SitesBLAST
Comparing H281DRAFT_01187 FitnessBrowser__Burk376:H281DRAFT_01187 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)
36% identity, 91% coverage: 25:265/265 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (= A73), F70 (≠ P79), S82 (≠ N91), R86 (= R95), G110 (≠ A119), E113 (≠ G122), P132 (= P141), E133 (= E142), I138 (≠ L147), P140 (vs. gap), G141 (vs. gap), A226 (≠ R232), F236 (≠ S242)
- binding coenzyme a: K24 (≠ V32), L25 (≠ K33), A63 (≠ S71), G64 (= G72), A65 (= A73), D66 (= D74), I67 (≠ L75), P132 (= P141), R166 (≠ K172), F248 (= F254), K251 (= K257)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
36% identity, 91% coverage: 22:263/265 of query aligns to 17:258/260 of 2hw5C
- active site: A68 (= A73), M73 (≠ R78), S83 (≠ P84), L87 (= L88), G111 (≠ A119), E114 (≠ G122), P133 (= P141), E134 (= E142), T139 (≠ L147), P141 (vs. gap), G142 (vs. gap), K227 (≠ R232), F237 (≠ S242)
- binding crotonyl coenzyme a: K26 (≠ E31), A27 (≠ V32), L28 (≠ K33), A30 (= A35), K62 (≠ D67), I70 (≠ L75), F109 (≠ L117)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 91% coverage: 22:263/265 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (= A73), M71 (vs. gap), S81 (≠ P84), L85 (= L88), G109 (≠ A119), E112 (≠ G122), P131 (= P141), E132 (= E142), T137 (≠ L147), P139 (vs. gap), G140 (vs. gap), K225 (≠ R232), F235 (≠ S242)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E31), L26 (≠ K33), A28 (= A35), A64 (≠ S71), G65 (= G72), A66 (= A73), D67 (= D74), I68 (≠ L75), L85 (= L88), W88 (= W93), G109 (≠ A119), P131 (= P141), L135 (≠ V145), G140 (vs. gap)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 91% coverage: 22:263/265 of query aligns to 17:258/260 of 1dubA
- active site: A68 (= A73), M73 (vs. gap), S83 (≠ P84), L87 (= L88), G111 (≠ A119), E114 (≠ G122), P133 (= P141), E134 (= E142), T139 (≠ L147), P141 (vs. gap), G142 (vs. gap), K227 (≠ R232), F237 (≠ S242)
- binding acetoacetyl-coenzyme a: K26 (≠ E31), A27 (≠ V32), L28 (≠ K33), A30 (= A35), A66 (≠ S71), A68 (= A73), D69 (= D74), I70 (≠ L75), Y107 (≠ A115), G110 (= G118), G111 (≠ A119), E114 (≠ G122), P133 (= P141), E134 (= E142), L137 (≠ V145), G142 (vs. gap), F233 (≠ T238), F249 (= F254)
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)
35% identity, 91% coverage: 22:263/265 of query aligns to 47:288/290 of P14604
- E144 (≠ G122) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E142) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 91% coverage: 22:263/265 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (= A73), M73 (≠ R78), S83 (≠ L88), L85 (≠ H90), G109 (≠ A119), E112 (≠ G122), P131 (= P141), E132 (= E142), T137 (≠ L147), P139 (vs. gap), G140 (vs. gap), K225 (≠ R232), F235 (≠ S242)
- binding hexanoyl-coenzyme a: K26 (≠ E31), A27 (≠ V32), L28 (≠ K33), A30 (= A35), A66 (≠ S71), G67 (= G72), A68 (= A73), D69 (= D74), I70 (≠ L75), G109 (≠ A119), P131 (= P141), E132 (= E142), L135 (≠ V145), G140 (vs. gap)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
33% identity, 90% coverage: 22:259/265 of query aligns to 66:318/327 of Q62651
- D176 (≠ G122) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E142) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ G150) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
34% identity, 91% coverage: 22:263/265 of query aligns to 16:252/254 of 2dubA
- active site: A67 (= A73), M72 (≠ R78), S82 (≠ N91), G105 (≠ A119), E108 (≠ G122), P127 (= P141), E128 (= E142), T133 (≠ L147), P135 (vs. gap), G136 (vs. gap), K221 (≠ R232), F231 (≠ S242)
- binding octanoyl-coenzyme a: K25 (≠ E31), A26 (≠ V32), L27 (≠ K33), A29 (= A35), A65 (≠ S71), A67 (= A73), D68 (= D74), I69 (≠ L75), K70 (≠ R76), G105 (≠ A119), E108 (≠ G122), P127 (= P141), E128 (= E142), G136 (vs. gap), A137 (= A148)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 91% coverage: 24:265/265 of query aligns to 20:266/266 of O53561
- K135 (≠ V137) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 137:144, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N144) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
33% identity, 92% coverage: 19:262/265 of query aligns to 31:278/285 of 4i42A
- active site: G86 (≠ A73), R91 (= R78), Y97 (≠ F87), H105 (≠ N91), L109 (≠ R95), G133 (≠ A119), V136 (≠ G122), G156 (≠ E142), S161 (≠ L147), D163 (vs. gap), G164 (vs. gap), A250 (≠ E234), Y258 (≠ S242)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V32), R45 (≠ K33), S84 (= S71), G85 (= G72), G86 (≠ A73), D87 (= D74), Q88 (≠ L75), K89 (≠ R76), Y97 (≠ F87), V108 (≠ T94), Y129 (≠ A115), G133 (≠ A119), T155 (≠ P141), S161 (≠ L147), T254 (= T238), F270 (= F254), K273 (= K257)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 92% coverage: 19:262/265 of query aligns to 31:278/285 of P0ABU0
- R45 (≠ K33) binding in other chain
- SGGDQK 84:89 (≠ SGADLR 71:76) binding in other chain
- K89 (≠ R76) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R78) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ F87) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AALGA 115:119) binding in other chain
- Q154 (≠ M140) 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 (≠ MPE 140:142) binding
- T155 (≠ P141) binding in other chain
- G156 (≠ E142) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L147) binding in other chain
- W184 (≠ F167) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ S242) binding
- R267 (= R251) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F254) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K257) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
33% identity, 92% coverage: 19:262/265 of query aligns to 27:274/281 of 3t88A
- active site: G82 (≠ A73), R87 (= R78), Y93 (≠ F87), H101 (≠ N91), L105 (≠ R95), G129 (≠ A119), V132 (≠ G122), G152 (≠ E142), S157 (≠ L147), D159 (vs. gap), G160 (vs. gap), A246 (≠ E234), Y254 (≠ S242)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E31), V40 (= V32), R41 (≠ K33), A43 (= A35), S80 (= S71), G81 (= G72), G82 (≠ A73), D83 (= D74), Q84 (≠ L75), K85 (≠ R76), Y93 (≠ F87), V104 (≠ T94), L105 (≠ R95), Y125 (≠ A115), G129 (≠ A119), T151 (≠ P141), V155 (= V145), F158 (vs. gap), D159 (vs. gap), T250 (= T238), Y254 (≠ S242), F266 (= F254), K269 (= K257)
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)
29% identity, 99% coverage: 1:263/265 of query aligns to 1:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
32% identity, 92% coverage: 19:262/265 of query aligns to 28:261/268 of 4elxA
- active site: G83 (≠ A73), H88 (≠ R78), L92 (= L88), G116 (≠ A119), V119 (≠ G122), G139 (≠ E142), S144 (≠ L147), D146 (vs. gap), G147 (vs. gap), A233 (≠ E234), Y241 (≠ S242)
- binding chloride ion: G115 (= G118), G139 (≠ E142), W167 (≠ F167)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
32% identity, 92% coverage: 19:262/265 of query aligns to 28:260/267 of 4elwA
- active site: G83 (≠ A73), L91 (= L88), G115 (≠ A119), V118 (≠ G122), G138 (≠ E142), S143 (≠ L147), D145 (vs. gap), G146 (vs. gap), A232 (≠ E234), Y240 (≠ S242)
- binding nitrate ion: G114 (= G118), T137 (≠ P141), G138 (≠ E142), F144 (vs. gap), W166 (≠ F167)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 92% coverage: 22:265/265 of query aligns to 15:261/261 of 5jbxB
- active site: A67 (= A73), R72 (= R78), L84 (= L88), R88 (= R95), G112 (≠ A119), E115 (≠ G122), T134 (≠ P141), E135 (= E142), I140 (≠ L147), P142 (vs. gap), G143 (vs. gap), A228 (≠ R232), L238 (≠ S242)
- binding coenzyme a: S24 (≠ E31), R25 (≠ V32), R26 (≠ K33), A28 (= A35), A65 (≠ S71), D68 (= D74), L69 (= L75), K70 (≠ R76), L110 (= L117), G111 (= G118), T134 (≠ P141), E135 (= E142), L138 (≠ V145), R168 (≠ K172)
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, 95% coverage: 10:262/265 of query aligns to 11:266/273 of Q5HH38
- R34 (≠ K33) binding in other chain
- SGGDQ 73:77 (≠ SGADL 71:75) binding in other chain
- S149 (≠ V145) binding in other chain
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
31% identity, 92% coverage: 19:262/265 of query aligns to 31:278/285 of Q7CQ56
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 93% coverage: 20:265/265 of query aligns to 11:257/257 of 6slbAAA
- active site: Q64 (≠ A73), F69 (≠ R78), L80 (≠ F87), N84 (= N91), A108 (= A119), S111 (≠ G122), A130 (≠ P141), F131 (≠ E142), L136 (= L147), P138 (vs. gap), D139 (vs. gap), A224 (≠ R232), G234 (≠ S242)
- 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 (≠ D67), A62 (≠ S71), Q64 (≠ A73), D65 (= D74), L66 (= L75), Y76 (≠ V83), A108 (= A119), F131 (≠ E142), D139 (vs. gap)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
32% identity, 95% coverage: 10:262/265 of query aligns to 6:253/260 of 2uzfA
- active site: G70 (≠ A73), R80 (≠ G85), L84 (= L88), G108 (≠ A119), V111 (≠ G122), T130 (vs. gap), G131 (vs. gap), S136 (≠ V145), D138 (≠ L147), A139 (= A148), A225 (≠ E234), Y233 (≠ S242)
- binding acetoacetyl-coenzyme a: V28 (= V32), R29 (≠ K33), S68 (= S71), G69 (= G72), G70 (≠ A73), D71 (= D74), Y104 (≠ A115), G108 (≠ A119)
Query Sequence
>H281DRAFT_01187 FitnessBrowser__Burk376:H281DRAFT_01187
MTMSEASSAEICAVTLAVTDGVALVTLNRPEVKNALSRAMRRRLIAIFDEISARNDIRCA
VLTGAGDTFCSGADLRDRPDPDVPGDFLDHNRWTRETGNAIKECVKPVIAAVNGAALGAG
LGLMAACDIMYASDNAVFAMPEINVGLAGGASMLRTLFGRSTVRRMFFTGDKLTAQDLLR
RNVLEDVLPADTLMPYVMELARRIARKSPIALIEAKKAANFTDQMPQREAYRHEQDITMM
LSRTEDAKEARMAFLEKREPVFKGR
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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