SitesBLAST
Comparing WP_015798934.1 NCBI__GCF_000023265.1:WP_015798934.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) 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)
56% identity, 96% coverage: 7:372/382 of query aligns to 9:376/376 of P9WQ73
- T154 (= T152) binding pyridoxal 5'-phosphate
- D176 (= D172) binding pyridoxal 5'-phosphate
- Q199 (= Q195) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
56% identity, 96% coverage: 7:372/382 of query aligns to 2:368/368 of 2fyfA
- active site: F101 (= F106), D168 (= D172), K192 (= K196)
- binding tetrachloroplatinate(ii): L2 (≠ I7), I321 (≠ V325), A324 (≠ S328)
- binding pyridoxal-5'-phosphate: A77 (= A82), T78 (= T83), W81 (= W86), F101 (= F106), T147 (= T152), D168 (= D172), T170 (= T174), Q191 (= Q195), K192 (= K196), N243 (= N247), T244 (= T248)
Sites not aligning to the query:
3ffrA Crystal structure of a phosphoserine aminotransferase serc (chu_0995) from cytophaga hutchinsonii atcc 33406 at 1.75 a resolution
27% identity, 90% coverage: 20:361/382 of query aligns to 7:352/361 of 3ffrA
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
24% identity, 70% coverage: 20:286/382 of query aligns to 4:266/349 of 5yb0B
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
24% identity, 94% coverage: 15:372/382 of query aligns to 15:375/381 of 2dr1A
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
22% identity, 90% coverage: 20:361/382 of query aligns to 6:348/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G81), A75 (= A82), T76 (= T83), W101 (≠ F106), T151 (= T152), D171 (= D172), S173 (≠ T174), Q194 (= Q195), K195 (= K196), N236 (= N247), T237 (= T248)
- binding phosphoserine: W101 (≠ F106), T151 (= T152), K195 (= K196), H326 (≠ Y337), R327 (= R338), R333 (= R346)
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
22% identity, 90% coverage: 19:361/382 of query aligns to 7:350/362 of 6czyA
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
22% identity, 90% coverage: 19:361/382 of query aligns to 75:418/430 of Q96255
- AT 145:146 (= AT 82:83) binding pyridoxal 5'-phosphate
- W171 (≠ F106) binding pyridoxal 5'-phosphate
- T221 (= T152) binding pyridoxal 5'-phosphate
- D241 (= D172) binding pyridoxal 5'-phosphate
- Q264 (= Q195) binding pyridoxal 5'-phosphate
- K265 (= K196) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 247:248) binding pyridoxal 5'-phosphate
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
23% identity, 90% coverage: 20:361/382 of query aligns to 7:349/361 of 1bt4A
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
21% identity, 90% coverage: 19:361/382 of query aligns to 9:357/370 of Q9Y617
- S43 (= S46) 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 (= H47) binding in other chain
- R45 (= R48) binding in other chain
- Y70 (= Y73) to N: in NLS2; uncertain significance
- G79 (≠ A82) 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 (≠ T83) binding pyridoxal 5'-phosphate
- P87 (≠ A90) 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 (≠ S98) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ Q99) 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 (≠ F106) binding pyridoxal 5'-phosphate
- E155 (= E151) to Q: in NLS2; uncertain significance
- T156 (= T152) binding pyridoxal 5'-phosphate
- D176 (= D172) binding pyridoxal 5'-phosphate
- S179 (= S175) 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 (= Q195) binding pyridoxal 5'-phosphate
- K200 (= K196) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N247) binding in other chain
- T242 (= T248) binding in other chain
- C245 (≠ I251) 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 (≠ Y337) binding O-phospho-L-serine
- R336 (= R338) binding O-phospho-L-serine
- R342 (= R346) binding O-phospho-L-serine; 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, 90% coverage: 19:361/382 of query aligns to 5:353/366 of 8a5vE
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
21% identity, 90% coverage: 19:361/382 of query aligns to 4:352/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
21% identity, 90% coverage: 19:361/382 of query aligns to 4:352/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G81), G74 (≠ A82), C75 (≠ T83), W102 (≠ F106), T151 (= T152), D171 (= D172), S173 (≠ T174), Q194 (= Q195), K195 (= K196)
- binding phosphoserine: H39 (= H47), R40 (= R48), H330 (≠ Y337), R337 (= R346)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
21% identity, 90% coverage: 19:361/382 of query aligns to 4:352/365 of 8a5vA
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
22% identity, 90% coverage: 19:361/382 of query aligns to 5:352/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H47), R41 (= R48), 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 (= G81), G75 (≠ A82), C76 (≠ T83), W103 (≠ F106), T152 (= T152), S174 (= S175), A194 (= A199), Q195 (≠ S200), N196 (≠ D201), H330 (≠ Y337), R331 (= R338), R337 (= R346), Y341 (≠ F350)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
22% identity, 90% coverage: 20:363/382 of query aligns to 5:349/359 of 3qboB
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
21% identity, 91% coverage: 19:365/382 of query aligns to 6:353/360 of 4azjA
- active site: W102 (≠ F106), D172 (≠ A173), K196 (= K196)
- binding pyridoxal-5'-phosphate: A76 (= A82), S77 (≠ T83), W102 (≠ F106), T152 (= T161), D172 (≠ A173), S174 (= S175), Q195 (= Q195), K196 (= K196), N237 (= N247), T238 (= T248)
- binding phosphoserine: H41 (= H47), R42 (= R48), W102 (≠ F106), T152 (= T161), K196 (= K196), H327 (≠ Y337), R328 (= R338), R334 (= R346)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
21% identity, 91% coverage: 19:365/382 of query aligns to 6:350/357 of 1w23B
- active site: W102 (≠ F106), D172 (≠ A173), K196 (= K196)
- binding magnesium ion: Y127 (≠ A136), Y154 (vs. gap), H285 (vs. gap), A286 (= A299)
- binding pyridoxal-5'-phosphate: A76 (= A82), S77 (≠ T83), W102 (≠ F106), T152 (= T161), D172 (≠ A173), S174 (= S175), Q195 (= Q195), K196 (= K196), N234 (= N247), T235 (= T248)
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
22% identity, 90% coverage: 19:363/382 of query aligns to 4:350/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G81), G74 (≠ A82), R75 (≠ T83), W100 (≠ F106), T151 (= T152), D172 (= D172), S174 (≠ T174), Q195 (= Q195), K196 (= K196), N237 (= N247), T238 (= T248)
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
24% identity, 86% coverage: 5:334/382 of query aligns to 12:339/377 of 1vjoA
Query Sequence
>WP_015798934.1 NCBI__GCF_000023265.1:WP_015798934.1
MPDADAIRLPSNLLPSDGRFGSGPSRIPPSHLEALAATGTTLMGTSHRRPTVRGLVASVQ
EGLAELFSAPEGYEIILGNGGATLFWDAAAYSMIEHKSQHLAFGEFSSKFASVVAATPHL
DEPDVRRAEAGSAPAAEPNPAVDTYALTQNETSTGVTTQVTRPSEDGLVLVDATSAAGAI
VFDPSQVDAYYFSPQKAFASDGGLFVAMLSPRAIERIERIAASGRAIPATLSLLTALENA
RLNQTYNTPAIATLFLMDLQIKALLELGGLKGANERSRQASDVLYAWATTHAHATPFVAD
PALRSPVTVTIDFDDTVDAKALAAVLRSNGIVDVEPYRKLGRNQLRIATFPATPVADVER
LRDAIDWVIERLADDARAPQTA
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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