SitesBLAST
Comparing WP_012975228.1 NCBI__GCF_000010725.1:WP_012975228.1 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
62% identity, 100% coverage: 2:258/258 of query aligns to 1:256/256 of 3h81A
- active site: A64 (= A65), M69 (= M70), T79 (≠ N80), F83 (≠ I84), G107 (= G109), E110 (= E112), P129 (= P131), E130 (= E132), V135 (≠ T137), P137 (= P139), G138 (= G140), L223 (≠ R225), F233 (= F235)
- binding calcium ion: F233 (= F235), Q238 (= Q240)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
63% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (= M70), T80 (≠ N80), F84 (≠ I84), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ T137), P138 (= P139), G139 (= G140), L224 (≠ R225), F234 (= F235)
- binding acetoacetyl-coenzyme a: Q23 (≠ K23), A24 (= A24), L25 (= L25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), K68 (= K68), M70 (= M70), F84 (≠ I84), G107 (= G108), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), P138 (= P139), G139 (= G140), M140 (≠ A141)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
63% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M70), T80 (≠ N80), F84 (≠ I84), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ T137), P138 (= P139), G139 (= G140), L224 (≠ R225), F234 (= F235)
- binding coenzyme a: L25 (= L25), A63 (= A63), I67 (= I67), K68 (= K68), Y104 (≠ F105), P130 (= P131), E131 (= E132), L134 (≠ I135)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
61% identity, 100% coverage: 2:258/258 of query aligns to 2:260/260 of 2hw5C
- active site: A68 (= A65), M73 (= M70), S83 (≠ N80), L87 (≠ I84), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (= T137), P141 (= P139), G142 (= G140), K227 (≠ R225), F237 (= F235)
- binding crotonyl coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), K62 (≠ R59), I70 (= I67), F109 (≠ L107)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
60% identity, 100% coverage: 2:258/258 of query aligns to 2:260/260 of 1dubA
- active site: A68 (= A65), M73 (= M70), S83 (≠ N80), L87 (≠ I84), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (= T137), P141 (= P139), G142 (= G140), K227 (≠ R225), F237 (= F235)
- binding acetoacetyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A63), A68 (= A65), D69 (= D66), I70 (= I67), Y107 (≠ F105), G110 (= G108), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), L137 (≠ I135), G142 (= G140), F233 (= F231), F249 (= F247)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
60% identity, 99% coverage: 3:258/258 of query aligns to 1:258/258 of 1ey3A
- active site: A66 (= A65), M71 (= M70), S81 (≠ N80), L85 (≠ I84), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (= T137), P139 (= P139), G140 (= G140), K225 (≠ R225), F235 (= F235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K23), L26 (= L25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (= I67), L85 (≠ I84), W88 (= W88), G109 (= G109), P131 (= P131), L135 (≠ I135), G140 (= G140)
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)
60% identity, 100% coverage: 2:258/258 of query aligns to 32:290/290 of P14604
- E144 (= E112) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E132) 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
62% identity, 98% coverage: 2:255/258 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (≠ N80), F79 (≠ I84), G103 (= G109), E106 (= E112), P125 (= P131), E126 (= E132), V131 (≠ T137), P133 (= P139), G134 (= G140), L219 (≠ R225), F229 (= F235)
- binding Butyryl Coenzyme A: F225 (= F231), F241 (= F247)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
59% identity, 100% coverage: 2:258/258 of query aligns to 2:258/258 of 1mj3A
- active site: A68 (= A65), M73 (= M70), S83 (≠ N80), L85 (≠ S85), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (= T137), P139 (= P139), G140 (= G140), K225 (≠ R225), F235 (= F235)
- binding hexanoyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (= I67), G109 (= G109), P131 (= P131), E132 (= E132), L135 (≠ I135), G140 (= G140)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
59% identity, 100% coverage: 2:258/258 of query aligns to 1:254/254 of 2dubA
- active site: A67 (= A65), M72 (= M70), S82 (≠ A86), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), T133 (= T137), P135 (= P139), G136 (= G140), K221 (≠ R225), F231 (= F235)
- binding octanoyl-coenzyme a: K25 (= K23), A26 (= A24), L27 (= L25), A29 (= A27), A65 (= A63), A67 (= A65), D68 (= D66), I69 (= I67), K70 (= K68), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), G136 (= G140), A137 (= A141)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
44% identity, 100% coverage: 1:258/258 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (= S81), R86 (≠ S85), G110 (= G109), E113 (= E112), P132 (= P131), E133 (= E132), I138 (≠ T137), P140 (= P139), G141 (= G140), A226 (≠ R225), F236 (= F235)
- binding coenzyme a: K24 (≠ A24), L25 (= L25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), P132 (= P131), R166 (≠ M165), F248 (= F247), K251 (= K250)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
37% identity, 97% coverage: 8:258/258 of query aligns to 9:261/261 of 5jbxB
- active site: A67 (= A65), R72 (≠ M70), L84 (≠ M76), R88 (≠ N80), G112 (= G109), E115 (= E112), T134 (≠ P131), E135 (= E132), I140 (≠ T137), P142 (= P139), G143 (= G140), A228 (≠ R225), L238 (≠ F235)
- binding coenzyme a: S24 (≠ K23), R25 (≠ A24), R26 (≠ L25), A28 (= A27), A65 (= A63), D68 (= D66), L69 (≠ I67), K70 (= K68), L110 (= L107), G111 (= G108), T134 (≠ P131), E135 (= E132), L138 (≠ I135), R168 (≠ M165)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 98% coverage: 6:258/258 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A65), L68 (≠ M76), N72 (= N80), A96 (≠ G109), S99 (≠ E112), A118 (≠ P131), F119 (≠ E132), L124 (≠ T137), P126 (= P139), N127 (≠ G140), A212 (≠ R225), G222 (≠ F235)
- 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 (= L25), A59 (= A63), Q61 (≠ A65), D62 (= D66), L63 (≠ I67), L68 (≠ M76), Y71 (= Y79), A94 (≠ L107), G95 (= G108), A96 (≠ G109), F119 (≠ E132), I122 (= I135), L124 (≠ T137), N127 (≠ G140), F234 (= F247), K237 (= K250)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 98% coverage: 6:258/258 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A65), F69 (≠ M70), L80 (≠ M76), N84 (= N80), A108 (≠ G109), S111 (≠ E112), A130 (≠ P131), F131 (≠ E132), L136 (≠ T137), P138 (= P139), D139 (≠ G140), A224 (≠ R225), G234 (≠ F235)
- 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 (= R59), A62 (= A63), Q64 (≠ A65), D65 (= D66), L66 (≠ I67), Y76 (vs. gap), A108 (≠ G109), F131 (≠ E132), D139 (≠ G140)
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, 93% coverage: 16:256/258 of query aligns to 23:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
36% identity, 92% coverage: 17:253/258 of query aligns to 37:276/285 of 4i42A
- active site: G86 (≠ A65), R91 (≠ M70), Y97 (= Y75), H105 (≠ N80), L109 (≠ I84), G133 (= G109), V136 (≠ E112), G156 (≠ E132), S161 (≠ T137), D163 (≠ P139), G164 (= G140), A250 (≠ I224), Y258 (≠ F235)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A24), R45 (≠ L25), S84 (≠ A63), G85 (= G64), G86 (≠ A65), D87 (= D66), Q88 (≠ I67), K89 (= K68), Y97 (= Y75), V108 (≠ F83), Y129 (≠ F105), G133 (= G109), T155 (≠ P131), S161 (≠ T137), T254 (≠ R228), F270 (= F247), K273 (= K250)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 92% coverage: 17:253/258 of query aligns to 37:276/285 of P0ABU0
- R45 (≠ L25) binding in other chain
- SGGDQK 84:89 (≠ AGADIK 63:68) binding in other chain
- K89 (= K68) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M70) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y75) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ FALGG 105:109) binding in other chain
- Q154 (= Q130) 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 (≠ QPE 130:132) binding hydrogencarbonate
- T155 (≠ P131) binding in other chain
- G156 (≠ E132) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ T137) binding in other chain
- W184 (≠ V160) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ F235) binding substrate
- R267 (≠ M244) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F247) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K250) binding substrate; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
36% identity, 92% coverage: 17:253/258 of query aligns to 33:272/281 of 3t88A
- active site: G82 (≠ A65), R87 (≠ M70), Y93 (= Y75), H101 (≠ N80), L105 (≠ I84), G129 (= G109), V132 (≠ E112), G152 (≠ E132), S157 (≠ T137), D159 (≠ P139), G160 (= G140), A246 (≠ I224), Y254 (≠ F235)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ K23), V40 (≠ A24), R41 (≠ L25), A43 (= A27), S80 (≠ A63), G81 (= G64), G82 (≠ A65), D83 (= D66), Q84 (≠ I67), K85 (= K68), Y93 (= Y75), V104 (≠ F83), L105 (≠ I84), Y125 (≠ F105), G129 (= G109), T151 (≠ P131), V155 (≠ I135), F158 (≠ I138), D159 (≠ P139), T250 (≠ R228), Y254 (≠ F235), F266 (= F247), K269 (= K250)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
36% identity, 92% coverage: 17:253/258 of query aligns to 37:276/285 of Q7CQ56
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 98% coverage: 7:258/258 of query aligns to 11:266/266 of O53561
- K135 (= K127) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 127:134, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ T134) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Query Sequence
>WP_012975228.1 NCBI__GCF_000010725.1:WP_012975228.1
MSYETILVETRGPVGLITLNRPKALNALCDQLVTELGQALDAFEADAAIGAIVVTGSERA
FAAGADIKEMAGFSYMDVYNSNFISAKWERLAKCRKPTIAAVAGFALGGGCELAMMADFI
LAADTAKFGQPEVTIGTIPGAGGTQRLTRLVGKSKAMEMVLTGRMIDAAEAERCGLVSRV
VPAAELVEEAVKVATKIASLSQPIVAMAKEAVNVAYESTLAEGIRFERRLFHSTFATEDQ
KEGMAAFSEKRQPGWKNR
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