SitesBLAST
Comparing GFF898 FitnessBrowser__Phaeo:GFF898 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)
7poaA An irreversible, promiscuous and highly thermostable claisen- condensation biocatalyst drives the synthesis of substituted pyrroles
36% identity, 91% coverage: 27:369/379 of query aligns to 44:385/398 of 7poaA
- binding pyridoxal-5'-phosphate: G113 (= G97), F114 (= F98), H138 (= H122), S140 (= S124), D210 (= D197), A212 (= A199), H213 (= H200), T242 (= T227), K245 (= K230), S274 (≠ A259), T275 (= T260)
P18079 5-aminolevulinate synthase; 5-aminolevulinic acid synthase; Delta-ALA synthase; Delta-aminolevulinate synthase; EC 2.3.1.37 from Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) (see paper)
34% identity, 91% coverage: 9:354/379 of query aligns to 8:376/409 of P18079
- R21 (= R22) binding
- S137 (≠ Y117) binding
- K156 (≠ T136) binding
- S189 (= S172) binding in other chain
- H217 (= H200) binding in other chain
- T245 (= T227) binding in other chain
- K248 (= K230) active site
- S277 (≠ A259) binding
- T278 (= T260) binding
- T365 (= T343) binding
1djeA Crystal structure of the plp-bound form of 8-amino-7-oxonanoate synthase (see paper)
36% identity, 95% coverage: 13:371/379 of query aligns to 17:379/383 of 1djeA
- active site: N46 (= N35), H132 (= H122), E174 (= E168), S178 (= S172), D203 (= D197), H206 (= H200), K235 (= K230)
- binding pyridoxal-5'-phosphate: G107 (= G97), F108 (= F98), H132 (= H122), E174 (= E168), S178 (= S172), D203 (= D197), A205 (= A199), H206 (= H200), T232 (= T227), K235 (= K230)
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)
36% identity, 95% coverage: 13:371/379 of query aligns to 17:379/383 of 1dj9A
- active site: N46 (= N35), H132 (= H122), E174 (= E168), S178 (= S172), D203 (= D197), H206 (= H200), K235 (= K230)
- binding n-[7-keto-8-aminopelargonic acid]-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: R20 (= R16), G107 (= G97), F108 (= F98), H132 (= H122), E174 (= E168), D203 (= D197), A205 (= A199), H206 (= H200), T232 (= T227), K235 (= K230), I347 (= I339), T351 (= T343)
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)
36% identity, 93% coverage: 19:371/379 of query aligns to 31:380/384 of P12998
- GF 108:109 (= GF 97:98) binding
- H133 (= H122) binding
- S179 (= S172) binding
- H207 (= H200) binding
- T233 (= T227) binding
- K236 (= K230) modified: N6-(pyridoxal phosphate)lysine
- T352 (= T343) 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)
36% identity, 93% coverage: 19:371/379 of query aligns to 30:379/383 of 2g6wA
- active site: N46 (= N35), H132 (= H122), E174 (= E168), S178 (= S172), D203 (= D197), H206 (= H200), K235 (= K230)
- binding (4-{(e)-[(2,2-difluoroethyl)imino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: N46 (= N35), G107 (= G97), H132 (= H122), E174 (= E168), S178 (= S172), D203 (= D197), A205 (= A199), H206 (= H200), K235 (= K230)
2bwoB 5-aminolevulinate synthase from rhodobacter capsulatus in complex with succinyl-coa (see paper)
33% identity, 91% coverage: 9:354/379 of query aligns to 8:376/399 of 2bwoB
- active site: N54 (= N35), H142 (= H122), E185 (= E168), S189 (= S172), D214 (= D197), H217 (= H200), K248 (= K230)
- binding pyridoxal-5'-phosphate: S114 (≠ G96), A115 (≠ G97), Y116 (≠ F98), H142 (= H122), E185 (= E168), S189 (= S172), D214 (= D197), V216 (≠ A199), H217 (= H200), T245 (= T227), K248 (= K230)
- binding succinyl-coenzyme a: R21 (= R22), T83 (≠ S65), N85 (≠ L67), S137 (≠ Y117), S139 (≠ A119), H142 (= H122), I146 (≠ H126), K150 (≠ R130), K156 (≠ T136), I158 (≠ S138), F276 (= F258), F363 (≠ P341), P364 (= P342), T365 (= T343)
2bwpA 5-aminolevulinate synthase from rhodobacter capsulatus in complex with glycine (see paper)
33% identity, 91% coverage: 9:354/379 of query aligns to 8:376/398 of 2bwpA
- active site: N54 (= N35), H142 (= H122), E185 (= E168), S189 (= S172), D214 (= D197), H217 (= H200), K248 (= K230)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: N54 (= N35), A115 (≠ G97), Y116 (≠ F98), H142 (= H122), E185 (= E168), D214 (= D197), V216 (≠ A199), H217 (= H200), T245 (= T227), K248 (= K230), S277 (≠ A259), T278 (= T260)
1fc4A 2-amino-3-ketobutyrate coa ligase (see paper)
34% identity, 88% coverage: 31:363/379 of query aligns to 49:383/401 of 1fc4A
- active site: N53 (= N35), H139 (= H122), D184 (≠ E168), S188 (= S172), D213 (= D197), H216 (= H200), K247 (= K230)
- binding 2-amino-3-ketobutyric acid: N53 (= N35), H139 (= H122), S188 (= S172), H216 (= H200), K247 (= K230), R371 (= R352)
- binding pyridoxal-5'-phosphate: S113 (≠ G96), C114 (≠ G97), F115 (= F98), H139 (= H122), S188 (= S172), D213 (= D197), S215 (≠ A199), H216 (= H200), T244 (= T227), K247 (= K230), F276 (= F258), S277 (≠ A259), N278 (≠ T260)
P0AB77 2-amino-3-ketobutyrate coenzyme A ligase; AKB ligase; Glycine acetyltransferase; EC 2.3.1.29 from Escherichia coli (strain K12) (see paper)
34% identity, 88% coverage: 31:363/379 of query aligns to 46:380/398 of P0AB77
- H136 (= H122) binding
- S185 (= S172) binding in other chain
- R368 (= R352) binding
2xbnA Inhibition of the plp-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation (see paper)
32% identity, 92% coverage: 27:373/379 of query aligns to 44:393/398 of 2xbnA
- active site: Y52 (≠ N35), H138 (= H122), E181 (= E168), S185 (= S172), D210 (= D197), H213 (= H200), K244 (= K230)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G97), Y114 (≠ F98), H138 (= H122), D210 (= D197), T241 (= T227), S243 (≠ G229), K244 (= K230)
2w8jA Spt with plp-ser (see paper)
32% identity, 92% coverage: 27:373/379 of query aligns to 44:393/398 of 2w8jA
- active site: Y52 (≠ N35), H138 (= H122), E181 (= E168), S185 (= S172), D210 (= D197), H213 (= H200), K244 (= K230)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: G113 (= G97), Y114 (≠ F98), H138 (= H122), D210 (= D197), A212 (= A199), H213 (= H200), T241 (= T227), S243 (≠ G229), K244 (= K230), R357 (= R340)
Sites not aligning to the query:
Q93UV0 Serine palmitoyltransferase; SPT; EC 2.3.1.50 from Sphingomonas paucimobilis (Pseudomonas paucimobilis) (see 4 papers)
32% identity, 92% coverage: 27:373/379 of query aligns to 65:414/420 of Q93UV0
- N100 (≠ G63) 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 (≠ GF 97:98) binding
- H234 (= H200) binding
- T262 (= T227) binding
- S264 (≠ G229) binding
- K265 (= K230) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of activity.
- R378 (= R340) 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
2x8uA Sphingomonas wittichii serine palmitoyltransferase (see paper)
31% identity, 91% coverage: 34:379/379 of query aligns to 51:399/399 of 2x8uA
- active site: Y52 (≠ N35), H138 (= H122), E181 (= E168), S185 (= S172), D210 (= D197), H213 (= H200), K244 (= K230)
- binding pyridoxal-5'-phosphate: G113 (= G97), Y114 (≠ F98), N117 (= N101), H138 (= H122), S140 (= S124), D210 (= D197), A212 (= A199), H213 (= H200), T241 (= T227), S243 (≠ G229), K244 (= K230), T273 (≠ A259), A274 (≠ T260)
4bmkA Serine palmitoyltransferase k265a from s. Paucimobilis with bound plp- myriocin aldimine (see paper)
31% identity, 92% coverage: 27:373/379 of query aligns to 44:393/398 of 4bmkA
- active site: Y52 (≠ N35), H138 (= H122), E181 (= E168), S185 (= S172), D210 (= D197), H213 (= H200), A244 (≠ K230)
- binding Decarboxylated Myriocin: Y52 (≠ N35), H138 (= H122), I271 (= I257), F272 (= F258), T273 (≠ A259)
- binding pyridoxal-5'-phosphate: G113 (= G97), Y114 (≠ F98), H138 (= H122), E181 (= E168), D210 (= D197), H213 (= H200), T241 (= T227), S243 (≠ G229), T273 (≠ A259), A274 (≠ T260)
3tqxA Structure of the 2-amino-3-ketobutyrate coenzyme a ligase (kbl) from coxiella burnetii (see paper)
32% identity, 88% coverage: 31:363/379 of query aligns to 44:379/396 of 3tqxA
- active site: N48 (= N35), H134 (= H122), D179 (≠ E168), S183 (= S172), D208 (= D197), H211 (= H200), K242 (= K230)
- binding pyridoxal-5'-phosphate: S108 (≠ G96), C109 (≠ G97), F110 (= F98), H134 (= H122), D208 (= D197), S210 (≠ A199), H211 (= H200), T239 (= T227), K242 (= K230), F271 (= F258), S272 (≠ A259), N273 (≠ T260)
Q8GW43 8-amino-7-oxononanoate synthase; AONS; 7-keto-8-amino-pelargonic acid synthase; 7-KAP synthase; KAPA synthase; 8-amino-7-ketopelargonate synthase; Biotin synthase 4; Biotin synthase F; AtbioF; EC 2.3.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 89% coverage: 18:356/379 of query aligns to 98:440/476 of Q8GW43
Sites not aligning to the query:
- 474:476 Peroxisomal targeting signal PTS1; mutation Missing: Incorrect cytosolic localization and loss of biotin synthase activity.
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)
33% identity, 86% coverage: 32:356/379 of query aligns to 290:612/653 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.
3a2bA Crystal structure of serine palmitoyltransferase from sphingobacterium multivorum with substrate l-serine (see paper)
29% identity, 96% coverage: 12:373/379 of query aligns to 15:387/392 of 3a2bA
- active site: N51 (= N35), H137 (= H122), D180 (≠ E168), S184 (= S172), D209 (= D197), H212 (= H200), K243 (= K230)
- binding pyridoxal-5'-phosphate: G112 (= G97), F113 (= F98), H137 (= H122), D209 (= D197), A211 (= A199), H212 (= H200), T240 (= T227), S242 (≠ G229), K243 (= K230)
- binding serine: H137 (= H122), K243 (= K230)
8h29A Serine palmitoyltransferase from sphingobacterium multivorum complexed with l-threonine (see paper)
29% identity, 96% coverage: 12:373/379 of query aligns to 15:387/394 of 8h29A
Query Sequence
>GFF898 FitnessBrowser__Phaeo:GFF898
MAGAFPRHETSLEALRNRGRYRHLMPRDGHDFASNDYLGLAGSDVLHAAAADALARGVPV
GAGGSRLLRGNDAEHQLLEAEAAAFFGTEAALFMGGGFTANQAIFSTLPQQGDLVLYDAL
IHASTHDGMRLGRAETRSFAHGDVEDASRVLKAWRAEGGTGQVWIAVEAVYSMDGDLAPL
DALMALADADGAVLVVDEAHSTGVFGDLGRGLAQGIAHRQNVLSLHTCGKALGASGALIC
GQKVLIETLINKARGFIFATAPSPLNAALVRAALAELQQNTGRREQAWQGITHAQAEAKR
LCGLDGFQSQILPVVIGDDKRTMALASAMQGHGYDIRGIRPPTVPRGTARLRLSITLNTP
EQVITDMFEDLARERETRP
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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