SitesBLAST
Comparing WP_012384268.1 NCBI__GCF_000019845.1:WP_012384268.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
23% identity, 96% coverage: 7:381/390 of query aligns to 7:367/368 of 2fyfA
- active site: F101 (= F100), D168 (= D169), K192 (= K193)
- binding tetrachloroplatinate(ii): I321 (≠ L335), A324 (≠ K338)
- binding pyridoxal-5'-phosphate: A77 (≠ D75), T78 (= T76), W81 (≠ V79), F101 (= F100), T147 (= T146), D168 (= D169), T170 (= T171), Q191 (= Q192), K192 (= K193), N243 (= N246), T244 (= T247)
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)
23% identity, 96% coverage: 7:381/390 of query aligns to 14:375/376 of P9WQ73
- T154 (= T146) binding pyridoxal 5'-phosphate
- D176 (= D169) binding pyridoxal 5'-phosphate
- Q199 (= Q192) binding pyridoxal 5'-phosphate
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
23% identity, 75% coverage: 15:308/390 of query aligns to 7:302/361 of 3ffrA
Sites not aligning to the query:
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
22% identity, 77% coverage: 15:314/390 of query aligns to 10:309/370 of Q9Y617
- S43 (= S39) 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 (= H40) binding in other chain
- R45 (= R41) binding in other chain
- Y70 (= Y66) to N: in NLS2; uncertain significance
- G79 (≠ D75) 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 (≠ T76) binding pyridoxal 5'-phosphate
- P87 (≠ E80) 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 (≠ V92) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (= D93) 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 (= W97) binding pyridoxal 5'-phosphate
- E155 (≠ G145) to Q: in NLS2; uncertain significance
- T156 (= T146) binding pyridoxal 5'-phosphate
- D176 (= D169) binding pyridoxal 5'-phosphate
- 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 pyridoxal 5'-phosphate
- 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
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
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
22% identity, 77% coverage: 15:314/390 of query aligns to 5:304/365 of 8a5wC
Sites not aligning to the query:
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
22% identity, 77% coverage: 15:314/390 of query aligns to 5:304/365 of 8a5wA
Sites not aligning to the query:
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
22% identity, 77% coverage: 15:314/390 of query aligns to 5:304/365 of 8a5vA
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
22% identity, 77% coverage: 15:314/390 of query aligns to 6:305/366 of 8a5vE
Sites not aligning to the query:
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
22% identity, 77% coverage: 15:314/390 of query aligns to 6:304/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H40), R41 (= R41), 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 (≠ S74), G75 (≠ D75), C76 (≠ T76), W103 (= W97), T152 (= T146), S174 (≠ T171), A194 (≠ W191), Q195 (= Q192), N196 (≠ K193)
Sites not aligning to the query:
3e77A Human phosphoserine aminotransferase in complex with plp
22% identity, 72% coverage: 34:314/390 of query aligns to 31:302/363 of 3e77A
- active site: W100 (= W97), D169 (= D169), K193 (= K193)
- binding pyridoxal-5'-phosphate: G71 (≠ S74), G72 (≠ D75), C73 (≠ T76), W100 (= W97), T149 (= T146), D169 (= D169), S171 (≠ T171), Q192 (= Q192), K193 (= K193), N234 (= N246), T235 (= T247)
Query Sequence
>WP_012384268.1 NCBI__GCF_000019845.1:WP_012384268.1
MTDTLPAARPANACFSSGPCAKRPGWTLSALQDAALGRSHRAKIGKTKLKLAIDLTREIL
QVPEDYRIGIVPGSDTGAVEMALWTLLGARGVDVLAWESFGQGWVTDIVKQLKLPNVRSL
KAGYGEIVDLATVDFNNDVVFTWNGTTSGVKVPNGDWIAADRQGLTICDATSAAFAQKLD
WPKLDVVTFSWQKVLGGEAAHGMLILSPRAVERLTTYTPAWPLPKVFRLTSGGKLTEGIF
VGETINTPSMLCVEDYIDALNWGKTVGGLEGLIARADANTKAIADWVEKTPWIDFLAADP
AIRSNTSVCLKVSDPAITALSDEAQAAFAKTLASLLEKEKVAYDIGAYRDAPPGLRIWCG
ATVETSDIIALTAWLDYAYAKAKSDLPKAA
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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