL 345
|
....
gi 503993316 357 AAIK 360
Cdd:cd00609 346 ERLA 349
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
136-194 |
2.36e-06 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 48.98 E-value: 2.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503993316 136 IAMVHSETTTGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANK 194
Cdd:PLN02855 177 VATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHK 235
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
119-194 |
4.18e-06 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 48.19 E-value: 4.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503993316 119 DAAAIERILQTDPAITHIAMVHSETttGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANK 194
Cdd:PRK02948 127 RLVDLERAITPDTVLASIQHANSEI--GTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHK 200
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
64-359 |
1.02e-05 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 46.91 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 64 GSGSYAVEAVLGSAIGAQGKVLIISNGAYGArMIEMAKLMCIAHHPYDCGEVA--RPDAAAIERILQTDPAITHIAMVHS 141
Cdd:pfam00155 69 GSGAGANIEALIFLLANPGDAILVPAPTYAS-YIRIARLAGGEVVRYPLYDSNdfHLDFDALEAALKEKPKVVLHTSPHN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 142 ETTTgMLNP--IEEVAALAKRYDKRYIVD--------AMSSFGGIPMDVAALNIDYLISSANKCIqGVPGF--AFVIARE 209
Cdd:pfam00155 148 PTGT-VATLeeLEKLLDLAKEHNILLLVDeayagfvfGSPDAVATRALLAEGPNLLVVGSFSKAF-GLAGWrvGYILGNA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 210 AELANCQGRSRslsldlyaqwrcmednhgkwRFTSPTHTVLAFAQAL-KELAEEGGVRARHQRYSTNQQRLVAGMRALGF 288
Cdd:pfam00155 226 AVISQLRKLAR--------------------PFYSSTHLQAAAAAALsDPLLVASELEEMRQRIKERRDYLRDGLQAAGL 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503993316 289 QPLLDDSlhspiitAFYS-PDAPQYRFKDFYQRLKEQGFVI-----YPGKvsqSDCFRIgNIGEVYDADITALLAAI 359
Cdd:pfam00155 286 SVLPSQA-------GFFLlTGLDPETAKELAQVLLEEVGVYvtpgsSPGV---PGWLRI-TVAGGTEEELEELLEAI 351
|
|
| PSAT_like |
cd00611 |
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ... |
37-278 |
1.40e-05 |
|
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major group in this CD corresponds to phosphoserine aminotransferase (PSAT). PSAT is active as a dimer and catalyzes the conversion of phosphohydroxypyruvate to phosphoserine.
Pssm-ID: 99736 [Multi-domain] Cd Length: 355 Bit Score: 46.52 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 37 LGVVQVIRQRLVELATPANGYTSVLLQGSGSYAVEAVLGSAIGAQGKVLIISNGAYGARMIEMAKLMCIAHHPYDCGE-- 114
Cdd:cd00611 43 EAIVNEAESDLRELLNIPDNYKVLFLQGGATGQFAAVPLNLLGDKGTADYVVTGAWSAKAAKEAKRYGGVVVIVAAKEeg 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 115 --VARPDAAAIEriLQTDPAITHIAMvhSETTTGMlnpieEVAALAKRYDKRYIVDAMSSFGGIPMDVAalNIDYLISSA 192
Cdd:cd00611 123 kyTKIPDVETWD--LAPDAAYVHYCS--NETIHGV-----EFDEVPDTGGVPLVADMSSNILSRPIDVS--KFGVIYAGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 193 NKCIqGVPGFAFVIAREAELANCQGRSRSLsLDlyaqWRCMEDNHGKWRfTSPTHTVLAFAQALKELAEEGGVRARHQRy 272
Cdd:cd00611 192 QKNL-GPAGVTVVIVRKDLLGKARKITPSM-LN----YKTHADNNSLYN-TPPTFAIYMMGLVLKWLKEQGGVEAMEKR- 263
|
....*.
gi 503993316 273 stNQQR 278
Cdd:cd00611 264 --NRQK 267
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
119-194 |
2.90e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 45.42 E-value: 2.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503993316 119 DAAAIERILQTDPAITHIAMVHSETttGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANK 194
Cdd:PLN02651 127 DLDELAAAIRPDTALVSVMAVNNEI--GVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK 200
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
119-194 |
4.28e-05 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 44.93 E-value: 4.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503993316 119 DAAAIERILQTDPAITHIAMVHSETttGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANK 194
Cdd:PRK14012 133 DLEKLEAAMRDDTILVSIMHVNNEI--GVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHK 206
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
132-212 |
4.77e-04 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 41.66 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 132 AITHIAMVhsettTGMLNPIEEVAALAKRYDKRYIVDAMSSFGGIPMDVAALNIDYLISSANKcIQGVPGFAFVIAREAE 211
Cdd:PRK09295 169 AITHVSNV-----LGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHK-LYGPTGIGILYVKEAL 242
|
.
gi 503993316 212 L 212
Cdd:PRK09295 243 L 243
|
|
| PRK03080 |
PRK03080 |
phosphoserine transaminase; |
39-187 |
6.59e-03 |
|
phosphoserine transaminase;
Pssm-ID: 235103 Cd Length: 378 Bit Score: 38.24 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993316 39 VVQVIRQRLVE-LATPAnGYTSVLLQGSGSYAVEAVLGSAIGAQGkVLIISNGAYGARMIEMA----KLMCIAHHPYDCG 113
Cdd:PRK03080 49 LLKRVIEGTRElLSLPE-GYEVGIVPGSDTGAWEMALWSLLGARR-VDHLAWESFGSKWATDVvkqlKLEDPRVLEADYG 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993316 114 EvaRPDAAAIerilqtDPAiTHIAMVHSETTTGMLNPIEEVAAlAKRyDKRYIVDAMSSFGGIPMDVAALNIDY 187
Cdd:PRK03080 127 S--LPDLSAV------DFD-RDVVFTWNGTTTGVRVPVARWIG-ADR-EGLTICDATSAAFALPLDWSKLDVYT 189
|
|
| Rnase_HI_RT_non_LTR |
cd09276 |
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into ... |
325-366 |
9.55e-03 |
|
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). Ribonuclease HI (RNase HI) is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as an adjunct domain to the reverse transcriptase gene in retroviruses, long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. The position of the RNase domain of non-LTR and LTR transposons is at the carboxyl terminal of the reverse transcriptase (RT) domain and their RNase domains group together, indicating a common evolutionary origin. Many non-LTR transposons have lost the RNase domain because their activity is at the nucleus and cellular RNase may suffice; however LTR retrotransposons always encode their own RNase domain because it requires RNase activity in RNA-protein particles in the cytoplasm. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.
Pssm-ID: 260008 [Multi-domain] Cd Length: 131 Bit Score: 36.04 E-value: 9.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503993316 325 GFVIYPGKVSQSDCFRIGNIGEVYDADITALLAAIKNAMYWQ 366
Cdd:cd09276 16 GFVIYRGGEVISRSYRLGTHASVFDAELEAILEALELALATA 57
|
|
| |
