SitesBLAST
Comparing WP_011840115.1 NCBI__GCF_000015985.1:WP_011840115.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
P9WQ73 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
26% identity, 97% coverage: 1:375/385 of query aligns to 1:374/376 of P9WQ73
- M1 (= M1) modified: Initiator methionine, Removed
- T154 (= T146) binding
- D176 (= D169) binding
- Q199 (= Q192) binding
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
26% identity, 97% coverage: 4:375/385 of query aligns to 2:366/368 of 2fyfA
- active site: F101 (≠ K111), D168 (= D169), K192 (= K193)
- binding tetrachloroplatinate(ii): L2 (= L4), I321 (≠ R330), A324 (≠ K333)
- binding pyridoxal-5'-phosphate: A77 (≠ D76), T78 (= T77), W81 (≠ V80), F101 (≠ K111), T147 (= T146), D168 (= D169), T170 (= T171), Q191 (= Q192), K192 (= K193), N243 (= N246), T244 (= T247)
Sites not aligning to the query:
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
26% identity, 83% coverage: 10:330/385 of query aligns to 14:332/381 of 2dr1A
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
20% identity, 89% coverage: 37:377/385 of query aligns to 40:368/370 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 ; 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
- P87 (≠ M84) 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 (≠ L96) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ A97) 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 (= W105) binding
- E155 (≠ G145) to Q: in NLS2; uncertain significance
- T156 (= T146) binding
- D176 (= D169) binding
- S179 (= S172) 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 (= Q192) binding
- K200 (= K193) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N246) binding in other chain
- T242 (= T247) binding in other chain
- C245 (≠ M250) 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 (≠ Y343) binding
- R336 (= R344) binding
- R342 (= R351) 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)
20% identity, 89% coverage: 37:377/385 of query aligns to 35:363/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
20% identity, 89% coverage: 37:377/385 of query aligns to 35:363/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (≠ S75), G74 (≠ D76), C75 (≠ T77), W102 (= W105), T151 (= T146), D171 (= D169), S173 (≠ T171), Q194 (= Q192), K195 (= K193)
- binding phosphoserine: H39 (= H41), R40 (= R42), H330 (≠ Y343), R337 (= R351)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
20% identity, 89% coverage: 37:377/385 of query aligns to 35:363/365 of 8a5vA
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
20% identity, 89% coverage: 37:377/385 of query aligns to 36:364/366 of 8a5vE
3e77A Human phosphoserine aminotransferase in complex with plp
20% identity, 89% coverage: 37:377/385 of query aligns to 33:361/363 of 3e77A
- active site: W100 (= W105), D169 (= D169), K193 (= K193)
- binding pyridoxal-5'-phosphate: G71 (≠ S75), G72 (≠ D76), C73 (≠ T77), W100 (= W105), T149 (= T146), D169 (= D169), S171 (≠ T171), Q192 (= Q192), K193 (= K193), N234 (= N246), T235 (= T247)
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
20% identity, 89% coverage: 37:377/385 of query aligns to 36:363/365 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 (= N246), T237 (= T247)
- 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 (= W105), T152 (= T146), S174 (≠ T171), A194 (≠ W191), Q195 (= Q192), N196 (≠ K193), H330 (≠ Y343), R331 (= R344), R337 (= R351), Y341 (≠ G355)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
21% identity, 64% coverage: 40:287/385 of query aligns to 40:275/357 of 1w23B
- active site: W102 (= W105), D172 (= D169), K196 (= K193)
- binding magnesium ion: Y127 (= Y124), Y154 (≠ S148)
- binding pyridoxal-5'-phosphate: A76 (≠ G78), S77 (≠ A79), W102 (= W105), T152 (= T146), D172 (= D169), S174 (≠ T171), Q195 (= Q192), K196 (= K193), N234 (= N246), T235 (= T247)
Sites not aligning to the query:
Query Sequence
>WP_011840115.1 NCBI__GCF_000015985.1:WP_011840115.1
MSDLQTPAARPANPRFSSGPCAKIPAYSLDLLSDAPLGRSHRAAVGKAKLKEAIDLTREI
LGVPEGYRIGIVPGSDTGAVEMAMWSLLGARPVEMLAWESFGEGWVTDAVKQLKLDATVR
KAAYGEIVDLAQVDFTRDVVFTWNGTTSGVRLPDGDAIPADREGLTICDATSAAFAMDLP
WDKLDVVTFSWQKVLGGEGGHGMLILSPRAVERLESYTPAWPMPKIFRMTKGGKLIEGIF
QGETINTPSMLAVEDYLVSLKWAQRIGGLKALVARAEANSKVVADFVAAHDWIANLAVDP
ATASTTSVCLKFTDPRIADGAAFAKAVAKRLEKEGVALDVGAYRDAPAGLRIWCGSTVET
ADVAALMPWIEWAFEAEIAALAKAA
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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