SitesBLAST
Comparing WP_013820554.1 NCBI__GCF_000214665.1:WP_013820554.1 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
46% identity, 98% coverage: 5:363/368 of query aligns to 2:358/361 of 1bt4A
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
43% identity, 97% coverage: 8:364/368 of query aligns to 74:428/430 of Q96255
- AT 145:146 (= AT 79:80) binding pyridoxal 5'-phosphate
- W171 (= W106) binding pyridoxal 5'-phosphate
- T221 (= T156) binding pyridoxal 5'-phosphate
- D241 (= D176) binding pyridoxal 5'-phosphate
- Q264 (= Q199) binding pyridoxal 5'-phosphate
- K265 (= K200) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 241:242) binding pyridoxal 5'-phosphate
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
44% identity, 96% coverage: 8:361/368 of query aligns to 3:359/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
44% identity, 96% coverage: 8:361/368 of query aligns to 3:359/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G78), G74 (≠ A79), C75 (≠ T80), W102 (= W106), T151 (= T156), D171 (= D176), S173 (= S178), Q194 (= Q199), K195 (= K200)
- binding phosphoserine: H39 (= H44), R40 (= R45), H330 (= H332), R337 (= R339)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
44% identity, 96% coverage: 8:361/368 of query aligns to 3:359/365 of 8a5vA
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
44% identity, 96% coverage: 8:361/368 of query aligns to 4:360/366 of 8a5vE
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
43% identity, 97% coverage: 8:364/368 of query aligns to 6:360/362 of 6czyA
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
43% identity, 97% coverage: 8:364/368 of query aligns to 4:358/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G78), A75 (= A79), T76 (= T80), W101 (= W106), T151 (= T156), D171 (= D176), S173 (= S178), Q194 (= Q199), K195 (= K200), N236 (= N241), T237 (= T242)
- binding phosphoserine: W101 (= W106), T151 (= T156), K195 (= K200), H326 (= H332), R327 (= R333), R333 (= R339)
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
44% identity, 96% coverage: 8:361/368 of query aligns to 8:364/370 of Q9Y617
- S43 (= S43) 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 (= H44) binding in other chain
- R45 (= R45) binding in other chain
- Y70 (= Y70) to N: in NLS2; uncertain significance
- G79 (≠ A79) 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 (≠ T80) binding pyridoxal 5'-phosphate
- P87 (= P87) 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 (= A98) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ E99) 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 (= W106) binding pyridoxal 5'-phosphate
- E155 (= E155) to Q: in NLS2; uncertain significance
- T156 (= T156) binding pyridoxal 5'-phosphate
- D176 (= D176) binding pyridoxal 5'-phosphate
- S179 (= S179) 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 (= Q199) binding pyridoxal 5'-phosphate
- K200 (= K200) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N241) binding in other chain
- T242 (= T242) binding in other chain
- C245 (≠ V245) 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 (= H332) binding O-phospho-L-serine
- R336 (= R333) binding O-phospho-L-serine
- R342 (= R339) 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
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
43% identity, 96% coverage: 8:361/368 of query aligns to 5:356/360 of 4azjA
- active site: W102 (= W106), D172 (= D176), K196 (= K200)
- binding pyridoxal-5'-phosphate: A76 (= A79), S77 (≠ T80), W102 (= W106), T152 (= T156), D172 (= D176), S174 (= S178), Q195 (= Q199), K196 (= K200), N237 (= N241), T238 (= T242)
- binding phosphoserine: H41 (= H44), R42 (= R45), W102 (= W106), T152 (= T156), K196 (= K200), H327 (= H332), R328 (= R333), R334 (= R339)
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
44% identity, 96% coverage: 8:361/368 of query aligns to 4:359/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H44), R41 (= R45), N236 (= N241), T237 (= T242)
- 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 (= G78), G75 (≠ A79), C76 (≠ T80), W103 (= W106), T152 (= T156), S174 (= S178), A194 (= A198), Q195 (= Q199), N196 (= N201), H330 (= H332), R331 (= R333), R337 (= R339), Y341 (= Y343)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
44% identity, 96% coverage: 8:361/368 of query aligns to 5:353/357 of 1w23B
- active site: W102 (= W106), D172 (= D176), K196 (= K200)
- binding magnesium ion: Y127 (≠ F131), Y154 (≠ E158), H285 (≠ R293), A286 (= A294)
- binding pyridoxal-5'-phosphate: A76 (= A79), S77 (≠ T80), W102 (= W106), T152 (= T156), D172 (= D176), S174 (= S178), Q195 (= Q199), K196 (= K200), N234 (= N241), T235 (= T242)
3e77A Human phosphoserine aminotransferase in complex with plp
44% identity, 94% coverage: 17:361/368 of query aligns to 10:357/363 of 3e77A
- active site: W100 (= W106), D169 (= D176), K193 (= K200)
- binding pyridoxal-5'-phosphate: G71 (= G78), G72 (≠ A79), C73 (≠ T80), W100 (= W106), T149 (= T156), D169 (= D176), S171 (= S178), Q192 (= Q199), K193 (= K200), N234 (= N241), T235 (= T242)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
44% identity, 97% coverage: 9:364/368 of query aligns to 4:357/359 of 3qboB
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
44% identity, 97% coverage: 9:364/368 of query aligns to 4:358/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G78), G74 (≠ A79), R75 (≠ T80), W100 (= W106), T151 (= T156), D172 (= D176), S174 (= S178), Q195 (= Q199), K196 (= K200), N237 (= N241), T238 (= T242)
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
44% identity, 97% coverage: 8:364/368 of query aligns to 3:358/360 of 1bjoA
- active site: W100 (= W106), D172 (= D176), K196 (= K200)
- binding alpha-methyl-l-glutamic acid: S7 (≠ G12), W100 (= W106), T151 (= T156), K196 (= K200)
- binding pyridoxal-5'-phosphate: G74 (≠ A79), R75 (≠ T80), W100 (= W106), T151 (= T156), D172 (= D176), S174 (= S178), Q195 (= Q199), K196 (= K200)
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
40% identity, 97% coverage: 7:364/368 of query aligns to 2:357/359 of 6xdkD
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
40% identity, 97% coverage: 7:364/368 of query aligns to 2:353/355 of 6xdkB
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
38% identity, 96% coverage: 9:361/368 of query aligns to 3:347/349 of 5yb0B
3qm2B 2.25 angstrom crystal structure of phosphoserine aminotransferase (serc) from salmonella enterica subsp. Enterica serovar typhimurium
42% identity, 97% coverage: 8:364/368 of query aligns to 3:329/331 of 3qm2B
Query Sequence
>WP_013820554.1 NCBI__GCF_000214665.1:WP_013820554.1
MMNLQNSLNFSGGPGALPESVLLQLSEELIQVPGLGISILGISHRSEWFAEVISELEDNI
RALLGLNEKYHVLLLQGGATQQFSMVPMTLLRGKSTAAEYIQTGYWSGKAIPEAKLEGPI
RVIWNGRAAGFNRLPTDDELCFSPDAPYIHYISNETVEGLQFQRVLGRDDVPRVCDMSSD
FLSKPGDFERFSLIYAHAQKNIGPSGITVVVVRDELIEQPHAELPSFLDYKTQAKAHSNF
NTPPVFAIYAVLLVTRWLIKDIGGLTQMDRINRRKAELLYGLIDDSDGFYQGRAETADRS
LMNVVFNLPSLELEKRFIQESQAAGFSGLAGHRAIGGLRASIYNAVTIEAVEELVNFMDA
FWRKSVRN
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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