SitesBLAST
Comparing BPHYT_RS03235 FitnessBrowser__BFirm:BPHYT_RS03235 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)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
46% identity, 95% coverage: 5:247/256 of query aligns to 4:247/247 of 7borA
- active site: N63 (= N64), F68 (= F69), D77 (≠ H78), G81 (≠ F82), I105 (= I106), T108 (= T109), F128 (= F129), L133 (= L134), P135 (= P136), E136 (= E137), A222 (≠ S222), L232 (= L232)
- binding coenzyme a: D21 (= D22), K22 (= K23), A25 (= A26), S61 (≠ A62), I65 (≠ L66), V103 (= V104), F128 (= F129), L131 (= L132), F244 (= F244), R247 (≠ K247)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
40% identity, 97% coverage: 5:253/256 of query aligns to 5:255/257 of 6slbAAA
- active site: Q64 (≠ N64), F69 (= F69), L80 (≠ A79), N84 (vs. gap), A108 (≠ I106), S111 (≠ T109), A130 (≠ P128), F131 (= F129), L136 (= L134), P138 (= P136), D139 (≠ E137), A224 (≠ S222), G234 (≠ L232)
- binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (≠ G58), A62 (= A62), Q64 (≠ N64), D65 (= D65), L66 (= L66), Y76 (≠ G76), A108 (≠ I106), F131 (= F129), D139 (≠ E137)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
39% identity, 97% coverage: 5:253/256 of query aligns to 2:243/245 of 6slaAAA
- active site: Q61 (≠ N64), L68 (≠ A79), N72 (vs. gap), A96 (≠ I106), S99 (≠ T109), A118 (≠ P128), F119 (= F129), L124 (= L134), P126 (= P136), N127 (≠ E137), A212 (≠ S222), G222 (≠ L232)
- binding ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ K24), A59 (= A62), Q61 (≠ N64), D62 (= D65), L63 (= L66), L68 (≠ A79), Y71 (≠ F82), A94 (≠ V104), G95 (= G105), A96 (≠ I106), F119 (= F129), I122 (≠ L132), L124 (= L134), N127 (≠ E137), F234 (= F244), K237 (= K247)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 97% coverage: 5:252/256 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (≠ N64), M69 (≠ F69), T75 (≠ M75), F79 (≠ A79), G103 (≠ I106), E106 (≠ T109), P125 (= P128), E126 (≠ F129), V131 (≠ L134), P133 (= P136), G134 (≠ E137), L219 (≠ S222), F229 (≠ L232)
- binding Butyryl Coenzyme A: F225 (= F228), F241 (= F244)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 97% coverage: 5:252/256 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (≠ N64), M70 (≠ F69), T80 (≠ H78), F84 (= F82), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (≠ L134), P138 (= P136), G139 (≠ E137), L224 (≠ S222), F234 (≠ L232)
- binding acetoacetyl-coenzyme a: Q23 (≠ D22), A24 (≠ K23), L25 (≠ K24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (≠ N64), D66 (= D65), I67 (≠ L66), K68 (≠ E67), M70 (≠ F69), F84 (= F82), G107 (= G105), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), P138 (= P136), G139 (≠ E137), M140 (≠ A138)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 97% coverage: 5:252/256 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (≠ N64), M70 (≠ F69), T80 (≠ H78), F84 (= F82), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (≠ L134), P138 (= P136), G139 (≠ E137), L224 (≠ S222), F234 (≠ L232)
- binding coenzyme a: L25 (≠ K24), A63 (= A62), I67 (≠ L66), K68 (≠ E67), Y104 (≠ A102), P130 (= P128), E131 (≠ F129), L134 (= L132)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 97% coverage: 5:252/256 of query aligns to 5:253/256 of 3h81A
- active site: A64 (≠ N64), M69 (≠ F69), T79 (≠ H78), F83 (= F82), G107 (≠ I106), E110 (≠ T109), P129 (= P128), E130 (≠ F129), V135 (≠ L134), P137 (= P136), G138 (≠ E137), L223 (≠ S222), F233 (≠ L232)
- binding calcium ion: F233 (≠ L232), Q238 (≠ A237)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
30% identity, 97% coverage: 5:253/256 of query aligns to 6:257/259 of 5zaiC
- active site: A65 (≠ N64), F70 (= F69), S82 (vs. gap), R86 (vs. gap), G110 (≠ I106), E113 (≠ T109), P132 (= P128), E133 (≠ F129), I138 (≠ L134), P140 (= P136), G141 (≠ E137), A226 (≠ S222), F236 (≠ L232)
- binding coenzyme a: K24 (= K23), L25 (≠ K24), A63 (= A62), G64 (= G63), A65 (≠ N64), D66 (= D65), I67 (≠ L66), P132 (= P128), R166 (≠ A162), F248 (= F244), K251 (= K247)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 98% coverage: 4:254/256 of query aligns to 9:265/266 of O53561
- K135 (≠ S124) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 124:131, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ Q131) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
33% identity, 98% coverage: 4:255/256 of query aligns to 9:256/260 of 2uzfA
- active site: G70 (≠ N64), R80 (≠ P74), L84 (≠ F82), G108 (≠ I106), V111 (≠ T109), T130 (≠ P128), G131 (≠ F129), S136 (≠ L134), D138 (≠ P136), A139 (≠ E137), A225 (≠ S222), Y233 (≠ L232)
- binding acetoacetyl-coenzyme a: V28 (≠ K23), R29 (≠ K24), S68 (≠ A62), G69 (= G63), G70 (≠ N64), D71 (= D65), Y104 (≠ A102), G108 (≠ I106)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
32% identity, 98% coverage: 4:255/256 of query aligns to 14:269/273 of Q5HH38
- R34 (≠ K24) binding in other chain
- SGGDQ 73:77 (≠ AGNDL 62:66) binding in other chain
- S149 (≠ L134) binding in other chain
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
30% identity, 98% coverage: 4:255/256 of query aligns to 21:264/268 of 4elxA
- active site: G83 (≠ N64), H88 (= H78), L92 (≠ F82), G116 (≠ I106), V119 (≠ T109), G139 (≠ F129), S144 (≠ L134), D146 (≠ P136), G147 (≠ E137), A233 (≠ Q218), Y241 (vs. gap)
- binding chloride ion: G115 (= G105), G139 (≠ F129), W167 (≠ L157)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
30% identity, 98% coverage: 4:255/256 of query aligns to 21:263/267 of 4elwA
- active site: G83 (≠ N64), L91 (≠ F82), G115 (≠ I106), V118 (≠ T109), G138 (≠ F129), S143 (≠ L134), D145 (≠ P136), G146 (≠ E137), A232 (≠ Q218), Y240 (vs. gap)
- binding nitrate ion: G114 (= G105), T137 (≠ P128), G138 (≠ F129), F144 (≠ C135), W166 (≠ L157)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
29% identity, 93% coverage: 16:253/256 of query aligns to 20:256/258 of 1mj3A
- active site: A68 (≠ N64), M73 (= M70), S83 (≠ P80), L85 (≠ F82), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ L134), P139 (= P136), G140 (≠ E137), K225 (vs. gap), F235 (≠ L232)
- binding hexanoyl-coenzyme a: K26 (≠ D22), A27 (≠ K23), L28 (≠ K24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (≠ N64), D69 (= D65), I70 (≠ L66), G109 (≠ I106), P131 (= P128), E132 (≠ F129), L135 (= L132), G140 (≠ E137)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 98% coverage: 4:255/256 of query aligns to 24:281/285 of 4i42A
- active site: G86 (≠ N64), R91 (vs. gap), Y97 (≠ M70), H105 (= H78), L109 (≠ F82), G133 (≠ I106), V136 (≠ T109), G156 (≠ F129), S161 (≠ L134), D163 (≠ P136), G164 (≠ E137), A250 (≠ Q218), Y258 (vs. gap)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K23), R45 (≠ K24), S84 (≠ A62), G85 (= G63), G86 (≠ N64), D87 (= D65), Q88 (≠ L66), K89 (≠ E67), Y97 (≠ M70), V108 (= V81), Y129 (≠ A102), G133 (≠ I106), T155 (≠ P128), S161 (≠ L134), T254 (≠ S222), F270 (= F244), K273 (= K247)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 98% coverage: 4:255/256 of query aligns to 24:281/285 of P0ABU0
- R45 (≠ K24) binding in other chain
- SGGDQK 84:89 (≠ AGNDLE 62:67) binding in other chain
- K89 (≠ E67) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (vs. gap) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ M70) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAVGI 102:106) binding in other chain
- Q154 (≠ L127) mutation to A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold.
- QTG 154:156 (≠ LPF 127:129) binding
- T155 (≠ P128) binding in other chain
- G156 (≠ F129) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L134) binding in other chain
- W184 (≠ L157) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (vs. gap) binding
- R267 (≠ F241) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F244) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K247) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 98% coverage: 4:255/256 of query aligns to 20:277/281 of 3t88A
- active site: G82 (≠ N64), R87 (vs. gap), Y93 (≠ M70), H101 (= H78), L105 (≠ F82), G129 (≠ I106), V132 (≠ T109), G152 (≠ F129), S157 (≠ L134), D159 (≠ P136), G160 (≠ E137), A246 (≠ Q218), Y254 (vs. gap)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D22), V40 (≠ K23), R41 (≠ K24), A43 (= A26), S80 (≠ A62), G81 (= G63), G82 (≠ N64), D83 (= D65), Q84 (≠ L66), K85 (≠ E67), Y93 (≠ M70), V104 (= V81), L105 (≠ F82), Y125 (≠ A102), G129 (≠ I106), T151 (≠ P128), V155 (≠ L132), F158 (≠ C135), D159 (≠ P136), T250 (≠ S222), Y254 (vs. gap), F266 (= F244), K269 (= K247)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
29% identity, 93% coverage: 16:253/256 of query aligns to 19:252/254 of 2dubA
- active site: A67 (≠ N64), M72 (≠ F69), S82 (≠ Q83), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), T133 (≠ L134), P135 (= P136), G136 (≠ E137), K221 (vs. gap), F231 (≠ L232)
- binding octanoyl-coenzyme a: K25 (≠ D22), A26 (≠ K23), L27 (≠ K24), A29 (= A26), A65 (= A62), A67 (≠ N64), D68 (= D65), I69 (≠ L66), K70 (≠ E67), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), G136 (≠ E137), A137 (= A138)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
31% identity, 98% coverage: 4:255/256 of query aligns to 20:262/266 of 3h02A
- active site: G82 (≠ N64), H86 (= H78), L90 (≠ F82), G114 (≠ I106), V117 (≠ T109), G137 (≠ F129), S142 (≠ L134), D144 (≠ P136), G145 (≠ E137), A231 (≠ Q218), Y239 (vs. gap)
- binding bicarbonate ion: G113 (= G105), Q135 (≠ L127), G137 (≠ F129), W165 (≠ L157)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 93% coverage: 16:253/256 of query aligns to 18:256/258 of 1ey3A
- active site: A66 (≠ N64), M71 (≠ F69), S81 (≠ A79), L85 (vs. gap), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ L134), P139 (= P136), G140 (≠ E137), K225 (vs. gap), F235 (≠ L232)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D22), L26 (≠ K24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (≠ N64), D67 (= D65), I68 (≠ L66), L85 (vs. gap), W88 (≠ L85), G109 (≠ I106), P131 (= P128), L135 (= L132), G140 (≠ E137)
Query Sequence
>BPHYT_RS03235 FitnessBrowser__BFirm:BPHYT_RS03235
MTMDILVERADGVLTIAFNRPDKKNAITAAMYQTMADALVEAQGDAAVRAILIRGSAGIF
SAGNDLEDFMKTPPMGEHAPVFQFLRAISSAEKPVVASVAGAAVGIGTTLLLHCDLVYAA
DTASFSLPFTQLGLCPEAASSLLLPRAAGYQAAAEKLLLGEAFDAAEAQRMGFVNRVLPA
SEVDAFAASQAAKLAALPASSLRVTKSLMKRASHQELQTQMSEEAVHFGKMLLAPEAREA
FKAFFEKRKPDFRQFD
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