SitesBLAST
Comparing Pf1N1B4_351 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_351 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)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
57% identity, 100% coverage: 1:292/292 of query aligns to 67:359/359 of 3qboB
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
56% identity, 100% coverage: 1:292/292 of query aligns to 67:360/360 of 1bjoA
- active site: W100 (= W34), D172 (= D104), K196 (= K128)
- binding alpha-methyl-l-glutamic acid: W100 (= W34), T151 (= T84), K196 (= K128)
- binding pyridoxal-5'-phosphate: G74 (≠ A8), R75 (≠ S9), W100 (= W34), T151 (= T84), D172 (= D104), S174 (= S106), Q195 (= Q127), K196 (= K128)
Sites not aligning to the query:
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
54% identity, 100% coverage: 1:292/292 of query aligns to 67:360/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G7), G74 (≠ A8), R75 (≠ S9), W100 (= W34), T151 (= T84), D172 (= D104), S174 (= S106), Q195 (= Q127), K196 (= K128), N237 (= N169), T238 (= T170)
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
49% identity, 100% coverage: 1:292/292 of query aligns to 69:361/361 of 1bt4A
3e77A Human phosphoserine aminotransferase in complex with plp
51% identity, 100% coverage: 1:291/292 of query aligns to 65:361/363 of 3e77A
- active site: W100 (= W34), D169 (= D104), K193 (= K128)
- binding pyridoxal-5'-phosphate: G71 (= G7), G72 (≠ A8), C73 (≠ S9), W100 (= W34), T149 (= T84), D169 (= D104), S171 (= S106), Q192 (= Q127), K193 (= K128), N234 (= N169), T235 (= T170)
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
51% identity, 100% coverage: 1:291/292 of query aligns to 67:363/365 of 8a5wC
Sites not aligning to the query:
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
51% identity, 100% coverage: 1:291/292 of query aligns to 67:363/365 of 8a5wA
Sites not aligning to the query:
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
51% identity, 100% coverage: 1:291/292 of query aligns to 67:363/365 of 8a5vA
3qm2B 2.25 angstrom crystal structure of phosphoserine aminotransferase (serc) from salmonella enterica subsp. Enterica serovar typhimurium
53% identity, 100% coverage: 1:292/292 of query aligns to 45:331/331 of 3qm2B
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
51% identity, 100% coverage: 1:291/292 of query aligns to 72:368/370 of Q9Y617
- G79 (≠ A8) 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 (≠ S9) binding
- P87 (= P16) 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 (= A26) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (= D27) 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 (= W34) binding
- E155 (= E83) to Q: in NLS2; unknown pathological significance
- T156 (= T84) binding
- D176 (= D104) binding
- S179 (= S107) 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 (= Q127) binding
- K200 (= K128) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N169) binding in other chain
- T242 (= T170) binding in other chain
- C245 (≠ T173) 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 (= H258) binding
- R336 (= R259) binding
- R342 (= R265) 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
Sites not aligning to the query:
- 43 S → 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
- 44 binding in other chain
- 45 binding in other chain
- 70 Y → N: in NLS2; unknown pathological significance
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
51% identity, 100% coverage: 1:291/292 of query aligns to 68:364/366 of 8a5vE
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
49% identity, 100% coverage: 1:292/292 of query aligns to 138:430/430 of Q96255
- AT 145:146 (≠ AS 8:9) binding
- W171 (= W34) binding
- T221 (= T84) binding
- D241 (= D104) binding
- Q264 (= Q127) binding
- K265 (= K128) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 169:170) binding
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
49% identity, 100% coverage: 1:292/292 of query aligns to 68:360/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G7), A75 (= A8), T76 (≠ S9), W101 (= W34), T151 (= T84), D171 (= D104), S173 (= S106), Q194 (= Q127), K195 (= K128), N236 (= N169), T237 (= T170)
- binding phosphoserine: W101 (= W34), T151 (= T84), K195 (= K128), H326 (= H258), R327 (= R259), R333 (= R265)
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
49% identity, 100% coverage: 1:292/292 of query aligns to 70:362/362 of 6czyA
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
51% identity, 100% coverage: 1:291/292 of query aligns to 68:363/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: N236 (= N169), T237 (= T170)
- 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 (= G7), G75 (≠ A8), C76 (≠ S9), W103 (= W34), T152 (= T84), S174 (= S106), A194 (= A126), Q195 (= Q127), N196 (= N129), H330 (= H258), R331 (= R259), R337 (= R265), Y341 (= Y269)
Sites not aligning to the query:
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
50% identity, 99% coverage: 1:289/292 of query aligns to 69:358/360 of 4azjA
- active site: W102 (= W34), D172 (= D104), K196 (= K128)
- binding pyridoxal-5'-phosphate: A76 (= A8), S77 (= S9), W102 (= W34), T152 (= T84), D172 (= D104), S174 (= S106), Q195 (= Q127), K196 (= K128), N237 (= N169), T238 (= T170)
- binding phosphoserine: W102 (= W34), T152 (= T84), K196 (= K128), H327 (= H258), R328 (= R259), R334 (= R265)
Sites not aligning to the query:
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
50% identity, 99% coverage: 1:289/292 of query aligns to 69:355/357 of 1w23B
- active site: W102 (= W34), D172 (= D104), K196 (= K128)
- binding magnesium ion: Y127 (= Y59), Y154 (≠ G86), H285 (≠ P219), A286 (≠ I220)
- binding pyridoxal-5'-phosphate: A76 (= A8), S77 (= S9), W102 (= W34), T152 (= T84), D172 (= D104), S174 (= S106), Q195 (= Q127), K196 (= K128), N234 (= N169), T235 (= T170)
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
49% identity, 100% coverage: 1:292/292 of query aligns to 67:359/359 of 6xdkD
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
48% identity, 100% coverage: 1:292/292 of query aligns to 67:355/355 of 6xdkB
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
44% identity, 99% coverage: 1:289/292 of query aligns to 65:349/349 of 5yb0B
Query Sequence
>Pf1N1B4_351 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_351
VLFLQGGASQQFAQIPLNLLPESGTADYIDTGIWSQKAIEEASRYGHVNVAATAKPYDYF
AIPGQNEWKLSKDAAYVHYAPNETIGGLEFQWIPETGDVPLVADMSSDILSRPVDVSRFG
MIYAGAQKNIGPSGIVVNIVREDLLGHARSICPTMLNYKVAADNGSMYNTPPTLAWYLSG
LVFEWLKEQGGVEAIGKLNEVKQRTLYDFIDASGLYSNPINKSDRSWMNVPFRLADDRLD
KPFLAGADERGLLNLKGHRSVGGMRASIYNAVDIVAVNALVSYMAEFEKEHG
Or try a new SitesBLAST search
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