SitesBLAST
Comparing 8500251 FitnessBrowser__Miya:8500251 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2g6wA Suicide inhibition of a-oxamine synthase: structures of the covalent adducts of 8-amino-7-oxonanoate synthase with trifluoroalanine (see paper)
32% identity, 81% coverage: 65:427/446 of query aligns to 36:379/383 of 2g6wA
- active site: N46 (= N75), H132 (= H161), E174 (= E223), S178 (= S227), D203 (= D252), H206 (= H255), K235 (= K281)
- binding (4-{(e)-[(2,2-difluoroethyl)imino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: N46 (= N75), G107 (= G136), H132 (= H161), E174 (= E223), S178 (= S227), D203 (= D252), A205 (= A254), H206 (= H255), K235 (= K281)
P12998 8-amino-7-oxononanoate synthase; AONS; 7-keto-8-amino-pelargonic acid synthase; 7-KAP synthase; KAPA synthase; 8-amino-7-ketopelargonate synthase; EC 2.3.1.47 from Escherichia coli (strain K12) (see 2 papers)
32% identity, 81% coverage: 65:427/446 of query aligns to 37:380/384 of P12998
- GF 108:109 (≠ GY 136:137) binding
- H133 (= H161) binding
- S179 (= S227) binding
- H207 (= H255) binding
- T233 (= T278) binding
- K236 (= K281) modified: N6-(pyridoxal phosphate)lysine
- T352 (= T399) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 21 binding
1djeA Crystal structure of the plp-bound form of 8-amino-7-oxonanoate synthase (see paper)
32% identity, 81% coverage: 65:427/446 of query aligns to 36:379/383 of 1djeA
- active site: N46 (= N75), H132 (= H161), E174 (= E223), S178 (= S227), D203 (= D252), H206 (= H255), K235 (= K281)
- binding pyridoxal-5'-phosphate: G107 (= G136), F108 (≠ Y137), H132 (= H161), E174 (= E223), S178 (= S227), D203 (= D252), A205 (= A254), H206 (= H255), T232 (= T278), K235 (= K281)
1dj9A Crystal structure of 8-amino-7-oxonanoate synthase (or 7-keto- 8aminipelargonate or kapa synthase) complexed with plp and the product 8(s)-amino-7-oxonanonoate (or kapa). The enzyme of biotin biosynthetic pathway. (see paper)
32% identity, 81% coverage: 65:427/446 of query aligns to 36:379/383 of 1dj9A
- active site: N46 (= N75), H132 (= H161), E174 (= E223), S178 (= S227), D203 (= D252), H206 (= H255), K235 (= K281)
- binding n-[7-keto-8-aminopelargonic acid]-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G107 (= G136), F108 (≠ Y137), H132 (= H161), E174 (= E223), D203 (= D252), A205 (= A254), H206 (= H255), T232 (= T278), K235 (= K281), I347 (≠ A395), T351 (= T399)
Sites not aligning to the query:
Q0P5L8 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial; AKB ligase; Aminoacetone synthase; Glycine acetyltransferase; EC 2.3.1.29 from Bos taurus (Bovine) (see paper)
29% identity, 82% coverage: 62:425/446 of query aligns to 58:406/419 of Q0P5L8
- K265 (= K281) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
Q93UV0 Serine palmitoyltransferase; SPT; EC 2.3.1.50 from Sphingomonas paucimobilis (Pseudomonas paucimobilis) (see 4 papers)
28% identity, 81% coverage: 55:415/446 of query aligns to 55:397/420 of Q93UV0
- N100 (≠ T102) mutation to C: 23-fold decrease in catalytic efficiency for L-serine.; mutation to W: 147-fold decrease in catalytic efficiency for L-serine. Affects the chemistry of the pyridoxal phosphate.; mutation to Y: 410-fold decrease in catalytic efficiency for L-serine. Affects the chemistry of the pyridoxal phosphate. Is less able to stabilize a quinonoid intermediate.
- GY 134:135 (= GY 136:137) binding
- H234 (= H255) binding
- T262 (= T278) binding
- S264 (≠ G280) binding
- K265 (= K281) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of activity.
- R378 (= R396) mutation to A: 40-fold decrease in catalytic efficiency for L-serine. Is less able to stabilize a quinonoid intermediate.; mutation to N: 60-fold decrease in catalytic efficiency for L-serine.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2xbnA Inhibition of the plp-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation (see paper)
28% identity, 81% coverage: 55:415/446 of query aligns to 34:376/398 of 2xbnA
- active site: Y52 (≠ N75), H138 (= H161), E181 (= E223), S185 (= S227), D210 (= D252), H213 (= H255), K244 (= K281)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G136), Y114 (= Y137), H138 (= H161), D210 (= D252), T241 (= T278), S243 (≠ G280), K244 (= K281)
2w8jA Spt with plp-ser (see paper)
28% identity, 81% coverage: 55:415/446 of query aligns to 34:376/398 of 2w8jA
- active site: Y52 (≠ N75), H138 (= H161), E181 (= E223), S185 (= S227), D210 (= D252), H213 (= H255), K244 (= K281)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: G113 (= G136), Y114 (= Y137), H138 (= H161), D210 (= D252), A212 (= A254), H213 (= H255), T241 (= T278), S243 (≠ G280), K244 (= K281), R357 (= R396)
Sites not aligning to the query:
3tqxA Structure of the 2-amino-3-ketobutyrate coenzyme a ligase (kbl) from coxiella burnetii (see paper)
27% identity, 85% coverage: 56:433/446 of query aligns to 29:392/396 of 3tqxA
- active site: N48 (= N75), H134 (= H161), D179 (≠ E223), S183 (= S227), D208 (= D252), H211 (= H255), K242 (= K281)
- binding pyridoxal-5'-phosphate: S108 (= S135), C109 (≠ G136), F110 (≠ Y137), H134 (= H161), D208 (= D252), S210 (≠ A254), H211 (= H255), T239 (= T278), K242 (= K281), F271 (≠ H309), S272 (= S310), N273 (≠ T311)
4bmkA Serine palmitoyltransferase k265a from s. Paucimobilis with bound plp- myriocin aldimine (see paper)
28% identity, 81% coverage: 55:415/446 of query aligns to 34:376/398 of 4bmkA
- active site: Y52 (≠ N75), H138 (= H161), E181 (= E223), S185 (= S227), D210 (= D252), H213 (= H255), A244 (≠ K281)
- binding Decarboxylated Myriocin: Y52 (≠ N75), H138 (= H161), I271 (= I308), F272 (≠ H309), T273 (≠ S310)
- binding pyridoxal-5'-phosphate: G113 (= G136), Y114 (= Y137), H138 (= H161), E181 (= E223), D210 (= D252), H213 (= H255), T241 (= T278), S243 (≠ G280), T273 (≠ S310), A274 (≠ T311)
7bxsA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator glycine binding form
27% identity, 93% coverage: 18:433/446 of query aligns to 7:395/399 of 7bxsA
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S112 (= S135), A113 (≠ G136), F114 (≠ Y137), H138 (= H161), S187 (= S227), D212 (= D252), C214 (≠ A254), H215 (= H255), T243 (= T278), F275 (≠ H309), S276 (= S310), N277 (≠ T311), R370 (= R408)
7bxrA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator 3- hydroxynorvaline binding form
27% identity, 93% coverage: 18:433/446 of query aligns to 7:395/399 of 7bxrA
- binding (2S,3R)-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]-3-oxidanyl-pentanoic acid: N52 (= N75), S112 (= S135), A113 (≠ G136), F114 (≠ Y137), H138 (= H161), S187 (= S227), D212 (= D252), C214 (≠ A254), H215 (= H255), T243 (= T278), L274 (≠ I308), F275 (≠ H309), S276 (= S310), N277 (≠ T311), R370 (= R408)
7bxqA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator l-threonine binding form
27% identity, 93% coverage: 18:433/446 of query aligns to 7:395/399 of 7bxqA
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-allothreonine: N52 (= N75), A113 (≠ G136), F114 (≠ Y137), H138 (= H161), S187 (= S227), D212 (= D252), C214 (≠ A254), H215 (= H255), T243 (= T278), F275 (≠ H309), S276 (= S310), N277 (≠ T311), R370 (= R408)
7u7hA Cysteate acyl-acp transferase from alistipes finegoldii (see paper)
28% identity, 80% coverage: 66:424/446 of query aligns to 44:392/423 of 7u7hA
2x8uA Sphingomonas wittichii serine palmitoyltransferase (see paper)
28% identity, 84% coverage: 56:430/446 of query aligns to 35:391/399 of 2x8uA
- active site: Y52 (≠ N75), H138 (= H161), E181 (= E223), S185 (= S227), D210 (= D252), H213 (= H255), K244 (= K281)
- binding pyridoxal-5'-phosphate: G113 (= G136), Y114 (= Y137), N117 (= N140), H138 (= H161), S140 (= S163), D210 (= D252), A212 (= A254), H213 (= H255), T241 (= T278), S243 (≠ G280), K244 (= K281), T273 (≠ S310), A274 (≠ T311)
1fc4A 2-amino-3-ketobutyrate coa ligase (see paper)
26% identity, 83% coverage: 65:433/446 of query aligns to 43:396/401 of 1fc4A
- active site: N53 (= N75), H139 (= H161), D184 (≠ E223), S188 (= S227), D213 (= D252), H216 (= H255), K247 (= K281)
- binding 2-amino-3-ketobutyric acid: N53 (= N75), H139 (= H161), S188 (= S227), H216 (= H255), K247 (= K281), R371 (= R408)
- binding pyridoxal-5'-phosphate: S113 (= S135), C114 (≠ G136), F115 (≠ Y137), H139 (= H161), S188 (= S227), D213 (= D252), S215 (≠ A254), H216 (= H255), T244 (= T278), K247 (= K281), F276 (≠ H309), S277 (= S310), N278 (≠ T311)
P0AB77 2-amino-3-ketobutyrate coenzyme A ligase; AKB ligase; Glycine acetyltransferase; EC 2.3.1.29 from Escherichia coli (strain K12) (see paper)
26% identity, 83% coverage: 65:433/446 of query aligns to 40:393/398 of P0AB77
- H136 (= H161) binding
- S185 (= S227) binding in other chain
- R368 (= R408) binding
7poaA An irreversible, promiscuous and highly thermostable claisen- condensation biocatalyst drives the synthesis of substituted pyrroles
28% identity, 85% coverage: 55:432/446 of query aligns to 32:392/398 of 7poaA
- binding pyridoxal-5'-phosphate: G113 (= G136), F114 (≠ Y137), H138 (= H161), S140 (= S163), D210 (= D252), A212 (= A254), H213 (= H255), T242 (= T278), K245 (= K281), S274 (= S310), T275 (= T311)
8h29A Serine palmitoyltransferase from sphingobacterium multivorum complexed with l-threonine (see paper)
23% identity, 92% coverage: 26:435/446 of query aligns to 15:393/394 of 8h29A
8h21A Serine palmitoyltransferase from sphingobacterium multivorum complexed with l-alanine (see paper)
23% identity, 92% coverage: 26:435/446 of query aligns to 15:393/394 of 8h21A
Query Sequence
>8500251 FitnessBrowser__Miya:8500251
MSGATPAAAPPPASPGLLAARLALRVEELHAAGLGRNALPLDGLPAPTSRSAAGQSPSPA
LVRMEGRPLLHFAGNDYLGLAADEDWRATVAACFARHAPSGTASRLAAGHTALTAEAETA
WADYFGYAECLFLPSGYQANLALLWGLLGHGDAVFLDRRVHASMAHALPPTGARLHTHRH
ADMDDLSRRLAAWRHNSDNDSGGHDGPPACGTACAPQPVVLAESLYSMDGTLPDMARLGA
VTREHGAFVIVDEAHAFGTLGAGGRGRAHGVADVAVGTLGKALGLFGAFLLLPRGTRNAL
ENLASPLIHSTALPEAHAACCLALLDLLPRLDDRRHHLAALGAALRTGLRAEGVPAREGA
HVVCVDVGDEDRCTRLAARLRTPADGGPGVLALAARHPTVPRGAATLRLGLTALHRVDDV
ARCVDLLARAWKEEEEKRGDAPGDQA
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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