SitesBLAST
Comparing WP_058929179.1 NCBI__GCF_001484605.1:WP_058929179.1 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
38% identity, 94% coverage: 18:262/262 of query aligns to 16:259/259 of 5zaiC
- active site: A65 (≠ G68), F70 (≠ L73), S82 (≠ T88), R86 (= R92), G110 (= G116), E113 (= E119), P132 (= P138), E133 (= E139), I138 (≠ M144), P140 (≠ A146), G141 (≠ N147), A226 (≠ R231), F236 (≠ L240)
- binding coenzyme a: K24 (≠ S26), L25 (≠ R27), A63 (= A66), G64 (= G67), A65 (≠ G68), D66 (= D69), I67 (≠ L70), P132 (= P138), R166 (≠ L171), F248 (= F251), K251 (= K254)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 93% coverage: 20:262/262 of query aligns to 19:261/261 of 5jbxB
- active site: A67 (≠ G68), R72 (≠ L73), L84 (≠ M87), R88 (≠ E91), G112 (= G116), E115 (= E119), T134 (≠ P138), E135 (= E139), I140 (vs. gap), P142 (≠ G145), G143 (≠ A146), A228 (≠ R231), L238 (vs. gap)
- binding coenzyme a: S24 (≠ E25), R25 (≠ S26), R26 (= R27), A28 (= A29), A65 (= A66), D68 (= D69), L69 (= L70), K70 (= K71), L110 (≠ V114), G111 (≠ A115), T134 (≠ P138), E135 (= E139), L138 (≠ R142), R168 (≠ L171)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 94% coverage: 16:260/262 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (≠ G68), M71 (≠ L73), S81 (≠ T88), L85 (≠ R92), G109 (= G116), E112 (= E119), P131 (= P138), E132 (= E139), T137 (≠ M144), P139 (vs. gap), G140 (= G145), K225 (≠ R231), F235 (≠ Y239)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E25), L26 (≠ R27), A28 (= A29), A64 (= A66), G65 (= G67), A66 (≠ G68), D67 (= D69), I68 (≠ L70), L85 (≠ R92), W88 (≠ F95), G109 (= G116), P131 (= P138), L135 (≠ R142), G140 (= G145)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 94% coverage: 16:260/262 of query aligns to 17:258/260 of 1dubA
- active site: A68 (≠ G68), M73 (≠ L73), S83 (≠ T88), L87 (≠ R92), G111 (= G116), E114 (= E119), P133 (= P138), E134 (= E139), T139 (≠ M144), P141 (vs. gap), G142 (= G145), K227 (≠ R231), F237 (≠ Y239)
- binding acetoacetyl-coenzyme a: K26 (≠ E25), A27 (≠ S26), L28 (≠ R27), A30 (= A29), A66 (= A66), A68 (≠ G68), D69 (= D69), I70 (≠ L70), Y107 (≠ P112), G110 (≠ A115), G111 (= G116), E114 (= E119), P133 (= P138), E134 (= E139), L137 (≠ R142), G142 (= G145), F233 (≠ G235), F249 (= F251)
P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
34% identity, 94% coverage: 16:260/262 of query aligns to 47:288/290 of P14604
- E144 (= E119) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E139) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 97% coverage: 6:259/262 of query aligns to 3:253/256 of 3h81A
- active site: A64 (≠ G68), M69 (≠ L73), T79 (= T88), F83 (≠ R92), G107 (= G116), E110 (= E119), P129 (= P138), E130 (= E139), V135 (vs. gap), P137 (vs. gap), G138 (= G143), L223 (≠ R231), F233 (≠ Y239)
- binding calcium ion: F233 (≠ Y239), Q238 (≠ R244)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 97% coverage: 6:259/262 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (≠ G68), M70 (≠ L73), T80 (= T88), F84 (≠ R92), G108 (= G116), E111 (= E119), P130 (= P138), E131 (= E139), V136 (vs. gap), P138 (vs. gap), G139 (= G143), L224 (≠ R231), F234 (≠ Y239)
- binding acetoacetyl-coenzyme a: Q23 (≠ E25), A24 (≠ S26), L25 (≠ R27), A27 (= A29), A63 (= A66), G64 (= G67), A65 (≠ G68), D66 (= D69), I67 (≠ L70), K68 (= K71), M70 (≠ L73), F84 (≠ R92), G107 (≠ A115), G108 (= G116), E111 (= E119), P130 (= P138), E131 (= E139), P138 (vs. gap), G139 (= G143), M140 (= M144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 97% coverage: 6:259/262 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (≠ G68), M70 (≠ L73), T80 (= T88), F84 (≠ R92), G108 (= G116), E111 (= E119), P130 (= P138), E131 (= E139), V136 (vs. gap), P138 (vs. gap), G139 (= G143), L224 (≠ R231), F234 (≠ Y239)
- binding coenzyme a: L25 (≠ R27), A63 (= A66), I67 (≠ L70), K68 (= K71), Y104 (≠ P112), P130 (= P138), E131 (= E139), L134 (≠ R142)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 94% coverage: 14:260/262 of query aligns to 15:258/260 of 2hw5C
- active site: A68 (≠ G68), M73 (≠ L73), S83 (≠ T88), L87 (≠ R92), G111 (= G116), E114 (= E119), P133 (= P138), E134 (= E139), T139 (≠ M144), P141 (vs. gap), G142 (= G145), K227 (≠ R231), F237 (≠ Y239)
- binding crotonyl coenzyme a: K26 (≠ E25), A27 (≠ S26), L28 (≠ R27), A30 (= A29), K62 (≠ R62), I70 (≠ L70), F109 (≠ V114)
Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
35% identity, 94% coverage: 15:259/262 of query aligns to 20:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
35% identity, 97% coverage: 6:260/262 of query aligns to 8:254/260 of 2uzfA
- active site: G70 (= G68), R80 (= R82), L84 (≠ R92), G108 (= G116), V111 (≠ E119), T130 (≠ P138), G131 (≠ E139), S136 (vs. gap), D138 (≠ G145), A139 (= A146), A225 (≠ V234), Y233 (= Y239)
- binding acetoacetyl-coenzyme a: V28 (≠ S26), R29 (= R27), S68 (≠ A66), G69 (= G67), G70 (= G68), D71 (= D69), Y104 (≠ P112), G108 (= G116)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 94% coverage: 16:260/262 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (≠ G68), M73 (≠ L73), S83 (≠ T88), L85 (≠ T90), G109 (= G116), E112 (= E119), P131 (= P138), E132 (= E139), T137 (≠ M144), P139 (vs. gap), G140 (= G145), K225 (≠ R231), F235 (≠ Y239)
- binding hexanoyl-coenzyme a: K26 (≠ E25), A27 (≠ S26), L28 (≠ R27), A30 (= A29), A66 (= A66), G67 (= G67), A68 (≠ G68), D69 (= D69), I70 (≠ L70), G109 (= G116), P131 (= P138), E132 (= E139), L135 (≠ R142), G140 (= G145)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 97% coverage: 6:259/262 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (≠ G68), M69 (≠ L73), T75 (= T88), F79 (≠ R92), G103 (= G116), E106 (= E119), P125 (= P138), E126 (= E139), V131 (vs. gap), P133 (vs. gap), G134 (= G143), L219 (≠ R231), F229 (≠ Y239)
- binding Butyryl Coenzyme A: F225 (≠ G235), F241 (= F251)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
34% identity, 97% coverage: 6:260/262 of query aligns to 13:267/273 of Q5HH38
- R34 (= R27) binding in other chain
- SGGDQ 73:77 (≠ AGGDL 66:70) binding in other chain
- S149 (vs. gap) binding in other chain
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 100% coverage: 1:262/262 of query aligns to 1:266/266 of O53561
- K135 (≠ T134) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 134:141, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K141) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 94% coverage: 16:260/262 of query aligns to 16:252/254 of 2dubA
- active site: A67 (≠ G68), M72 (≠ L73), S82 (≠ T88), G105 (= G116), E108 (= E119), P127 (= P138), E128 (= E139), T133 (≠ M144), P135 (vs. gap), G136 (= G145), K221 (≠ R231), F231 (≠ Y239)
- binding octanoyl-coenzyme a: K25 (≠ E25), A26 (≠ S26), L27 (≠ R27), A29 (= A29), A65 (= A66), A67 (≠ G68), D68 (= D69), I69 (≠ L70), K70 (= K71), G105 (= G116), E108 (= E119), P127 (= P138), E128 (= E139), G136 (= G145), A137 (= A146)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
32% identity, 96% coverage: 6:257/262 of query aligns to 20:258/267 of 4elwA
- active site: G83 (= G68), L91 (≠ I76), G115 (= G116), V118 (≠ E119), G138 (≠ E139), S143 (vs. gap), D145 (≠ G145), G146 (≠ A146), A232 (≠ V234), Y240 (= Y239)
- binding nitrate ion: G114 (≠ A115), T137 (≠ P138), G138 (≠ E139), F144 (≠ M144), W166 (≠ L166)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
32% identity, 93% coverage: 14:257/262 of query aligns to 28:257/266 of 3h02A
- active site: G82 (= G68), H86 (≠ E72), L90 (≠ I76), G114 (= G116), V117 (≠ E119), G137 (≠ E139), S142 (vs. gap), D144 (≠ G145), G145 (≠ A146), A231 (≠ V234), Y239 (= Y239)
- binding bicarbonate ion: G113 (≠ A115), Q135 (≠ M137), G137 (≠ E139), W165 (≠ L166)
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 80% coverage: 7:215/262 of query aligns to 76:285/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
32% identity, 96% coverage: 6:257/262 of query aligns to 10:252/261 of 4emlA
- active site: G77 (= G68), R81 (≠ E72), L85 (≠ I76), G109 (= G116), V112 (≠ E119), G132 (≠ E139), S137 (vs. gap), D139 (≠ G145), G140 (≠ A146), A226 (≠ V234), Y234 (= Y239)
- binding bicarbonate ion: G108 (≠ A115), Q130 (≠ M137), G132 (≠ E139), W160 (≠ L166)
- binding chloride ion: D184 (= D190), R185 (≠ Q191), E187 (≠ A193), E188 (≠ K194)
Query Sequence
>WP_058929179.1 NCBI__GCF_001484605.1:WP_058929179.1
MSNVEEEVLFEIRDRVAYITMNRPESRNALSQAVVARLAEVFTVAAEDNDVWAIVLTGAG
DRAFCAGGDLKELNQIAQEGRRFPVPMTGTERNLFELVLEVGKPTIASLNGPAVAGGFEL
ALACDIRIAAEHSTIGMPEAKRGMGANFATVLLPRLVPRSVALSMLYTGELMAPSEALHW
GLVNAVHPADQLAKETEEFVRSIVANAPLALRRYKEMVTKGWELSVQAALRLNVGPNPYL
SADREEGVRAFIEKRAPRWEGK
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