SitesBLAST
Comparing PP_4030 FitnessBrowser__Putida:PP_4030 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)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
52% identity, 94% coverage: 11:274/280 of query aligns to 49:317/327 of Q62651
- D176 (= D134) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E154) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D162) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 95% coverage: 13:278/280 of query aligns to 2:256/259 of 5zaiC
- active site: A65 (≠ I76), F70 (≠ L81), S82 (≠ G93), R86 (= R97), G110 (= G131), E113 (≠ D134), P132 (≠ K153), E133 (= E154), I138 (≠ M159), P140 (≠ A161), G141 (≠ D162), A226 (≠ D248), F236 (≠ L258)
- binding coenzyme a: K24 (= K35), L25 (≠ V36), A63 (= A74), G64 (= G75), A65 (≠ I76), D66 (= D77), I67 (≠ L78), P132 (≠ K153), R166 (≠ N187), F248 (≠ H270), K251 (= K273)
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)
32% identity, 92% coverage: 22:278/280 of query aligns to 18:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
28% identity, 93% coverage: 22:280/280 of query aligns to 13:253/254 of 2dubA
- active site: A67 (≠ I76), M72 (≠ L81), S82 (≠ A108), G105 (= G131), E108 (≠ D134), P127 (≠ K153), E128 (= E154), T133 (≠ M159), P135 (≠ A161), G136 (≠ D162), K221 (≠ D248), F231 (≠ L258)
- binding octanoyl-coenzyme a: K25 (≠ E34), A26 (≠ K35), L27 (≠ V36), A29 (= A38), A65 (= A74), A67 (≠ I76), D68 (= D77), I69 (≠ L78), K70 (≠ M79), G105 (= G131), E108 (≠ D134), P127 (≠ K153), E128 (= E154), G136 (≠ D162), A137 (≠ V163)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
28% identity, 93% coverage: 22:280/280 of query aligns to 14:259/260 of 1dubA
- active site: A68 (≠ I76), M73 (≠ L81), S83 (≠ I103), L87 (≠ Q107), G111 (= G131), E114 (≠ D134), P133 (≠ K153), E134 (= E154), T139 (≠ M159), P141 (≠ A161), G142 (≠ D162), K227 (≠ D248), F237 (≠ L258)
- binding acetoacetyl-coenzyme a: K26 (≠ E34), A27 (≠ K35), L28 (≠ V36), A30 (= A38), A66 (= A74), A68 (≠ I76), D69 (= D77), I70 (≠ L78), Y107 (= Y127), G110 (= G130), G111 (= G131), E114 (≠ D134), P133 (≠ K153), E134 (= E154), L137 (≠ M157), G142 (≠ D162), F233 (≠ N254), F249 (≠ H270)
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)
28% identity, 93% coverage: 22:280/280 of query aligns to 44:289/290 of P14604
- E144 (≠ D134) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E154) 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
28% identity, 93% coverage: 22:280/280 of query aligns to 12:257/258 of 1ey3A
- active site: A66 (≠ I76), M71 (≠ L81), S81 (≠ I103), L85 (≠ Q107), G109 (= G131), E112 (≠ D134), P131 (≠ K153), E132 (= E154), T137 (≠ M159), P139 (≠ A161), G140 (≠ D162), K225 (≠ D248), F235 (≠ L258)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E34), L26 (≠ V36), A28 (= A38), A64 (= A74), G65 (= G75), A66 (≠ I76), D67 (= D77), I68 (≠ L78), L85 (≠ Q107), W88 (≠ F110), G109 (= G131), P131 (≠ K153), L135 (≠ M157), G140 (≠ D162)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 95% coverage: 14:278/280 of query aligns to 3:254/255 of 3q0jC
- active site: A65 (≠ I76), M70 (≠ L81), T80 (≠ I103), F84 (≠ Q107), G108 (= G131), E111 (≠ D134), P130 (≠ K153), E131 (= E154), V136 (≠ M159), P138 (≠ A161), G139 (≠ D162), L224 (≠ D248), F234 (≠ L258)
- binding acetoacetyl-coenzyme a: Q23 (≠ E34), A24 (≠ K35), L25 (≠ V36), A27 (= A38), A63 (= A74), G64 (= G75), A65 (≠ I76), D66 (= D77), I67 (≠ L78), K68 (≠ M79), M70 (≠ L81), F84 (≠ Q107), G107 (= G130), G108 (= G131), E111 (≠ D134), P130 (≠ K153), E131 (= E154), P138 (≠ A161), G139 (≠ D162), M140 (≠ V163)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 95% coverage: 14:278/280 of query aligns to 3:254/255 of 3q0gC
- active site: A65 (≠ I76), M70 (≠ L81), T80 (≠ I103), F84 (≠ Q107), G108 (= G131), E111 (≠ D134), P130 (≠ K153), E131 (= E154), V136 (≠ M159), P138 (≠ A161), G139 (≠ D162), L224 (≠ D248), F234 (≠ L258)
- binding coenzyme a: L25 (≠ V36), A63 (= A74), I67 (≠ L78), K68 (≠ M79), Y104 (= Y127), P130 (≠ K153), E131 (= E154), L134 (≠ M157)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 95% coverage: 14:278/280 of query aligns to 2:253/256 of 3h81A
- active site: A64 (≠ I76), M69 (≠ L81), T79 (≠ I103), F83 (≠ Q107), G107 (= G131), E110 (≠ D134), P129 (≠ K153), E130 (= E154), V135 (≠ M159), P137 (≠ A161), G138 (≠ D162), L223 (≠ D248), F233 (≠ L258)
- binding calcium ion: F233 (≠ L258), Q238 (≠ L263)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
28% identity, 93% coverage: 22:280/280 of query aligns to 14:257/258 of 1mj3A
- active site: A68 (≠ I76), M73 (≠ L81), S83 (≠ A108), L85 (≠ F110), G109 (= G131), E112 (≠ D134), P131 (≠ K153), E132 (= E154), T137 (≠ M159), P139 (≠ A161), G140 (≠ D162), K225 (≠ D248), F235 (≠ L258)
- binding hexanoyl-coenzyme a: K26 (≠ E34), A27 (≠ K35), L28 (≠ V36), A30 (= A38), A66 (= A74), G67 (= G75), A68 (≠ I76), D69 (= D77), I70 (≠ L78), G109 (= G131), P131 (≠ K153), E132 (= E154), L135 (≠ M157), G140 (≠ D162)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
29% identity, 93% coverage: 22:280/280 of query aligns to 14:259/260 of 2hw5C
- active site: A68 (≠ I76), M73 (≠ L81), S83 (≠ N95), L87 (= L99), G111 (= G131), E114 (≠ D134), P133 (≠ K153), E134 (= E154), T139 (≠ M159), P141 (≠ A161), G142 (≠ D162), K227 (≠ D248), F237 (≠ L258)
- binding crotonyl coenzyme a: K26 (≠ E34), A27 (≠ K35), L28 (≠ V36), A30 (= A38), K62 (= K70), I70 (≠ L78), F109 (≠ I129)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 95% coverage: 14:278/280 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (≠ I76), M69 (= M88), T75 (≠ N95), F79 (≠ L99), G103 (= G131), E106 (≠ D134), P125 (≠ K153), E126 (= E154), V131 (≠ M159), P133 (≠ A161), G134 (≠ D162), L219 (≠ D248), F229 (≠ L258)
- binding Butyryl Coenzyme A: F225 (≠ N254), F241 (≠ H270)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
29% identity, 94% coverage: 17:278/280 of query aligns to 7:258/261 of 5jbxB
- active site: A67 (≠ I76), R72 (≠ L81), L84 (≠ I103), R88 (≠ Q107), G112 (= G131), E115 (≠ D134), T134 (≠ K153), E135 (= E154), I140 (≠ M159), P142 (≠ A161), G143 (≠ D162), A228 (≠ D248), L238 (= L258)
- binding coenzyme a: S24 (≠ E34), R25 (≠ K35), R26 (≠ V36), A28 (= A38), A65 (= A74), D68 (= D77), L69 (= L78), K70 (≠ M79), L110 (≠ I129), G111 (= G130), T134 (≠ K153), E135 (= E154), L138 (≠ M157), R168 (≠ N187)
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
28% identity, 85% coverage: 14:250/280 of query aligns to 6:236/246 of 2vssD
- active site: M68 (≠ I76), Y73 (≠ M88), D78 (≠ G93), R90 (= R105), Q94 (= Q107), G118 (= G131), S121 (≠ D134), S140 (≠ K153), E141 (= E154), I146 (≠ M159), P148 (≠ A161), G149 (≠ D162)
- binding acetyl coenzyme *a: E26 (= E34), K27 (= K35), R28 (≠ V36), A30 (= A38), A66 (= A74), M68 (≠ I76), D69 (= D77), L70 (= L78), F74 (≠ G89), W114 (≠ Y127), F116 (≠ I129), S140 (≠ K153)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ I76), Y73 (≠ M88), F74 (≠ G89), Q96 (≠ S109), E141 (= E154), G149 (≠ D162), N150 (≠ V163)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
28% identity, 85% coverage: 14:250/280 of query aligns to 5:235/247 of 2vssB
- active site: M67 (≠ I76), Y72 (≠ M88), D77 (≠ G93), R89 (= R105), Q93 (= Q107), G117 (= G131), S120 (≠ D134), S139 (≠ K153), E140 (= E154), I145 (≠ M159), P147 (≠ A161), G148 (≠ D162)
- binding acetyl coenzyme *a: E25 (= E34), K26 (= K35), R27 (≠ V36), A29 (= A38), A65 (= A74), M67 (≠ I76), D68 (= D77), W113 (≠ Y127), F115 (≠ I129), G117 (= G131), S139 (≠ K153), E140 (= E154)
Sites not aligning to the query:
O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
29% identity, 85% coverage: 14:250/280 of query aligns to 8:238/276 of O69762
- K29 (= K35) binding
- A68 (= A74) binding
- M70 (≠ I76) binding
- L72 (= L78) binding
- Y75 (≠ M88) binding
- G120 (= G131) binding
- S123 (≠ D134) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ K153) binding
- E143 (= E154) mutation to A: Abolishes catalytic activity.
- W146 (≠ M157) binding
- G151 (vs. gap) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 239 binding ; Y→F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
28% identity, 93% coverage: 20:278/280 of query aligns to 8:254/257 of 6slbAAA
- active site: Q64 (≠ I76), F69 (≠ L81), L80 (≠ A96), N84 (≠ R100), A108 (≠ G131), S111 (≠ D134), A130 (≠ K153), F131 (≠ E154), L136 (≠ M159), P138 (≠ A161), D139 (= D162), A224 (≠ D248), G234 (≠ L258)
- 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 (≠ K70), A62 (= A74), Q64 (≠ I76), D65 (= D77), L66 (= L78), Y76 (≠ V92), A108 (≠ G131), F131 (≠ E154), D139 (= D162)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
29% identity, 85% coverage: 14:250/280 of query aligns to 7:232/244 of 6l3pA
- active site: M69 (≠ I76), Y74 (≠ V92), R86 (= R105), Q90 (= Q107), G114 (= G131), S117 (≠ D134), S136 (≠ K153), E137 (= E154), I142 (vs. gap), P144 (vs. gap), G145 (vs. gap)
- binding coenzyme a: K28 (= K35), R29 (≠ V36), A31 (= A38), A67 (= A74), M69 (≠ I76), D70 (= D77), L71 (= L78), G113 (= G130)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
27% identity, 93% coverage: 20:278/280 of query aligns to 5:242/245 of 6slaAAA
- active site: Q61 (≠ I76), L68 (≠ I103), N72 (≠ Q107), A96 (≠ G131), S99 (≠ D134), A118 (≠ K153), F119 (≠ E154), L124 (≠ M159), P126 (≠ A161), N127 (≠ D162), A212 (≠ D248), G222 (≠ L258)
- 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 (≠ V36), A59 (= A74), Q61 (≠ I76), D62 (= D77), L63 (= L78), L68 (≠ I103), Y71 (≠ L106), A94 (≠ I129), G95 (= G130), A96 (≠ G131), F119 (≠ E154), I122 (≠ M157), L124 (≠ M159), N127 (≠ D162), F234 (≠ H270), K237 (= K273)
Query Sequence
>PP_4030 FitnessBrowser__Putida:PP_4030
MNLSTSGVLPVTEYSAFKVELTDSVAHVQINRPEKVNAMNAAFWEEIVDIFQWIDDTDAV
RVVVISGAGKHFSAGIDLMMLASLAGQMGKDVGRNARFLRKTIQRLQASFTAVDACRKPV
LAAVQGYCIGGAIDLISACDMRYCSRDAQFSIKEIDMGMAADVGTLQRLPRIIGDGIMRE
LAFTGRNVEADEALRIGLVNRVYDDQAALMDGVFAIAREIAAKSPIAVAGTKEMLSYMRD
HRIDDGLDYIATWNAAMLQSEDLRVAVAAHMSKQKPTFAD
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