SitesBLAST
Comparing 208061 MicrobesOnline__882:208061 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)
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)
31% identity, 91% coverage: 34:418/424 of query aligns to 32:381/384 of P12998
- GF 108:109 (≠ GY 110:111) binding
- H133 (= H135) binding
- S179 (= S216) binding
- H207 (= H244) binding
- T233 (= T273) binding
- K236 (= K276) modified: N6-(pyridoxal phosphate)lysine
- T352 (= T389) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 21 binding
2g6wA Suicide inhibition of a-oxamine synthase: structures of the covalent adducts of 8-amino-7-oxonanoate synthase with trifluoroalanine (see paper)
31% identity, 91% coverage: 34:418/424 of query aligns to 31:380/383 of 2g6wA
- active site: N46 (= N49), H132 (= H135), E174 (= E212), S178 (= S216), D203 (= D241), H206 (= H244), K235 (= K276)
- binding (4-{(e)-[(2,2-difluoroethyl)imino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: N46 (= N49), G107 (= G110), H132 (= H135), E174 (= E212), S178 (= S216), D203 (= D241), A205 (= A243), H206 (= H244), K235 (= K276)
1fc4A 2-amino-3-ketobutyrate coa ligase (see paper)
28% identity, 98% coverage: 1:415/424 of query aligns to 4:388/401 of 1fc4A
- active site: N53 (= N49), H139 (= H135), D184 (≠ E212), S188 (= S216), D213 (= D241), H216 (= H244), K247 (= K276)
- binding 2-amino-3-ketobutyric acid: N53 (= N49), H139 (= H135), S188 (= S216), H216 (= H244), K247 (= K276), R371 (= R398)
- binding pyridoxal-5'-phosphate: S113 (= S109), C114 (≠ G110), F115 (≠ Y111), H139 (= H135), S188 (= S216), D213 (= D241), S215 (≠ A243), H216 (= H244), T244 (= T273), K247 (= K276), F276 (≠ H304), S277 (= S305), N278 (≠ T306)
1djeA Crystal structure of the plp-bound form of 8-amino-7-oxonanoate synthase (see paper)
30% identity, 98% coverage: 5:418/424 of query aligns to 2:380/383 of 1djeA
- active site: N46 (= N49), H132 (= H135), E174 (= E212), S178 (= S216), D203 (= D241), H206 (= H244), K235 (= K276)
- binding pyridoxal-5'-phosphate: G107 (= G110), F108 (≠ Y111), H132 (= H135), E174 (= E212), S178 (= S216), D203 (= D241), A205 (= A243), H206 (= H244), T232 (= T273), K235 (= K276)
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)
30% identity, 98% coverage: 5:418/424 of query aligns to 2:380/383 of 1dj9A
- active site: N46 (= N49), H132 (= H135), E174 (= E212), S178 (= S216), D203 (= D241), H206 (= H244), K235 (= K276)
- binding n-[7-keto-8-aminopelargonic acid]-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: R20 (= R23), G107 (= G110), F108 (≠ Y111), H132 (= H135), E174 (= E212), D203 (= D241), A205 (= A243), H206 (= H244), T232 (= T273), K235 (= K276), I347 (≠ A385), T351 (= T389)
P0AB77 2-amino-3-ketobutyrate coenzyme A ligase; AKB ligase; Glycine acetyltransferase; EC 2.3.1.29 from Escherichia coli (strain K12) (see paper)
28% identity, 98% coverage: 1:415/424 of query aligns to 1:385/398 of P0AB77
- H136 (= H135) binding
- S185 (= S216) binding in other chain
- R368 (= R398) binding
7poaA An irreversible, promiscuous and highly thermostable claisen- condensation biocatalyst drives the synthesis of substituted pyrroles
30% identity, 91% coverage: 23:408/424 of query aligns to 29:378/398 of 7poaA
- binding pyridoxal-5'-phosphate: G113 (= G110), F114 (≠ Y111), H138 (= H135), S140 (= S137), D210 (= D241), A212 (= A243), H213 (= H244), T242 (= T273), K245 (= K276), S274 (= S305), T275 (= T306)
Q5W264 4-hydroxy-2,2'-bipyrrole-5-methanol synthase PigH; HBM synthase; Aminotransferase PigH; EC 2.3.2.- from Serratia sp. (strain ATCC 39006) (see paper)
27% identity, 92% coverage: 22:410/424 of query aligns to 272:620/653 of Q5W264
Sites not aligning to the query:
- 45 S→A: The pyrrolyl-beta-ketoacyl moiety is formed.
- 139 S→A: The pyrrolyl-beta-ketoacyl moiety is formed.
3tqxA Structure of the 2-amino-3-ketobutyrate coenzyme a ligase (kbl) from coxiella burnetii (see paper)
25% identity, 96% coverage: 3:410/424 of query aligns to 2:379/396 of 3tqxA
- active site: N48 (= N49), H134 (= H135), D179 (≠ E212), S183 (= S216), D208 (= D241), H211 (= H244), K242 (= K276)
- binding pyridoxal-5'-phosphate: S108 (= S109), C109 (≠ G110), F110 (≠ Y111), H134 (= H135), D208 (= D241), S210 (≠ A243), H211 (= H244), T239 (= T273), K242 (= K276), F271 (≠ H304), S272 (= S305), N273 (≠ T306)
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)
26% identity, 96% coverage: 9:415/424 of query aligns to 31:406/419 of Q0P5L8
- K265 (= K276) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
7v58B Structural insights into the substrate selectivity of acyl-coa transferase (see paper)
27% identity, 92% coverage: 17:406/424 of query aligns to 19:378/400 of 7v58B
2x8uA Sphingomonas wittichii serine palmitoyltransferase (see paper)
25% identity, 88% coverage: 37:410/424 of query aligns to 40:381/399 of 2x8uA
- active site: Y52 (≠ N49), H138 (= H135), E181 (= E212), S185 (= S216), D210 (= D241), H213 (= H244), K244 (= K276)
- binding pyridoxal-5'-phosphate: G113 (= G110), Y114 (= Y111), N117 (= N114), H138 (= H135), S140 (= S137), D210 (= D241), A212 (= A243), H213 (= H244), T241 (= T273), S243 (≠ G275), K244 (= K276), T273 (≠ S305), A274 (≠ T306)
Q93UV0 Serine palmitoyltransferase; SPT; EC 2.3.1.50 from Sphingomonas paucimobilis (Pseudomonas paucimobilis) (see 4 papers)
25% identity, 93% coverage: 13:406/424 of query aligns to 31:398/420 of Q93UV0
- N100 (≠ T76) 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 110:111) binding
- H234 (= H244) binding
- T262 (= T273) binding
- S264 (≠ G275) binding
- K265 (= K276) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of activity.
- R378 (= R386) 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)
25% identity, 93% coverage: 13:406/424 of query aligns to 10:377/398 of 2xbnA
- active site: Y52 (≠ N49), H138 (= H135), E181 (= E212), S185 (= S216), D210 (= D241), H213 (= H244), K244 (= K276)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G110), Y114 (= Y111), H138 (= H135), D210 (= D241), T241 (= T273), S243 (≠ G275), K244 (= K276)
2w8jA Spt with plp-ser (see paper)
25% identity, 93% coverage: 13:406/424 of query aligns to 10:377/398 of 2w8jA
- active site: Y52 (≠ N49), H138 (= H135), E181 (= E212), S185 (= S216), D210 (= D241), H213 (= H244), K244 (= K276)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: G113 (= G110), Y114 (= Y111), H138 (= H135), D210 (= D241), A212 (= A243), H213 (= H244), T241 (= T273), S243 (≠ G275), K244 (= K276), R357 (= R386)
Sites not aligning to the query:
7bxsA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator glycine binding form
27% identity, 96% coverage: 2:407/424 of query aligns to 4:379/399 of 7bxsA
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S112 (= S109), A113 (≠ G110), F114 (≠ Y111), H138 (= H135), S187 (= S216), D212 (= D241), C214 (≠ A243), H215 (= H244), T243 (= T273), F275 (≠ H304), S276 (= S305), N277 (≠ T306), R370 (= R398)
7bxrA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator 3- hydroxynorvaline binding form
27% identity, 96% coverage: 2:407/424 of query aligns to 4:379/399 of 7bxrA
- binding (2S,3R)-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]-3-oxidanyl-pentanoic acid: N52 (= N49), S112 (= S109), A113 (≠ G110), F114 (≠ Y111), H138 (= H135), S187 (= S216), D212 (= D241), C214 (≠ A243), H215 (= H244), T243 (= T273), L274 (≠ M303), F275 (≠ H304), S276 (= S305), N277 (≠ T306), R370 (= R398)
7bxqA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator l-threonine binding form
27% identity, 96% coverage: 2:407/424 of query aligns to 4:379/399 of 7bxqA
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-allothreonine: N52 (= N49), A113 (≠ G110), F114 (≠ Y111), H138 (= H135), S187 (= S216), D212 (= D241), C214 (≠ A243), H215 (= H244), T243 (= T273), F275 (≠ H304), S276 (= S305), N277 (≠ T306), R370 (= R398)
4bmkA Serine palmitoyltransferase k265a from s. Paucimobilis with bound plp- myriocin aldimine (see paper)
24% identity, 93% coverage: 13:406/424 of query aligns to 10:377/398 of 4bmkA
- active site: Y52 (≠ N49), H138 (= H135), E181 (= E212), S185 (= S216), D210 (= D241), H213 (= H244), A244 (≠ K276)
- binding Decarboxylated Myriocin: Y52 (≠ N49), H138 (= H135), I271 (≠ M303), F272 (≠ H304), T273 (≠ S305)
- binding pyridoxal-5'-phosphate: G113 (= G110), Y114 (= Y111), H138 (= H135), E181 (= E212), D210 (= D241), H213 (= H244), T241 (= T273), S243 (≠ G275), T273 (≠ S305), A274 (≠ T306)
7yjoB Cryo-em structure of the monomeric atspt-orm1 (lcb2a-deltan5) complex (see paper)
24% identity, 87% coverage: 42:410/424 of query aligns to 93:445/467 of 7yjoB
Sites not aligning to the query:
Query Sequence
>208061 MicrobesOnline__882:208061
MAHPFLHRLTLRLDAQRAAGLDRTVMTPETRTTRHVILDGQRLCNFASNDYLGLADDAAW
RAEVADCFARHPASGTASRLAAGHSALVAEAEAAWAEHFGYESCLFLPSGYQANLAVVTG
LLHTGDTLFIDRRIHASMARAVPLCGAHPVTYPHGDLARLDRRLTAWRHETTAETASAAP
LTEGAPLSSPPATCPTASPPPHGDASPVILTESLFSMDGTVTSMDALATLRSRHGAFVIL
DEAHACGALGQGGRGLAWGQTENAPAADVIVGTLGKGPGFFGAFVLMPRIVRESLENFAS
AVMHSTALPEAHAAAVLRLLPRMAGMDDARARLARNARALREGLAGCGLPVHGDAHILCI
ETGDEAQATQLARRLRTQGVLALSARHPTVPHGHAIVRFSVTAAHTDDDITYCKETVHTC
LHTR
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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