SitesBLAST
Comparing 5210128 FitnessBrowser__PV4:5210128 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)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
32% identity, 85% coverage: 17:243/266 of query aligns to 12:245/246 of 6p5uE
- active site: M67 (≠ A72), Y72 (≠ W76), D77 (vs. gap), R89 (≠ D91), A93 (= A96), G117 (= G120), T120 (≠ G123), E140 (= E143), I145 (≠ L148), P147 (= P150), A148 (= A151), A236 (= A234)
- binding coenzyme a: D25 (= D30), K26 (= K31), R27 (≠ H32), A29 (= A34), A65 (= A70), M67 (≠ A72), D68 (= D73), L69 (= L74), W113 (≠ A116), F115 (= F118), S139 (= S142), W143 (≠ L146)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
26% identity, 97% coverage: 9:266/266 of query aligns to 2:258/259 of 5zaiC
- active site: A65 (= A72), F70 (≠ M77), S82 (≠ L89), R86 (≠ N93), G110 (= G120), E113 (≠ G123), P132 (≠ S142), E133 (= E143), I138 (≠ L148), P140 (= P150), G141 (≠ A151), A226 (= A234), F236 (≠ R244)
- binding coenzyme a: K24 (= K31), L25 (≠ H32), A63 (= A70), G64 (= G71), A65 (= A72), D66 (= D73), I67 (≠ L74), P132 (≠ S142), R166 (= R175), F248 (= F256), K251 (= K259)
6n97A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- amino(dethia)-coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 2:257/260 of 6n97A
- active site: H65 (≠ A72), L70 (≠ M77), G109 (= G120), E112 (≠ G123), P132 (≠ E143), V137 (≠ L148), Y139 (≠ P150), E227 (= E238), Y237 (vs. gap)
- binding (2R)-sulfonatepropionyl-amino(dethia)-CoA: L24 (≠ H32), K59 (≠ R66), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), L135 (= L146), Y139 (≠ P150), F249 (= F256), K252 (= K259)
- binding (2S)-sulfonatepropionyl-amino(dethia)-CoA: L24 (≠ H32), K59 (≠ R66), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), L135 (= L146), Y139 (≠ P150), F249 (= F256), K252 (= K259)
6n96A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- oxa(dethia)-coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 2:257/260 of 6n96A
- active site: H65 (≠ A72), L70 (≠ M77), G109 (= G120), E112 (≠ G123), P132 (≠ E143), V137 (≠ L148), Y139 (≠ P150), E227 (= E238), Y237 (vs. gap)
- binding (2~{S})-1-[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]ethoxy]-1-oxidanylidene-propane-2-sulfonic acid: K59 (≠ R66), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), H68 (≠ N75), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), L135 (= L146), V137 (≠ L148), Y139 (≠ P150), F249 (= F256), K252 (= K259)
- binding (2~{R})-1-[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]ethoxy]-1-oxidanylidene-propane-2-sulfonic acid: K59 (≠ R66), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), H68 (≠ N75), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), L135 (= L146), V137 (≠ L148), Y139 (≠ P150), F249 (= F256), K252 (= K259)
6n95A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 2:257/260 of 6n95A
- active site: H65 (≠ A72), L70 (≠ M77), G109 (= G120), E112 (≠ G123), P132 (≠ E143), V137 (≠ L148), Y139 (≠ P150), E227 (= E238), Y237 (vs. gap)
- binding (2R)-sulfonatepropionyl-CoA: K23 (= K31), L24 (≠ H32), K59 (≠ R66), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), H68 (≠ N75), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), L135 (= L146), Y139 (≠ P150), F249 (= F256), K252 (= K259)
- binding (2S)-sulfonatepropionyl-CoA: K23 (= K31), L24 (≠ H32), K59 (≠ R66), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), H68 (≠ N75), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), L135 (= L146), V137 (≠ L148), Y139 (≠ P150), F249 (= F256), K252 (= K259)
6n94A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- amino(dethia)-coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 2:257/260 of 6n94A
- active site: H65 (≠ A72), L70 (≠ M77), G109 (= G120), E112 (≠ G123), P132 (≠ E143), V137 (≠ L148), Y139 (≠ P150), E227 (= E238), Y237 (vs. gap)
- binding [1-[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]ethylamino]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: K23 (= K31), L24 (≠ H32), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), H68 (≠ N75), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), Y139 (≠ P150)
6n93A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- oxa(dethia)-coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 2:257/260 of 6n93A
- active site: H65 (≠ A72), L70 (≠ M77), G109 (= G120), E112 (≠ G123), P132 (≠ E143), V137 (≠ L148), Y139 (≠ P150), E227 (= E238), Y237 (vs. gap)
- binding [1-[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]ethoxy]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: L24 (≠ H32), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), H68 (≠ N75), W107 (≠ F118), T131 (≠ S142), L135 (= L146), F249 (= F256), K252 (= K259)
6n92F Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 2:257/260 of 6n92F
- active site: H65 (≠ A72), L70 (≠ M77), G109 (= G120), E112 (≠ G123), P132 (≠ E143), V137 (≠ L148), Y139 (≠ P150), E227 (= E238), Y237 (vs. gap)
- binding [1-[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]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: R22 (≠ D30), K23 (= K31), L24 (≠ H32), A63 (= A70), H65 (≠ A72), D66 (= D73), S105 (≠ A116), W107 (≠ F118), W107 (≠ F118), G108 (= G119), G109 (= G120), T127 (≠ S138), F128 (= F139), S129 (≠ C140), T131 (≠ S142), P132 (≠ E143), Y139 (≠ P150), S164 (≠ E174), P165 (≠ R175), F249 (= F256)
- binding (2E)-2-(hydroxyimino)propanoic acid: E240 (≠ D247)
Sites not aligning to the query:
6n92A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 2:257/260 of 6n92A
- active site: H65 (≠ A72), L70 (≠ M77), G109 (= G120), E112 (≠ G123), P132 (≠ E143), V137 (≠ L148), Y139 (≠ P150), E227 (= E238), Y237 (vs. gap)
- binding [1-[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]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: L24 (≠ H32), A63 (= A70), H65 (≠ A72), D66 (= D73), I67 (≠ L74), H68 (≠ N75), W107 (≠ F118), G108 (= G119), G109 (= G120), T131 (≠ S142), P132 (≠ E143), Y139 (≠ P150), F249 (= F256), K252 (= K259)
1ef9A The crystal structure of methylmalonyl coa decarboxylase complexed with 2s-carboxypropyl coa (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 3:258/261 of 1ef9A
- active site: H66 (≠ A72), L71 (≠ M77), D82 (≠ A92), R86 (≠ A96), G110 (= G120), E113 (≠ G123), P133 (≠ E143), V138 (≠ L148), Y140 (≠ P150), N141 (≠ A151), E228 (= E238), Y238 (vs. gap)
- binding 2-carboxypropyl-coenzyme a: A64 (= A70), H66 (≠ A72), D67 (= D73), I68 (≠ L74), H69 (≠ N75), W108 (≠ F118), G110 (= G120), T132 (≠ S142), P133 (≠ E143), K253 (= K259)
P52045 Methylmalonyl-CoA decarboxylase; MMCD; Transcarboxylase; EC 4.1.1.- from Escherichia coli (strain K12) (see paper)
27% identity, 96% coverage: 10:264/266 of query aligns to 3:258/261 of P52045
- G110 (= G120) binding
- T132 (≠ S142) binding
- K253 (= K259) binding
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
28% identity, 92% coverage: 18:262/266 of query aligns to 31:276/285 of Q7CQ56
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
28% identity, 92% coverage: 18:262/266 of query aligns to 27:257/266 of 3h02A
- active site: G82 (≠ A72), H86 (≠ W76), L90 (≠ M83), G114 (= G120), V117 (≠ G123), G137 (≠ E143), S142 (≠ L148), D144 (≠ P150), G145 (≠ A151), A231 (= A234), Y239 (≠ R244)
- binding bicarbonate ion: G113 (= G119), Q135 (≠ L141), G137 (≠ E143), W165 (≠ M170)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
27% identity, 92% coverage: 18:262/266 of query aligns to 27:272/281 of 3t88A
- active site: G82 (≠ A72), R87 (≠ K82), Y93 (≠ N88), H101 (vs. gap), L105 (≠ A96), G129 (= G120), V132 (≠ G123), G152 (≠ E143), S157 (≠ L148), D159 (≠ P150), G160 (≠ A151), A246 (= A234), Y254 (≠ R244)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D30), V40 (≠ K31), R41 (≠ H32), A43 (= A34), S80 (≠ A70), G81 (= G71), G82 (≠ A72), D83 (= D73), Q84 (≠ K79), K85 (≠ Q80), Y93 (≠ N88), V104 (≠ L95), L105 (≠ A96), Y125 (≠ A116), G129 (= G120), T151 (≠ S142), V155 (≠ L146), F158 (≠ I149), D159 (≠ P150), T250 (≠ E238), Y254 (≠ R244), F266 (= F256), K269 (= K259)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
27% identity, 92% coverage: 18:262/266 of query aligns to 31:276/285 of 4i42A
- active site: G86 (≠ A72), R91 (≠ K82), Y97 (≠ N88), H105 (vs. gap), L109 (≠ A96), G133 (= G120), V136 (≠ G123), G156 (≠ E143), S161 (≠ L148), D163 (≠ P150), G164 (≠ A151), A250 (= A234), Y258 (≠ R244)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K31), R45 (≠ H32), S84 (≠ A70), G85 (= G71), G86 (≠ A72), D87 (= D73), Q88 (≠ K79), K89 (≠ Q80), Y97 (≠ N88), V108 (≠ L95), Y129 (≠ A116), G133 (= G120), T155 (≠ S142), S161 (≠ L148), T254 (≠ E238), F270 (= F256), K273 (= K259)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 92% coverage: 18:262/266 of query aligns to 31:276/285 of P0ABU0
- R45 (≠ H32) binding in other chain
- SGGD-----QK 84:89 (≠ AGADLNWMRKQ 70:80) binding in other chain
- K89 (≠ Q80) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ K82) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ N88) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAFGG 116:120) binding in other chain
- Q154 (≠ L141) 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 (≠ LSE 141:143) binding
- T155 (≠ S142) binding in other chain
- G156 (≠ E143) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L148) binding in other chain
- W184 (≠ M170) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R244) binding
- R267 (≠ L253) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F256) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K259) binding ; mutation to A: Impairs protein folding.
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
27% identity, 92% coverage: 18:262/266 of query aligns to 28:258/267 of 4elwA
- active site: G83 (≠ A72), L91 (≠ M83), G115 (= G120), V118 (≠ G123), G138 (≠ E143), S143 (≠ L148), D145 (≠ P150), G146 (≠ A151), A232 (= A234), Y240 (≠ R244)
- binding nitrate ion: G114 (= G119), T137 (≠ S142), G138 (≠ E143), F144 (≠ I149), W166 (≠ M170)
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)
27% identity, 70% coverage: 5:189/266 of query aligns to 3:190/276 of O69762
- K29 (= K31) binding
- A68 (= A70) binding
- M70 (≠ A72) binding
- L72 (= L74) binding
- Y75 (≠ M77) binding
- G120 (= G120) binding
- S123 (≠ G123) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S142) binding
- E143 (= E143) mutation to A: Abolishes catalytic activity.
- W146 (≠ L146) binding
- G151 (≠ A151) 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.
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
27% identity, 70% coverage: 5:189/266 of query aligns to 1:188/246 of 2vssD
- active site: M68 (≠ A72), Y73 (≠ M77), D78 (vs. gap), R90 (≠ S90), Q94 (≠ E94), G118 (= G120), S121 (≠ G123), S140 (= S142), E141 (= E143), I146 (≠ L148), P148 (= P150), G149 (≠ A151)
- binding acetyl coenzyme *a: E26 (≠ D30), K27 (= K31), R28 (≠ H32), A30 (= A34), A66 (= A70), M68 (≠ A72), D69 (= D73), L70 (= L74), F74 (≠ R78), W114 (≠ A116), F116 (= F118), S140 (= S142)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A72), Y73 (≠ M77), F74 (≠ R78), Q96 (≠ A96), E141 (= E143), G149 (≠ A151), N150 (vs. gap)
Sites not aligning to the query:
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
29% identity, 65% coverage: 17:189/266 of query aligns to 14:184/244 of 6l3pA
- active site: M69 (≠ A72), Y74 (≠ M77), R86 (≠ S90), Q90 (≠ E94), G114 (= G120), S117 (≠ G123), S136 (= S142), E137 (= E143), I142 (≠ L148), P144 (= P150), G145 (≠ A151)
- binding coenzyme a: K28 (= K31), R29 (≠ H32), A31 (= A34), A67 (= A70), M69 (≠ A72), D70 (= D73), L71 (= L74), G113 (= G119)
Sites not aligning to the query:
Query Sequence
>5210128 FitnessBrowser__PV4:5210128
MTSQTITQEFEYLSCALSDGVGEMVLDRADKHNAFDEVMIAEMIAALDLFAADDSCQLLV
LKANGRNFSAGADLNWMRKQAKMDFEQNLSDANELATLMHKLDKFPKPTLALVQGAAFGG
ALGLICASDIAIADSRASFCLSEVKLGLIPAVISPYVVRAMGQRASRRYMLTAERFDAET
ALKLNVIHEINDDLEGASAPIITALKGNSPQGMAWVKTLLSRLEDGVIDQETLAYTSERI
ARIRVSDEGQEGLNAFFEKRSPRWNA
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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