SitesBLAST
Comparing WP_011734678.1 NCBI__GCF_000015045.1:WP_011734678.1 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)
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
51% identity, 100% coverage: 2:364/364 of query aligns to 71:430/430 of Q96255
- AT 145:146 (≠ AS 76:77) binding pyridoxal 5'-phosphate
- W171 (= W102) binding pyridoxal 5'-phosphate
- T221 (= T150) binding pyridoxal 5'-phosphate
- D241 (= D170) binding pyridoxal 5'-phosphate
- Q264 (= Q193) binding pyridoxal 5'-phosphate
- K265 (= K194) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 235:236) binding pyridoxal 5'-phosphate
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
51% identity, 99% coverage: 3:364/364 of query aligns to 4:362/362 of 6czyA
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
51% identity, 99% coverage: 3:364/364 of query aligns to 2:360/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G75), A75 (= A76), T76 (≠ S77), W101 (= W102), T151 (= T150), D171 (= D170), S173 (= S172), Q194 (= Q193), K195 (= K194), N236 (= N235), T237 (= T236)
- binding phosphoserine: W101 (= W102), T151 (= T150), K195 (= K194), H326 (= H330), R327 (= R331), R333 (= R337)
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
47% identity, 99% coverage: 1:360/364 of query aligns to 1:357/360 of 4azjA
- active site: W102 (= W102), D172 (= D170), K196 (= K194)
- binding pyridoxal-5'-phosphate: A76 (= A76), S77 (= S77), W102 (= W102), T152 (= T150), D172 (= D170), S174 (= S172), Q195 (= Q193), K196 (= K194), N237 (= N235), T238 (= T236)
- binding phosphoserine: H41 (= H41), R42 (= R42), W102 (= W102), T152 (= T150), K196 (= K194), H327 (= H330), R328 (= R331), R334 (= R337)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
47% identity, 99% coverage: 1:360/364 of query aligns to 1:354/357 of 1w23B
- active site: W102 (= W102), D172 (= D170), K196 (= K194)
- binding magnesium ion: Y127 (≠ W127), Y154 (≠ E152), H285 (≠ P285), A286 (≠ V286)
- binding pyridoxal-5'-phosphate: A76 (= A76), S77 (= S77), W102 (= W102), T152 (= T150), D172 (= D170), S174 (= S172), Q195 (= Q193), K196 (= K194), N234 (= N235), T235 (= T236)
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
47% identity, 99% coverage: 2:360/364 of query aligns to 2:357/361 of 1bt4A
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
44% identity, 98% coverage: 2:359/364 of query aligns to 5:364/370 of Q9Y617
- S43 (= S40) 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 (= H41) binding in other chain
- R45 (= R42) binding in other chain
- Y70 (= Y67) to N: in NLS2; uncertain significance
- G79 (≠ A76) binding pyridoxal 5'-phosphate; 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 (≠ S77) binding pyridoxal 5'-phosphate
- P87 (= P84) 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 (= A94) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (= D95) 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 (= W102) binding pyridoxal 5'-phosphate
- E155 (≠ N149) to Q: in NLS2; uncertain significance
- T156 (= T150) binding pyridoxal 5'-phosphate
- D176 (= D170) binding pyridoxal 5'-phosphate
- S179 (= S173) 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 (= Q193) binding pyridoxal 5'-phosphate
- K200 (= K194) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N235) binding in other chain
- T242 (= T236) binding in other chain
- C245 (= C239) 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 (= H330) binding O-phospho-L-serine
- R336 (= R331) binding O-phospho-L-serine
- R342 (= R337) binding O-phospho-L-serine; 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
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
44% identity, 98% coverage: 2:359/364 of query aligns to 1:360/366 of 8a5vE
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
45% identity, 97% coverage: 6:359/364 of query aligns to 4:359/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
45% identity, 97% coverage: 6:359/364 of query aligns to 4:359/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G75), G74 (≠ A76), C75 (≠ S77), W102 (= W102), T151 (= T150), D171 (= D170), S173 (= S172), Q194 (= Q193), K195 (= K194)
- binding phosphoserine: H39 (= H41), R40 (= R42), H330 (= H330), R337 (= R337)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
45% identity, 97% coverage: 6:359/364 of query aligns to 4:359/365 of 8a5vA
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
45% identity, 99% coverage: 3:362/364 of query aligns to 1:357/359 of 6xdkD
3e77A Human phosphoserine aminotransferase in complex with plp
45% identity, 96% coverage: 12:359/364 of query aligns to 8:357/363 of 3e77A
- active site: W100 (= W102), D169 (= D170), K193 (= K194)
- binding pyridoxal-5'-phosphate: G71 (= G75), G72 (≠ A76), C73 (≠ S77), W100 (= W102), T149 (= T150), D169 (= D170), S171 (= S172), Q192 (= Q193), K193 (= K194), N234 (= N235), T235 (= T236)
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
44% identity, 98% coverage: 2:359/364 of query aligns to 1:359/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H41), R41 (= R42), N236 (= N235), T237 (= T236)
- 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 (= G75), G75 (≠ A76), C76 (≠ S77), W103 (= W102), T152 (= T150), S174 (= S172), A194 (= A192), Q195 (= Q193), N196 (= N195), H330 (= H330), R331 (= R331), R337 (= R337), Y341 (= Y341)
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
45% identity, 99% coverage: 3:362/364 of query aligns to 1:353/355 of 6xdkB
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
43% identity, 99% coverage: 3:362/364 of query aligns to 1:357/359 of 3qboB
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
43% identity, 98% coverage: 4:360/364 of query aligns to 1:348/349 of 5yb0B
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
45% identity, 99% coverage: 3:362/364 of query aligns to 1:358/360 of 1bjoA
- active site: W100 (= W102), D172 (= D170), K196 (= K194)
- binding alpha-methyl-l-glutamic acid: S7 (≠ A9), W100 (= W102), T151 (= T150), K196 (= K194)
- binding pyridoxal-5'-phosphate: G74 (≠ A76), R75 (≠ S77), W100 (= W102), T151 (= T150), D172 (= D170), S174 (= S172), Q195 (= Q193), K196 (= K194)
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
44% identity, 99% coverage: 3:362/364 of query aligns to 1:358/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G75), G74 (≠ A76), R75 (≠ S77), W100 (= W102), T151 (= T150), D172 (= D170), S174 (= S172), Q195 (= Q193), K196 (= K194), N237 (= N235), T238 (= T236)
3qm2B 2.25 angstrom crystal structure of phosphoserine aminotransferase (serc) from salmonella enterica subsp. Enterica serovar typhimurium
41% identity, 99% coverage: 3:362/364 of query aligns to 1:329/331 of 3qm2B
Query Sequence
>WP_011734678.1 NCBI__GCF_000015045.1:WP_011734678.1
MKRFYNFSAGPSMLPESVLAKAADEMLCYETSGQSVMEMSHRSKPFEAIIAGAEALVRQN
MAIPDDYHVLFLQGGASLQFHMLPLNFMTINKKADFTLTGTWAQKAAEEAKRLGTANIVG
SSKDKKWSYLPEITGADPEADYFHICYNNTIEGTQYHSIPEVGAVPLIGDISSGVLSAPL
DVTRFAVLYAGAQKNLGPAGVTLVIIRKDMMERIPAGLPAMLSYKTHVDGGSMYNTPPCY
AIYIFKLVQEWIRDMGGAEVIYRQNQEKARLLYDFLDSSSLFFSPVEKSVRSLMNVPFLT
TEKDADKAEALNKKFVKESEAAGLVNLAGHRSVGGMRASIYNAMPLEGVQALVAFMKEFE
ARCA
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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