SitesBLAST
Comparing WP_012851206.1 NCBI__GCF_000024385.1:WP_012851206.1 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 20 (the maximum) hits to proteins with known functional sites (download)
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
67% identity, 99% coverage: 6:370/370 of query aligns to 4:368/368 of 2fyfA
- active site: F101 (= F103), D168 (= D170), K192 (= K194)
- binding tetrachloroplatinate(ii): I321 (≠ T323), A324 (= A326)
- binding pyridoxal-5'-phosphate: A77 (≠ T79), T78 (= T80), W81 (= W83), F101 (= F103), T147 (= T149), D168 (= D170), T170 (= T172), Q191 (= Q193), K192 (= K194), N243 (= N245), T244 (= T246)
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)
67% identity, 99% coverage: 6:370/370 of query aligns to 11:376/376 of P9WQ73
- T154 (= T149) binding
- D176 (= D170) binding
- Q199 (= Q193) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3ffrA Crystal structure of a phosphoserine aminotransferase serc (chu_0995) from cytophaga hutchinsonii atcc 33406 at 1.75 a resolution
25% identity, 94% coverage: 17:363/370 of query aligns to 7:356/361 of 3ffrA
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
23% identity, 94% coverage: 16:363/370 of query aligns to 3:344/349 of 5yb0B
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
25% identity, 95% coverage: 16:368/370 of query aligns to 9:366/370 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 (≠ T79) 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 (≠ T80) binding
- P87 (≠ A87) 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 (≠ S95) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ Q96) 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 (≠ F103) binding
- E155 (= E148) to Q: in NLS2; uncertain significance
- T156 (= T149) binding
- D176 (= D170) binding
- 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
- K200 (= K194) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N245) binding in other chain
- T242 (= T246) binding in other chain
- C245 (≠ V249) 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 (≠ Y335) binding
- R336 (= R336) binding
- R342 (= R344) 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
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
25% identity, 95% coverage: 16:368/370 of query aligns to 4:361/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
25% identity, 95% coverage: 16:368/370 of query aligns to 4:361/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G78), G74 (≠ T79), C75 (≠ T80), W102 (≠ F103), T151 (= T149), D171 (= D170), S173 (≠ T172), Q194 (= Q193), K195 (= K194)
- binding phosphoserine: H39 (= H44), R40 (= R45), H330 (≠ Y335), R337 (= R344)
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
25% identity, 95% coverage: 16:368/370 of query aligns to 5:362/366 of 8a5vE
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
25% identity, 95% coverage: 16:368/370 of query aligns to 4:361/365 of 8a5vA
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
24% identity, 95% coverage: 16:368/370 of query aligns to 5:361/365 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 (= N245), T237 (= T246)
- 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 (≠ T79), C76 (≠ T80), W103 (≠ F103), T152 (= T149), S174 (≠ T172), A194 (≠ P192), Q195 (= Q193), N196 (≠ K194), H330 (≠ Y335), R331 (= R336), R337 (= R344), Y341 (≠ F348)
3e77A Human phosphoserine aminotransferase in complex with plp
25% identity, 90% coverage: 36:368/370 of query aligns to 29:359/363 of 3e77A
- active site: W100 (≠ F103), D169 (= D170), K193 (= K194)
- binding pyridoxal-5'-phosphate: G71 (= G78), G72 (≠ T79), C73 (≠ T80), W100 (≠ F103), T149 (= T149), D169 (= D170), S171 (≠ T172), Q192 (= Q193), K193 (= K194), N234 (= N245), T235 (= T246)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
23% identity, 93% coverage: 16:360/370 of query aligns to 4:348/359 of 3qboB
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
23% identity, 95% coverage: 16:365/370 of query aligns to 6:355/361 of 1bt4A
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
24% identity, 94% coverage: 16:361/370 of query aligns to 5:350/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G78), A75 (≠ T79), T76 (= T80), W101 (≠ F103), T151 (= T149), D171 (= D170), S173 (≠ T172), Q194 (= Q193), K195 (= K194), N236 (= N245), T237 (= T246)
- binding phosphoserine: W101 (≠ F103), T151 (= T149), K195 (= K194), H326 (≠ Y335), R327 (= R336), R333 (= R344)
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
24% identity, 94% coverage: 16:361/370 of query aligns to 7:352/362 of 6czyA
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
24% identity, 94% coverage: 16:361/370 of query aligns to 75:420/430 of Q96255
- AT 145:146 (≠ TT 79:80) binding
- W171 (≠ F103) binding
- T221 (= T149) binding
- D241 (= D170) binding
- Q264 (= Q193) binding
- K265 (= K194) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 245:246) binding
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
21% identity, 98% coverage: 10:370/370 of query aligns to 13:375/381 of 2dr1A
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
23% identity, 95% coverage: 16:368/370 of query aligns to 4:354/360 of 1bjoA
- active site: W100 (≠ F103), D172 (= D170), K196 (= K194)
- binding alpha-methyl-l-glutamic acid: S7 (≠ C19), W100 (≠ F103), T151 (= T149), K196 (= K194)
- binding pyridoxal-5'-phosphate: G74 (≠ T79), R75 (≠ T80), W100 (≠ F103), T151 (= T149), D172 (= D170), S174 (≠ T172), Q195 (= Q193), K196 (= K194)
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
23% identity, 81% coverage: 12:309/370 of query aligns to 17:317/383 of 3kgxA
Sites not aligning to the query:
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
23% identity, 81% coverage: 12:309/370 of query aligns to 21:322/388 of 3kgwB
Query Sequence
>WP_012851206.1 NCBI__GCF_000024385.1:WP_012851206.1
MTEIVIPADLKPADGRFGCGPSKVRPEQLRALAESGAAYLGTSHRQAPVKSLVRRVREGL
AELFSLPEGYRVLLSNGGTTAFWDAAAFGLIRRKSQHLTFGEFSSKFAKVAKAAPWLEEP
SLISAEPGSHPLPRAEDGVDVYALTHNETSTGVAMPIQRVGGEDSLVLVDATSGAGGLPV
DITQADVYYFAPQKCFASDGGLWVALVSPAALERIEQIASSDRYIPEFFNLKTVIDNSAK
DQTYNTPAVATLLLFAEQIEWMNAQGGLAWTTARTADSAQRLYTWAEKSSYATPFVADPA
QRSQVVGTIDFVDSVDAAAVAKTLRANGIVDTEPYRKLGRNQLRIGMFPAVDPADVEALT
ACIDYVVERL
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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