SitesBLAST
Comparing WP_035236531.1 NCBI__GCF_000745975.1:WP_035236531.1 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)
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
57% identity, 98% coverage: 4:359/362 of query aligns to 2:358/361 of 1bt4A
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
51% identity, 99% coverage: 4:361/362 of query aligns to 2:360/360 of 4azjA
- active site: W102 (= W104), D172 (= D173), K196 (= K197)
- binding pyridoxal-5'-phosphate: A76 (= A78), S77 (= S79), W102 (= W104), T152 (= T153), D172 (= D173), S174 (= S175), Q195 (= Q196), K196 (= K197), N237 (= N238), T238 (= T239)
- binding phosphoserine: H41 (= H43), R42 (= R44), W102 (= W104), T152 (= T153), K196 (= K197), H327 (= H328), R328 (= R329), R334 (= R335)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
50% identity, 99% coverage: 4:361/362 of query aligns to 2:357/357 of 1w23B
- active site: W102 (= W104), D172 (= D173), K196 (= K197)
- binding magnesium ion: Y127 (≠ F130), Y154 (≠ K155), H285 (≠ T289), A286 (= A290)
- binding pyridoxal-5'-phosphate: A76 (= A78), S77 (= S79), W102 (= W104), T152 (= T153), D172 (= D173), S174 (= S175), Q195 (= Q196), K196 (= K197), N234 (= N238), T235 (= T239)
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
47% identity, 99% coverage: 2:358/362 of query aligns to 69:426/430 of Q96255
- AT 145:146 (≠ AS 78:79) binding
- W171 (= W104) binding
- T221 (= T153) binding
- D241 (= D173) binding
- Q264 (= Q196) binding
- K265 (= K197) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 238:239) binding
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
47% identity, 99% coverage: 2:358/362 of query aligns to 1:358/362 of 6czyA
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
48% identity, 98% coverage: 5:358/362 of query aligns to 2:356/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G77), A75 (= A78), T76 (≠ S79), W101 (= W104), T151 (= T153), D171 (= D173), S173 (= S175), Q194 (= Q196), K195 (= K197), N236 (= N238), T237 (= T239)
- binding phosphoserine: W101 (= W104), T151 (= T153), K195 (= K197), H326 (= H328), R327 (= R329), R333 (= R335)
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
47% identity, 98% coverage: 5:360/362 of query aligns to 1:357/359 of 6xdkD
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
46% identity, 98% coverage: 5:360/362 of query aligns to 1:353/355 of 6xdkB
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
44% identity, 98% coverage: 5:360/362 of query aligns to 1:357/359 of 3qboB
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
44% identity, 98% coverage: 6:359/362 of query aligns to 1:349/349 of 5yb0B
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
43% identity, 98% coverage: 5:360/362 of query aligns to 1:358/360 of 1bjoA
- active site: W100 (= W104), D172 (= D173), K196 (= K197)
- binding alpha-methyl-l-glutamic acid: S7 (≠ A11), W100 (= W104), T151 (= T153), K196 (= K197)
- binding pyridoxal-5'-phosphate: G74 (≠ A78), R75 (≠ S79), W100 (= W104), T151 (= T153), D172 (= D173), S174 (= S175), Q195 (= Q196), K196 (= K197)
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
43% identity, 98% coverage: 5:360/362 of query aligns to 1:358/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G77), G74 (≠ A78), R75 (≠ S79), W100 (= W104), T151 (= T153), D172 (= D173), S174 (= S175), Q195 (= Q196), K196 (= K197), N237 (= N238), T238 (= T239)
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
42% identity, 98% coverage: 4:357/362 of query aligns to 5:364/370 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 (≠ A78) 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 (≠ S79) binding
- P87 (= P86) 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 (= D97) 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 (≠ N152) to Q: in NLS2; uncertain significance
- T156 (= T153) binding
- D176 (= D173) binding
- S179 (= S176) 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 (= Q196) binding
- K200 (= K197) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N238) binding in other chain
- T242 (= T239) binding in other chain
- C245 (= C242) 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 (= H328) binding
- R336 (= R329) binding
- R342 (= R335) 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
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
42% identity, 98% coverage: 4:357/362 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)
42% identity, 98% coverage: 5:357/362 of query aligns to 1:359/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
42% identity, 98% coverage: 5:357/362 of query aligns to 1:359/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G77), G74 (≠ A78), C75 (≠ S79), W102 (= W104), T151 (= T153), D171 (= D173), S173 (= S175), Q194 (= Q196), K195 (= K197)
- binding phosphoserine: H39 (= H43), R40 (= R44), H330 (= H328), R337 (= R335)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
42% identity, 98% coverage: 5:357/362 of query aligns to 1:359/365 of 8a5vA
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
42% identity, 98% coverage: 4:357/362 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 (= H43), R41 (= R44), N236 (= N238), T237 (= T239)
- 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 (≠ A78), C76 (≠ S79), W103 (= W104), T152 (= T153), S174 (= S175), A194 (= A195), Q195 (= Q196), N196 (= N198), H330 (= H328), R331 (= R329), R337 (= R335), Y341 (= Y339)
3e77A Human phosphoserine aminotransferase in complex with plp
42% identity, 94% coverage: 16:357/362 of query aligns to 10:357/363 of 3e77A
- active site: W100 (= W104), D169 (= D173), K193 (= K197)
- binding pyridoxal-5'-phosphate: G71 (= G77), G72 (≠ A78), C73 (≠ S79), W100 (= W104), T149 (= T153), D169 (= D173), S171 (= S175), Q192 (= Q196), K193 (= K197), N234 (= N238), T235 (= T239)
3qm2B 2.25 angstrom crystal structure of phosphoserine aminotransferase (serc) from salmonella enterica subsp. Enterica serovar typhimurium
40% identity, 98% coverage: 5:360/362 of query aligns to 1:329/331 of 3qm2B
Query Sequence
>WP_035236531.1 NCBI__GCF_000745975.1:WP_035236531.1
MTDQRIYNFNAGPAALPLPVLEEIQASFLNFGNSGMSITEISHRSSYFDDVINDAVARAK
RLLGLDDQYHVLFIQGGASLQFAMIPMNFLSGDQSADYVNTGTWSTKAIKEAKIQNKKHV
VVASSEDKDFSYIPGNIPFSKDAKYVHITSNNTIKGTQFADFPDTGGVPIIADMSSDIFS
RPLPMEKFGMIYAGAQKNLGPSGTCVVILRKDLLETANSDLPSMLKYSTYAEKNSMYNTP
PCFGIYTIDLVLKWIEEEMGGLEKMEAFNKEKAGLLYDFMEASNFYRATAAQGSRSLMNV
TFRLPSEELEQKFIKEATAKGLGGLKGHRSVGGCRASIYNATTMEGIKALVQFMDAFQKE
AK
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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