






| Protein: | GLT1 |
| Organism: | Saccharomyces cerevisiae |
| Length: | 2145 amino acids |
| Reference: | Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for GLT1.
| Description | E-value | Query Range |
Subject Range |
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0.0 | [31..1567] | [85..1611] |
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0.0 | [23..1550] | [3..1520] |
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0.0 | [54..1549] | [1..1461] |
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0.0 | [43..2141] | [48..2207] |
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0.0 | [40..1565] | [84..1616] |
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0.0 | [40..1578] | [2..1510] |
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0.0 | [1183..2132] | [1..913] |
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0.0 | [50..1551] | [33..1536] |
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0.0 | [41..1582] | [10..1485] |
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0.0 | [26..1568] | [29..1537] |
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Region A: Residues: [1-499] |
1 11 21 31 41 51
| | | | | |
1 MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE HDACGVGFVA 60
61 NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL GIPHEFMKRE FKLDLDLDIP 120
121 EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF EDLAASFNLS VLGWRNVPVD STILGDVALS 180
181 REPTILQPLL VPLYDEKQPE FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK 240
241 GQLTPAQVYN YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN 300
301 KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL SLPEAVMMMV 360
361 PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC GAILDRNGLR PCRYYITSDD 420
421 RVICASEVGV IPIENSLVVQ KGKLKPGDLF LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS 480
481 KVIKLDDLLS KTANLVPKE
|
| Detection Method: | |
| Confidence: | 11000.0 |
| Match: | 1llwA_ |
| Description: | Alpha subunit of glutamate synthase, C-terminal domain; Alpha subunit of glutamate synthase, central and FMN domains; Alpha subunit of glutamate synthase, N-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
|
| Term | Confidence | Notes |
| glutamate synthase activity | 10.2123323896554 | bayes_pls_golite062009 |
| glutamate synthase activity, NADH or NADPH as acceptor | 9.64220719720108 | bayes_pls_golite062009 |
| glutamate synthase (NADPH) activity | 7.71666213946687 | bayes_pls_golite062009 |
| oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor | 3.97793872368585 | bayes_pls_golite062009 |
| oxidoreductase activity | 3.55520438339582 | bayes_pls_golite062009 |
| oxidoreductase activity, acting on the CH-CH group of donors | 1.75223963289059 | bayes_pls_golite062009 |
| catalytic activity | 1.19663085909195 | bayes_pls_golite062009 |
| nucleic acid binding | 1.07596988808091 | bayes_pls_golite062009 |
| endopeptidase activity | 1.05931638234802 | bayes_pls_golite062009 |
| peptidase activity, acting on L-amino acid peptides | 0.821264875808897 | bayes_pls_golite062009 |
| peptidase activity | 0.755649562279406 | bayes_pls_golite062009 |
| binding | 0.752066499785082 | bayes_pls_golite062009 |
| glutamate synthase (NADH) activity | 0.589012306271491 | bayes_pls_golite062009 |
| oxidoreductase activity, acting on the CH-NH2 group of donors | 0.391558094818592 | bayes_pls_golite062009 |
| transferase activity, transferring acyl groups | 0.181206025480438 | bayes_pls_golite062009 |
|
Region A: Residues: [500-856] |
1 11 21 31 41 51
| | | | | |
1 FISQDSLSLK VQSDPRLLAN GYTFEQVTFL LTPMALTGKE ALGSMGNDAP LACLNENPVL 60
61 LYDYFRQLFA QVTNPPIDPI REANVMSLEC YVGPQGNLLE MHSSQCDRLL LKSPILHWNE 120
121 FQALKNIEAA YPSWSVAEID ITFDKSEGLL GYTDTIDKIT KLASEAIDDG KKILIITDRK 180
181 MGANRVSISS LIAISCIHHH LIRNKQRSQV ALILETGEAR EIHHFCVLLG YGCDGVYPYL 240
241 AMETLVRMNR EGLLRNVNND NDTLEEGQIL ENYKHAIDAG ILKVMSKMGI STLASYKGAQ 300
301 IFEALGLDNS IVDLCFTGTS SRIRGVTFEY LAQDAFSLHE RGYPSRQTIS KSVNLPE
|
| Detection Method: | |
| Confidence: | 11000.0 |
| Match: | 1llwA_ |
| Description: | Alpha subunit of glutamate synthase, C-terminal domain; Alpha subunit of glutamate synthase, central and FMN domains; Alpha subunit of glutamate synthase, N-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
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Region A: Residues: [857-1292] |
1 11 21 31 41 51
| | | | | |
1 SGEYHFRDGG YKHVNEPTAI ASLQDTVRNK NDVSWQLYVK KEMEAIRDCT LRGLLELDFE 60
61 NSVSIPLEQV EPWTEIARRF ASGAMSYGSI SMEAHSTLAI AMNRLGAKSN CGEGGEDAER 120
121 SAVQENGDTM RSAIKQVASA RFGVTSYYLS DADEIQIKIA QGAKPGEGGE LPAHKVSKDI 180
181 AKTRHSTPNV GLISPPPHHD IYSIEDLKQL IYDLKCANPR AGISVKLVSE VGVGIVASGV 240
241 AKAKADHILV SGHDGGTGAA RWTSVKYAGL PWELGLAETH QTLVLNDLRR NVVVQTDGQL 300
301 RTGFDIAVAV LLGAESFTLA TVPLIAMGCV MLRRCHLNSC AVGIATQDPY LRSKFKGQPE 360
361 HVINFFYYLI QDLRQIMAKL GFRTIDEMVG HSEKLKKRDD VNAKAINIDL SPILTPAHVI 420
421 RPGVPTKFTK KQDHKL
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| Detection Method: | |
| Confidence: | 11000.0 |
| Match: | 1llwA_ |
| Description: | Alpha subunit of glutamate synthase, C-terminal domain; Alpha subunit of glutamate synthase, central and FMN domains; Alpha subunit of glutamate synthase, N-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
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Region A: Residues: [1293-1608] |
1 11 21 31 41 51
| | | | | |
1 HTRLDNKLID EAEVTLDRGL PVNIDASIIN TDRALGSTLS YRVSKKFGED GLPKDTVVVN 60
61 IEGSAGQSFG AFLASGITFI LNGDANDYVG KGLSGGIIVI KPPKDSKFKS DENVIVGNTC 120
121 FYGATSGTAF ISGSAGERFG VRNSGATIVV ERIKGNNAFE YMTGGRAIVL SQMESLNAFS 180
181 GATGGIAYCL TSDYDDFVGK INKDTVELES LCDPVEIAFV KNLIQEHWNY TQSDLAARIL 240
241 GNFNHYLKDF VKVIPTDYKK VLLKEKAEAA KAKAKATSEY LKKFRSNQEV DDEVNTLLIA 300
301 NQKAKEQEKK KSITIS
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| Detection Method: | |
| Confidence: | 11000.0 |
| Match: | 1llwA_ |
| Description: | Alpha subunit of glutamate synthase, C-terminal domain; Alpha subunit of glutamate synthase, central and FMN domains; Alpha subunit of glutamate synthase, N-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
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Region A: Residues: [1609-2145] |
1 11 21 31 41 51
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1 NKATLKEPKV VDLEDAVPDS KQLEKNSERI EKTRGFMIHK RRHETHRDPR TRVNDWKEFT 60
61 NPITKKDAKY QTARCMDCGT PFCLSDTGCP LSNIIPKFNE LLFKNQWKLA LDKLLETNNF 120
121 PEFTGRVCPA PCEGACTLGI IEDPVGIKSV ERIIIDNAFK EGWIKPCPPS TRTGFTVGVI 180
181 GSGPAGLACA DMLNRAGHTV TVYERSDRCG GLLMYGIPNM KLDKAIVQRR IDLLSAEGID 240
241 FVTNTEIGKT ISMDELKNKH NAVVYAIGST IPRDLPIKGR ELKNIDFAMQ LLESNTKALL 300
301 NKDLEIIREK IQGKKVIVVG GGDTGNDCLG TSVRHGAASV LNFELLPEPP VERAKDNPWP 360
361 QWPRVMRVDY GHAEVKEHYG RDPREYCILS KEFIGNDEGE VTAIRTVRVE WKKSQSGVWQ 420
421 MVEIPNSEEI FEADIILLSM GFVGPELING NDNEVKKTRR GTIATLDDSS YSIDGGKTFA 480
481 CGDCRRGQSL IVWAIQEGRK CAASVDKFLM DGTTYLPSNG GIVQRDYKLL KELASQV
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| Detection Method: | |
| Confidence: | 259.9897 |
| Match: | 1gt8A_ |
| Description: | Dihydropyrimidine dehydrogenase, N-terminal domain; Dihydropyrimidine dehydrogenase, domain 4; Dihydropyrimidine dehydrogenase, domain 3; Dihydropyrimidine dehydrogenase, domain 2; Dihydropyrimidine dehydrogenase, C-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
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