SitesBLAST
Comparing 201554 FitnessBrowser__MR1:201554 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
58% identity, 98% coverage: 6:364/367 of query aligns to 2:359/360 of 1bjoA
- active site: W100 (= W104), D172 (= D177), K196 (= K201)
- binding alpha-methyl-l-glutamic acid: S7 (≠ A11), W100 (= W104), T151 (= T158), K196 (= K201)
- binding pyridoxal-5'-phosphate: G74 (= G78), R75 (= R79), W100 (= W104), T151 (= T158), D172 (= D177), S174 (= S179), Q195 (= Q200), K196 (= K201)
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
57% identity, 98% coverage: 6:364/367 of query aligns to 2:359/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G77), G74 (= G78), R75 (= R79), W100 (= W104), T151 (= T158), D172 (= D177), S174 (= S179), Q195 (= Q200), K196 (= K201), N237 (= N242), T238 (= T243)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
56% identity, 98% coverage: 6:364/367 of query aligns to 2:358/359 of 3qboB
3qm2B 2.25 angstrom crystal structure of phosphoserine aminotransferase (serc) from salmonella enterica subsp. Enterica serovar typhimurium
51% identity, 98% coverage: 6:364/367 of query aligns to 2:330/331 of 3qm2B
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
48% identity, 98% coverage: 7:364/367 of query aligns to 3:358/359 of 6xdkD
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
47% identity, 98% coverage: 7:364/367 of query aligns to 3:354/355 of 6xdkB
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
44% identity, 98% coverage: 6:364/367 of query aligns to 73:429/430 of Q96255
- AT 145:146 (≠ GR 78:79) binding
- W171 (= W104) binding
- T221 (= T158) binding
- D241 (= D177) binding
- Q264 (= Q200) binding
- K265 (= K201) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 242:243) 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: 6:364/367 of query aligns to 3:359/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G77), A75 (≠ G78), T76 (≠ R79), W101 (= W104), T151 (= T158), D171 (= D177), S173 (= S179), Q194 (= Q200), K195 (= K201), N236 (= N242), T237 (= T243)
- binding phosphoserine: W101 (= W104), T151 (= T158), K195 (= K201), H326 (= H331), R327 (= R332), R333 (= R338)
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
44% identity, 98% coverage: 6:364/367 of query aligns to 5:361/362 of 6czyA
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
42% identity, 96% coverage: 7:360/367 of query aligns to 5:356/361 of 1bt4A
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
42% identity, 98% coverage: 6:364/367 of query aligns to 2:363/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
42% identity, 98% coverage: 6:364/367 of query aligns to 2:363/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G77), G74 (= G78), C75 (≠ R79), W102 (= W104), T151 (= T158), D171 (= D177), S173 (= S179), Q194 (= Q200), K195 (= K201)
- binding phosphoserine: H39 (= H43), R40 (= R44), H330 (= H331), R337 (= R338)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
42% identity, 98% coverage: 6:364/367 of query aligns to 2:363/365 of 8a5vA
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
42% identity, 98% coverage: 6:364/367 of query aligns to 3:364/366 of 8a5vE
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
42% identity, 98% coverage: 6:364/367 of query aligns to 7:368/370 of Q9Y617
- S43 (= S42) 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 (= H43) binding in other chain
- R45 (= R44) binding in other chain
- Y70 (= Y69) to N: in NLS2; uncertain significance
- G79 (= G78) 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 (≠ R79) binding
- P87 (≠ V86) 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 (= A96) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ L97) 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 (= W104) binding
- E155 (= E157) to Q: in NLS2; uncertain significance
- T156 (= T158) binding
- D176 (= D177) binding
- S179 (= S180) 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 (= Q200) binding
- K200 (= K201) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N242) binding in other chain
- T242 (= T243) binding in other chain
- C245 (≠ T246) 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 (= H331) binding
- R336 (= R332) binding
- R342 (= R338) 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
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
41% identity, 98% coverage: 3:360/367 of query aligns to 1:356/360 of 4azjA
- active site: W102 (= W104), D172 (= D177), K196 (= K201)
- binding pyridoxal-5'-phosphate: A76 (≠ G78), S77 (≠ R79), W102 (= W104), T152 (= T158), D172 (= D177), S174 (= S179), Q195 (= Q200), K196 (= K201), N237 (= N242), T238 (= T243)
- binding phosphoserine: H41 (= H43), R42 (= R44), W102 (= W104), T152 (= T158), K196 (= K201), H327 (= H331), R328 (= R332), R334 (= R338)
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
41% identity, 98% coverage: 6:364/367 of query aligns to 3:363/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H43), R41 (= R44), N236 (= N242), T237 (= T243)
- 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 (= G77), G75 (= G78), C76 (≠ R79), W103 (= W104), T152 (= T158), S174 (= S179), A194 (= A199), Q195 (= Q200), N196 (= N202), H330 (= H331), R331 (= R332), R337 (= R338), Y341 (= Y342)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
41% identity, 98% coverage: 3:360/367 of query aligns to 1:353/357 of 1w23B
- active site: W102 (= W104), D172 (= D177), K196 (= K201)
- binding magnesium ion: Y127 (≠ L133), Y154 (≠ D160), H285 (≠ G292), A286 (≠ V293)
- binding pyridoxal-5'-phosphate: A76 (≠ G78), S77 (≠ R79), W102 (= W104), T152 (= T158), D172 (= D177), S174 (= S179), Q195 (= Q200), K196 (= K201), N234 (= N242), T235 (= T243)
3e77A Human phosphoserine aminotransferase in complex with plp
42% identity, 96% coverage: 14:364/367 of query aligns to 8:361/363 of 3e77A
- active site: W100 (= W104), D169 (= D177), K193 (= K201)
- binding pyridoxal-5'-phosphate: G71 (= G77), G72 (= G78), C73 (≠ R79), W100 (= W104), T149 (= T158), D169 (= D177), S171 (= S179), Q192 (= Q200), K193 (= K201), N234 (= N242), T235 (= T243)
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
39% identity, 97% coverage: 6:360/367 of query aligns to 1:347/349 of 5yb0B
Query Sequence
>201554 FitnessBrowser__MR1:201554
MAVSAIYNFCAGPAMLPAAVMKKAQQELLDWNGLGVSVMEVSHRGKEFIALTKQAEADLR
ELMHIPQNYHVLFMHGGGRGQFSAVVNNFLGNQGRALYLVSGQWSSAALAEAQKLAGDAQ
IDSLNIVEKHNCLNAVVLPDLHKIDADYRYVHYCPNETVDGIEIFDELDSPWPIVADLSS
TIMSREIDVSRYGLIYAGAQKNIGPSGLSIVIVRDDMLTLPSLPQSSIMDYRLAVEHDSM
FNTPPTFAWYLAAEVFAWLKSIGGVASIAKINQQKAQMLYACIDANPFYKNGVVAANRSQ
MNVTFQLADESLDGAFLKEAEAVGLVALKGHRIVGGMRASLYNAMPLEGVAALVTFMNEF
AAKHYNI
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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