SitesBLAST
Comparing WP_012066838.1 NCBI__GCF_000017145.1:WP_012066838.1 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 11 hits to proteins with known functional sites (download)
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
24% identity, 95% coverage: 8:381/392 of query aligns to 7:366/368 of 2fyfA
- active site: F101 (= F101), D168 (= D170), K192 (= K194)
- binding tetrachloroplatinate(ii): I321 (≠ L337), A324 (≠ E340)
- binding pyridoxal-5'-phosphate: A77 (≠ D76), T78 (= T77), W81 (≠ V80), F101 (= F101), T147 (= T147), D168 (= D170), T170 (= T172), Q191 (= Q193), K192 (= K194), N243 (= N247), T244 (= T248)
Sites not aligning to the query:
P9WQ73 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
24% identity, 95% coverage: 8:381/392 of query aligns to 14:374/376 of P9WQ73
- T154 (= T147) binding pyridoxal 5'-phosphate
- D176 (= D170) binding pyridoxal 5'-phosphate
- Q199 (= Q193) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
21% identity, 71% coverage: 37:313/392 of query aligns to 40:307/370 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 (≠ D76) 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 (≠ T77) binding pyridoxal 5'-phosphate
- P87 (≠ E81) 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 (≠ V93) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (= D94) 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 (≠ F101) binding pyridoxal 5'-phosphate
- E155 (≠ S149) to Q: in NLS2; uncertain significance
- T156 (≠ G150) 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 (= N247) binding in other chain
- T242 (= T248) binding in other chain
- C245 (= C253) 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
Sites not aligning to the query:
- 335 binding O-phospho-L-serine
- 336 binding O-phospho-L-serine
- 342 binding O-phospho-L-serine; R → 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)
21% identity, 71% coverage: 37:313/392 of query aligns to 36:303/366 of 8a5vE
Sites not aligning to the query:
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
21% identity, 71% coverage: 37:313/392 of query aligns to 35:302/365 of 8a5wC
Sites not aligning to the query:
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
21% identity, 71% coverage: 37:313/392 of query aligns to 35:302/365 of 8a5wA
Sites not aligning to the query:
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
21% identity, 71% coverage: 37:313/392 of query aligns to 35:302/365 of 8a5vA
3e77A Human phosphoserine aminotransferase in complex with plp
21% identity, 71% coverage: 37:313/392 of query aligns to 33:300/363 of 3e77A
- active site: W100 (≠ F101), D169 (= D170), K193 (= K194)
- binding pyridoxal-5'-phosphate: G71 (≠ S75), G72 (≠ D76), C73 (≠ T77), W100 (≠ F101), T149 (≠ G150), D169 (= D170), S171 (≠ T172), Q192 (= Q193), K193 (= K194), N234 (= N247), T235 (= T248)
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
22% identity, 71% coverage: 37:313/392 of query aligns to 36:302/365 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 (= N247), T237 (= T248)
- 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 (≠ S75), G75 (≠ D76), C76 (≠ T77), W103 (≠ F101), T152 (≠ G150), S174 (≠ T172), A194 (≠ W192), Q195 (= Q193), N196 (≠ K194)
Sites not aligning to the query:
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
22% identity, 78% coverage: 15:319/392 of query aligns to 6:306/357 of 1w23B
- active site: W102 (= W105), D172 (= D170), K196 (= K194)
- binding magnesium ion: Y127 (= Y125), Y154 (≠ S149), H285 (≠ L297), A286 (= A298)
- binding pyridoxal-5'-phosphate: A76 (≠ D76), S77 (≠ T77), W102 (= W105), T152 (= T147), D172 (= D170), S174 (≠ T172), Q195 (= Q193), K196 (= K194), N234 (= N247), T235 (= T248)
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
23% identity, 78% coverage: 15:319/392 of query aligns to 6:309/360 of 4azjA
- active site: W102 (= W105), D172 (= D170), K196 (= K194)
- binding pyridoxal-5'-phosphate: A76 (≠ D76), S77 (≠ T77), W102 (= W105), T152 (= T147), D172 (= D170), S174 (≠ T172), Q195 (= Q193), K196 (= K194), N237 (= N247), T238 (= T248)
- binding phosphoserine: H41 (= H41), R42 (= R42), W102 (= W105), T152 (= T147), K196 (= K194)
Sites not aligning to the query:
Query Sequence
>WP_012066838.1 NCBI__GCF_000017145.1:WP_012066838.1
MTKPAKPAQRPANTHFSSGPCAKRPGWTLEALSDAPLGRSHRAKIGKTKLKQAIDLTREI
LEVPADYRIGIVPASDTGAVEMALWSMLGARGVDMLAWESFGSGWVTDVVKQLKLADVRR
LEADYGELPDLSRVDFDRDVVFTWNGTTSGVRVPDADFIPSGRKGLTICDATSAAFAQAL
DFAKLDVVTFSWQKVLGGEGAHGVLILSPRAVERLETYVPAWPLPKIFRMTKGGKLIEGI
FTGETINTPSMLCVEDYIDALLWAKSVGGLKGLTARADANAEVIHRFVAANDWIVNLAVK
PETRSNTSVCLRIVDGDVSALDADAQGAFAKGVVALLEKEGVAFDIGHYRDAPSGLRIWA
GATIETSDMEALMPWLAWAFETQKATLSQVAA
Or try a new SitesBLAST search
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