SitesBLAST
Comparing Ga0059261_2265 FitnessBrowser__Korea:Ga0059261_2265 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
25% identity, 96% coverage: 9:369/378 of query aligns to 7:363/368 of 2fyfA
- active site: F101 (= F102), D168 (= D170), K192 (= K194)
- binding tetrachloroplatinate(ii): I321 (≠ L327), A324 (= A331)
- binding pyridoxal-5'-phosphate: A77 (≠ D77), T78 (= T78), W81 (≠ F81), F101 (= F102), 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)
26% identity, 96% coverage: 9:369/378 of query aligns to 14:371/376 of P9WQ73
- T154 (= T147) binding
- D176 (= D170) binding
- Q199 (= Q193) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
24% identity, 81% coverage: 17:321/378 of query aligns to 7:313/360 of 4azjA
- active site: W102 (= W106), D172 (= D170), K196 (= K194)
- binding pyridoxal-5'-phosphate: A76 (≠ D77), S77 (≠ T78), W102 (= W106), T152 (= T147), D172 (= D170), S174 (≠ T172), Q195 (= Q193), K196 (= K194), N237 (= N247), T238 (= T248)
- binding phosphoserine: H41 (= H42), R42 (= R43), W102 (= W106), T152 (= T147), K196 (= K194)
Sites not aligning to the query:
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
24% identity, 81% coverage: 17:321/378 of query aligns to 7:310/357 of 1w23B
- active site: W102 (= W106), D172 (= D170), K196 (= K194)
- binding magnesium ion: Y127 (= Y125), Y154 (≠ S149), H285 (= H296), A286 (= A299)
- binding pyridoxal-5'-phosphate: A76 (≠ D77), S77 (≠ T78), W102 (= W106), T152 (= T147), D172 (= D170), S174 (≠ T172), Q195 (= Q193), K196 (= K194), N234 (= N247), T235 (= T248)
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
23% identity, 88% coverage: 37:367/378 of query aligns to 39:361/370 of Q9Y617
- S43 (= S41) 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 (= H42) binding in other chain
- R45 (= R43) binding in other chain
- Y70 (≠ H68) to N: in NLS2; unknown pathological significance
- G79 (≠ D77) 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 (≠ T78) binding
- P87 (≠ M85) 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 (≠ L97) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ A98) 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
- E155 (≠ G146) to Q: in NLS2; unknown pathological significance
- T156 (= T147) 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 (= N247) binding in other chain
- T242 (= T248) binding in other chain
- C245 (≠ M251) 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 (≠ Y340) binding
- R336 (= R341) binding
- R342 (= R348) 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)
23% identity, 88% coverage: 37:367/378 of query aligns to 35:357/366 of 8a5vE
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
23% identity, 88% coverage: 37:367/378 of query aligns to 34:356/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
23% identity, 88% coverage: 37:367/378 of query aligns to 34:356/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (≠ S76), G74 (≠ D77), C75 (≠ T78), W102 (= W106), T151 (= T147), D171 (= D170), S173 (≠ T172), Q194 (= Q193), K195 (= K194)
- binding phosphoserine: H39 (= H42), R40 (= R43), H330 (≠ Y340), R337 (= R348)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
23% identity, 88% coverage: 37:367/378 of query aligns to 34:356/365 of 8a5vA
3e77A Human phosphoserine aminotransferase in complex with plp
23% identity, 88% coverage: 37:367/378 of query aligns to 32:354/363 of 3e77A
- active site: W100 (= W106), D169 (= D170), K193 (= K194)
- binding pyridoxal-5'-phosphate: G71 (≠ S76), G72 (≠ D77), C73 (≠ T78), W100 (= W106), T149 (= T147), 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, 88% coverage: 37:367/378 of query aligns to 35:356/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H42), R41 (= R43), 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 (≠ S76), G75 (≠ D77), C76 (≠ T78), W103 (= W106), T152 (= T147), S174 (≠ T172), A194 (≠ W192), Q195 (= Q193), N196 (≠ K194), H330 (≠ Y340), R331 (= R341), R337 (= R348), Y341 (≠ G352)
3ffrA Crystal structure of a phosphoserine aminotransferase serc (chu_0995) from cytophaga hutchinsonii atcc 33406 at 1.75 a resolution
25% identity, 53% coverage: 14:214/378 of query aligns to 4:210/361 of 3ffrA
Sites not aligning to the query:
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
25% identity, 55% coverage: 10:217/378 of query aligns to 13:227/381 of 2dr1A
Query Sequence
>Ga0059261_2265 FitnessBrowser__Korea:Ga0059261_2265
MTDLPAAPATKPARPYFSSGPCAKPPGWSADKLHTEVLGRSHRSKLGKTRLQYAIDLMRE
MLKLPDTHRIGIVPGSDTGAFEMAMWTMLGARGVTTLAWESFGEGWVTDAVKQLKLDPTV
IRADYGQLPDLSQVDFADDVLFTWNGTTSGVRVPNGDWIPDDREGLTFADSTSAVFAYDL
PWDKIDVATFSWQKVLGGEGGHGVLILGPRAVERLEQYTPAWPLPKVFRLMAKGKLAEGV
FKGETINTPSMLAVEDAIFALEWAKGLGGLDGLIARSDANAAALDKIVAERDWLGHLAAD
EATRSKTSVCLTVEGADEAFIKTFASLLEKADAAYDVAGYRDAPAGLRIWCGATVDTADI
EALGPWLDWAYASAKASN
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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