SitesBLAST
Comparing Pf1N1B4_267 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_267 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)
33% identity, 97% coverage: 9:262/263 of query aligns to 6:258/259 of 5zaiC
- active site: A65 (≠ L68), F70 (≠ A73), S82 (≠ P84), R86 (≠ C88), G110 (≠ V114), E113 (= E117), P132 (≠ K136), E133 (= E137), I138 (= I142), P140 (= P144), G141 (≠ F145), A226 (= A231), F236 (vs. gap)
- binding coenzyme a: K24 (= K27), L25 (≠ R28), A63 (= A66), G64 (= G67), A65 (≠ L68), D66 (= D69), I67 (≠ L70), P132 (≠ K136), R166 (≠ E170), F248 (≠ M252), K251 (= K255)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 95% coverage: 12:261/263 of query aligns to 13:264/266 of O53561
- K135 (≠ R132) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 132:139, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ Q139) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
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)
36% identity, 92% coverage: 16:256/263 of query aligns to 20:261/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
32% identity, 95% coverage: 13:261/263 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (≠ L68), M73 (≠ A73), S83 (≠ G86), L85 (≠ C88), G109 (≠ V114), E112 (= E117), P131 (≠ K136), E132 (= E137), T137 (≠ I142), P139 (= P144), G140 (≠ F145), K225 (≠ A231), F235 (≠ L240)
- binding hexanoyl-coenzyme a: K26 (≠ A26), A27 (≠ K27), L28 (≠ R28), A30 (= A30), A66 (= A66), G67 (= G67), A68 (≠ L68), D69 (= D69), I70 (≠ L70), G109 (≠ V114), P131 (≠ K136), E132 (= E137), L135 (≠ R140), G140 (≠ F145)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 95% coverage: 11:261/263 of query aligns to 11:258/260 of 2hw5C
- active site: A68 (≠ L68), M73 (vs. gap), S83 (≠ Q82), L87 (≠ C88), G111 (≠ V114), E114 (= E117), P133 (≠ K136), E134 (= E137), T139 (≠ I142), P141 (= P144), G142 (≠ F145), K227 (≠ A231), F237 (≠ L240)
- binding crotonyl coenzyme a: K26 (≠ A26), A27 (≠ K27), L28 (≠ R28), A30 (= A30), K62 (≠ E62), I70 (≠ L70), F109 (≠ L112)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
32% identity, 95% coverage: 13:261/263 of query aligns to 12:252/254 of 2dubA
- active site: A67 (≠ L68), M72 (≠ G80), S82 (≠ D89), G105 (≠ V114), E108 (= E117), P127 (≠ K136), E128 (= E137), T133 (≠ I142), P135 (= P144), G136 (≠ F145), K221 (≠ A231), F231 (≠ L240)
- binding octanoyl-coenzyme a: K25 (≠ A26), A26 (≠ K27), L27 (≠ R28), A29 (= A30), A65 (= A66), A67 (≠ L68), D68 (= D69), I69 (≠ L70), K70 (≠ A78), G105 (≠ V114), E108 (= E117), P127 (≠ K136), E128 (= E137), G136 (≠ F145), A137 (≠ G146)
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)
31% identity, 95% coverage: 13:261/263 of query aligns to 43:288/290 of P14604
- E144 (= E117) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E137) 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
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 95% coverage: 13:261/263 of query aligns to 13:258/260 of 1dubA
- active site: A68 (≠ L68), M73 (≠ G80), S83 (≠ P90), L87 (= L94), G111 (≠ V114), E114 (= E117), P133 (≠ K136), E134 (= E137), T139 (≠ I142), P141 (= P144), G142 (≠ F145), K227 (≠ A231), F237 (≠ L240)
- binding acetoacetyl-coenzyme a: K26 (≠ A26), A27 (≠ K27), L28 (≠ R28), A30 (= A30), A66 (= A66), A68 (≠ L68), D69 (= D69), I70 (≠ L70), Y107 (= Y110), G110 (≠ T113), G111 (≠ V114), E114 (= E117), P133 (≠ K136), E134 (= E137), L137 (≠ R140), G142 (≠ F145), F233 (≠ V236), F249 (≠ M252)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 95% coverage: 13:261/263 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (≠ L68), M71 (≠ G80), S81 (≠ P90), L85 (= L94), G109 (≠ V114), E112 (= E117), P131 (≠ K136), E132 (= E137), T137 (≠ I142), P139 (= P144), G140 (≠ F145), K225 (≠ A231), F235 (≠ L240)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A26), L26 (≠ R28), A28 (= A30), A64 (= A66), G65 (= G67), A66 (≠ L68), D67 (= D69), I68 (≠ L70), L85 (= L94), W88 (vs. gap), G109 (≠ V114), P131 (≠ K136), L135 (≠ R140), G140 (≠ F145)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 97% coverage: 9:262/263 of query aligns to 2:244/245 of 6slaAAA
- active site: Q61 (≠ L68), L68 (≠ A75), N72 (≠ E79), A96 (≠ V114), S99 (≠ E117), A118 (≠ K136), F119 (≠ E137), L124 (≠ I142), P126 (= P144), N127 (≠ F145), A212 (= A231), G222 (vs. gap)
- 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 (≠ R28), A59 (= A66), Q61 (≠ L68), D62 (= D69), L63 (= L70), L68 (≠ A75), Y71 (≠ A78), A94 (≠ L112), G95 (≠ T113), A96 (≠ V114), F119 (≠ E137), I122 (≠ R140), L124 (≠ I142), N127 (≠ F145), F234 (≠ M252), K237 (= K255)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 97% coverage: 9:262/263 of query aligns to 5:256/257 of 6slbAAA
- active site: Q64 (≠ L68), F69 (≠ A73), L80 (≠ P84), N84 (≠ C88), A108 (≠ V114), S111 (≠ E117), A130 (≠ K136), F131 (≠ E137), L136 (≠ I142), P138 (= P144), D139 (≠ F145), A224 (= A231), G234 (vs. gap)
- 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 (≠ E62), A62 (= A66), Q64 (≠ L68), D65 (= D69), L66 (= L70), Y76 (≠ G80), A108 (≠ V114), F131 (≠ E137), D139 (≠ F145)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 95% coverage: 12:260/263 of query aligns to 9:254/255 of 3q0jC
- active site: A65 (≠ L68), M70 (vs. gap), T80 (≠ Q82), F84 (≠ G86), G108 (≠ V114), E111 (= E117), P130 (≠ K136), E131 (= E137), V136 (≠ I142), P138 (= P144), G139 (≠ F145), L224 (= L240), F234 (vs. gap)
- binding acetoacetyl-coenzyme a: Q23 (≠ A26), A24 (≠ K27), L25 (≠ R28), A27 (= A30), A63 (= A66), G64 (= G67), A65 (≠ L68), D66 (= D69), I67 (≠ L70), K68 (≠ V71), M70 (vs. gap), F84 (≠ G86), G107 (≠ T113), G108 (≠ V114), E111 (= E117), P130 (≠ K136), E131 (= E137), P138 (= P144), G139 (≠ F145), M140 (≠ G146)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 95% coverage: 12:260/263 of query aligns to 9:254/255 of 3q0gC
- active site: A65 (≠ L68), M70 (vs. gap), T80 (≠ Q82), F84 (≠ G86), G108 (≠ V114), E111 (= E117), P130 (≠ K136), E131 (= E137), V136 (≠ I142), P138 (= P144), G139 (≠ F145), L224 (= L240), F234 (vs. gap)
- binding coenzyme a: L25 (≠ R28), A63 (= A66), I67 (≠ L70), K68 (≠ V71), Y104 (= Y110), P130 (≠ K136), E131 (= E137), L134 (≠ R140)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 95% coverage: 12:260/263 of query aligns to 8:253/256 of 3h81A
- active site: A64 (≠ L68), M69 (vs. gap), T79 (≠ Q82), F83 (≠ G86), G107 (≠ V114), E110 (= E117), P129 (≠ K136), E130 (= E137), V135 (≠ I142), P137 (= P144), G138 (≠ F145), L223 (= L240), F233 (vs. gap)
- binding calcium ion: F233 (vs. gap), Q238 (≠ A245)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 95% coverage: 12:260/263 of query aligns to 8:249/250 of 3q0gD
- active site: A64 (≠ L68), M69 (≠ A73), T75 (≠ Q82), F79 (≠ G86), G103 (≠ V114), E106 (= E117), P125 (≠ K136), E126 (= E137), V131 (≠ I142), P133 (= P144), G134 (≠ F145), L219 (= L240), F229 (vs. gap)
- binding Butyryl Coenzyme A: F225 (vs. gap), F241 (≠ M252)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
29% identity, 92% coverage: 14:256/263 of query aligns to 63:317/327 of Q62651
- D176 (≠ E117) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E137) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ F145) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
35% identity, 79% coverage: 10:216/263 of query aligns to 7:194/224 of 3p85A
- active site: L62 (= L68), L67 (≠ P84), P68 (= P85), G92 (≠ V114), E95 (= E117), T114 (≠ K136), H115 (≠ E137), L120 (≠ I142), P122 (= P144), T123 (≠ F145)
- binding calcium ion: D43 (= D49), D45 (≠ E51)
Sites not aligning to the query:
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
32% identity, 89% coverage: 13:245/263 of query aligns to 17:247/267 of Q5LLW6
- K31 (= K27) binding
- R32 (= R28) binding
- A69 (= A66) binding
- L71 (= L68) binding
- L73 (= L70) binding
- G118 (≠ V114) binding
- E121 (= E117) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (= E137) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (= R140) binding
- G149 (≠ F145) binding
4izcB Crystal structure of dmdd e121a in complex with mta-coa (see paper)
32% identity, 89% coverage: 13:245/263 of query aligns to 16:246/266 of 4izcB
- active site: L70 (= L68), H75 (≠ G80), C89 (≠ L94), H93 (vs. gap), G117 (≠ V114), A120 (≠ E117), E140 (= E137), G148 (≠ F145), Y232 (≠ Q230)
- binding methylthioacryloyl-CoA: D29 (≠ A26), K30 (= K27), R31 (= R28), A33 (= A30), A68 (= A66), L70 (= L68), D71 (= D69), L72 (= L70), W92 (vs. gap), G117 (≠ V114), P139 (≠ K136), E140 (= E137), R143 (= R140), G148 (≠ F145)
4izdA Crystal structure of dmdd e121a in complex with mmpa-coa (see paper)
32% identity, 89% coverage: 13:245/263 of query aligns to 16:246/253 of 4izdA
- active site: L70 (= L68), H75 (≠ G80), C89 (≠ L94), H93 (vs. gap), G117 (≠ V114), A120 (≠ E117), E140 (= E137), G148 (≠ F145), Y232 (≠ Q230)
- binding 3-methylmercaptopropionate-CoA (MMPA-CoA): D29 (≠ A26), K30 (= K27), R31 (= R28), A33 (= A30), A68 (= A66), L70 (= L68), D71 (= D69), L72 (= L70)
Query Sequence
>Pf1N1B4_267 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_267
MNQPSPSRVTRERHGHVLMIGLDRVAKRNAFDLNLLNELSLAYGEFEADSEARVAVVFGH
GEHFTAGLDLVSAGAALAEGWQAPPGGCDPWGVLAGPRVSKPVIVAAQGYCLTVGIELML
AADINLCASNTRFAQKEVQRGIFPFGGATLRLHQVAGWGNAMRWLLTGDEFDAHDALHLG
LVQEVMASEDLLPRAIELAERIARQAPLGVQATLMSARQARYEGEMTAAQALPALVKNLL
NSEDAKEGVRSMIEKRPGVFKGV
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