SitesBLAST
Comparing CA265_RS09005 CA265_RS09005 phosphoserine transaminase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
57% identity, 98% coverage: 3:351/357 of query aligns to 2:349/349 of 5yb0B
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
47% identity, 99% coverage: 3:354/357 of query aligns to 5:361/361 of 1bt4A
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
49% identity, 97% coverage: 4:351/357 of query aligns to 6:358/360 of 4azjA
- active site: W102 (= W99), D172 (= D166), K196 (= K190)
- binding pyridoxal-5'-phosphate: A76 (= A73), S77 (= S74), W102 (= W99), T152 (= T147), D172 (= D166), S174 (= S168), Q195 (= Q189), K196 (= K190), N237 (= N231), T238 (= T232)
- binding phosphoserine: H41 (= H38), R42 (= R39), W102 (= W99), T152 (= T147), K196 (= K190), H327 (= H320), R328 (= R321), R334 (= R327)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
49% identity, 97% coverage: 4:351/357 of query aligns to 6:355/357 of 1w23B
- active site: W102 (= W99), D172 (= D166), K196 (= K190)
- binding magnesium ion: Y127 (= Y124), Y154 (= Y149), H285 (≠ T281), A286 (≠ C282)
- binding pyridoxal-5'-phosphate: A76 (= A73), S77 (= S74), W102 (= W99), T152 (= T147), D172 (= D166), S174 (= S168), Q195 (= Q189), K196 (= K190), N234 (= N231), T235 (= T232)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
48% identity, 99% coverage: 3:354/357 of query aligns to 3:359/359 of 3qboB
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
48% identity, 98% coverage: 4:354/357 of query aligns to 4:360/360 of 1bjoA
- active site: W100 (= W99), D172 (= D166), K196 (= K190)
- binding alpha-methyl-l-glutamic acid: S7 (≠ A7), W100 (= W99), T151 (= T147), K196 (= K190)
- binding pyridoxal-5'-phosphate: G74 (≠ A73), R75 (≠ S74), W100 (= W99), T151 (= T147), D172 (= D166), S174 (= S168), Q195 (= Q189), K196 (= K190)
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
46% identity, 99% coverage: 3:354/357 of query aligns to 3:360/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G72), G74 (≠ A73), R75 (≠ S74), W100 (= W99), T151 (= T147), D172 (= D166), S174 (= S168), Q195 (= Q189), K196 (= K190), N237 (= N231), T238 (= T232)
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
42% identity, 98% coverage: 4:353/357 of query aligns to 4:358/359 of 6xdkD
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
45% identity, 98% coverage: 4:354/357 of query aligns to 75:430/430 of Q96255
- AT 145:146 (≠ AS 73:74) binding
- W171 (= W99) binding
- T221 (= T147) binding
- D241 (= D166) binding
- Q264 (= Q189) binding
- K265 (= K190) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 231:232) binding
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
44% identity, 98% coverage: 4:354/357 of query aligns to 5:360/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G72), A75 (= A73), T76 (≠ S74), W101 (= W99), T151 (= T147), D171 (= D166), S173 (= S168), Q194 (= Q189), K195 (= K190), N236 (= N231), T237 (= T232)
- binding phosphoserine: W101 (= W99), T151 (= T147), K195 (= K190), H326 (= H320), R327 (= R321), R333 (= R327)
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
44% identity, 98% coverage: 4:354/357 of query aligns to 7:362/362 of 6czyA
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
44% identity, 98% coverage: 4:353/357 of query aligns to 5:364/366 of 8a5vE
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
44% identity, 98% coverage: 4:353/357 of query aligns to 9:368/370 of Q9Y617
- S43 (= S37) to R: in PSATD; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 3-fold increase of KM for 3-phosphohydroxypyruvate; 5-fold increase of KM for L-glutamate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability
- H44 (= H38) binding in other chain
- R45 (= R39) binding in other chain
- Y70 (= Y64) to N: in NLS2; unknown pathological significance
- G79 (≠ A73) binding ; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway
- C80 (≠ S74) binding
- P87 (= P81) to A: has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; no effect on function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability; dbSNP:rs11540974
- A99 (= A91) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ S92) to A: in PSATD; has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; does not affect secondary structure; results in increased protein aggregation as shown by dynamic light scattering; dbSNP:rs118203967
- W107 (= W99) binding
- E155 (≠ N146) to Q: in NLS2; unknown pathological significance
- T156 (= T147) binding
- D176 (= D166) binding
- S179 (= S169) to L: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs587777777
- Q199 (= Q189) binding
- K200 (= K190) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N231) binding in other chain
- T242 (= T232) binding in other chain
- C245 (≠ V235) to R: in NLS2; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 9-fold increase of KM for L-glutamate; does not affect KM for 3-phosphohydroxypyruvate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization
- H335 (= H320) binding
- R336 (= R321) binding
- R342 (= R327) binding ; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs202103028
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
44% identity, 98% coverage: 4:353/357 of query aligns to 4:363/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
44% identity, 98% coverage: 4:353/357 of query aligns to 4:363/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G72), G74 (≠ A73), C75 (≠ S74), W102 (= W99), T151 (= T147), D171 (= D166), S173 (= S168), Q194 (= Q189), K195 (= K190)
- binding phosphoserine: H39 (= H38), R40 (= R39), H330 (= H320), R337 (= R327)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
44% identity, 98% coverage: 4:353/357 of query aligns to 4:363/365 of 8a5vA
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
41% identity, 98% coverage: 4:353/357 of query aligns to 4:354/355 of 6xdkB
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
44% identity, 98% coverage: 4:353/357 of query aligns to 5:363/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H38), R41 (= R39), N236 (= N231), T237 (= T232)
- binding (2~{S})-2-[[(~{R})-[[(5~{S})-5-azanyl-6-oxidanylidene-hexyl]amino]-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methyl]amino]-3-phosphonooxy-propanoic acid: G74 (= G72), G75 (≠ A73), C76 (≠ S74), W103 (= W99), T152 (= T147), S174 (= S168), A194 (= A188), Q195 (= Q189), N196 (= N191), H330 (= H320), R331 (= R321), R337 (= R327), Y341 (= Y331)
3e77A Human phosphoserine aminotransferase in complex with plp
44% identity, 96% coverage: 11:353/357 of query aligns to 9:361/363 of 3e77A
- active site: W100 (= W99), D169 (= D166), K193 (= K190)
- binding pyridoxal-5'-phosphate: G71 (= G72), G72 (≠ A73), C73 (≠ S74), W100 (= W99), T149 (= T147), D169 (= D166), S171 (= S168), Q192 (= Q189), K193 (= K190), N234 (= N231), T235 (= T232)
3qm2B 2.25 angstrom crystal structure of phosphoserine aminotransferase (serc) from salmonella enterica subsp. Enterica serovar typhimurium
42% identity, 98% coverage: 4:354/357 of query aligns to 4:331/331 of 3qm2B
Query Sequence
>CA265_RS09005 CA265_RS09005 phosphoserine transaminase
MKHNFGAGPCILPQEVFKQAAQAVLDFNDGLSILEISHRTTEFEAVVAEADKLVKELLNV
PSGYSVLFLQGGASLQFAMVPMNLLGDGQTASYLDSGVWATKALKEAKFIGNVNVVASSK
DANYTFIPKDFEIPADSAYFHYTSNNTIYGTELFEVPKTNVPVVCDMSSDIMSRVIDVSK
FDLIYAGAQKNVGPAGLTIAIVKNEVLGKIDRKIPSMLNYQSHIDNDSMYNTPPVFSIYV
ALLNLRWLKSKGGVAEIEKENKQKAEALYREIDRNPLFKGTCAVEDRSRMNVCFVMENPE
LEKPFLKYAEEQGIVGIKGHRSVGGFRASMYNALPITSVHALVDAMQVFEEQQAKAN
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory