SitesBLAST
Comparing 201057 FitnessBrowser__MR1:201057 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)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
30% identity, 83% coverage: 20:257/288 of query aligns to 1:245/246 of 6p5uE
- active site: M67 (≠ A86), Y72 (≠ F99), D77 (≠ N104), R89 (vs. gap), A93 (vs. gap), G117 (= G134), T120 (≠ G137), E140 (= E157), I145 (≠ L162), P147 (= P164), A148 (= A165), A236 (≠ D248)
- binding coenzyme a: D25 (≠ E44), K26 (≠ V45), R27 (≠ H46), A29 (= A48), A65 (= A84), M67 (≠ A86), D68 (= D87), L69 (= L88), W113 (≠ A130), F115 (= F132), S139 (= S156), W143 (≠ L160)
Sites not aligning to the query:
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, 85% coverage: 33:278/288 of query aligns to 32:278/285 of Q7CQ56
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
28% identity, 83% coverage: 22:261/288 of query aligns to 5:243/244 of 6l3pA
- active site: M69 (≠ A86), Y74 (≠ Q94), R86 (≠ A106), Q90 (≠ A110), G114 (= G134), S117 (≠ G137), S136 (= S156), E137 (= E157), I142 (≠ L162), P144 (= P164), G145 (≠ A165), Y233 (≠ S251), D243 (= D261)
- binding coenzyme a: K28 (≠ V45), R29 (≠ H46), A31 (= A48), A67 (= A84), M69 (≠ A86), D70 (= D87), L71 (= L88), G113 (= G133)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
28% identity, 85% coverage: 33:278/288 of query aligns to 28:259/266 of 3h02A
- active site: G82 (≠ A86), H86 (≠ W90), L90 (≠ M97), G114 (= G134), V117 (≠ G137), G137 (≠ E157), S142 (≠ L162), D144 (≠ P164), G145 (≠ A165), A231 (≠ D248), Y239 (≠ R258)
- binding bicarbonate ion: G113 (= G133), Q135 (≠ L155), G137 (≠ E157), W165 (≠ M184)
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)
28% identity, 88% coverage: 22:274/288 of query aligns to 6:265/276 of O69762
- K29 (≠ V45) binding
- A68 (= A84) binding
- M70 (≠ A86) binding
- L72 (= L88) binding
- Y75 (≠ W90) binding
- G120 (= G134) binding
- S123 (≠ G137) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S156) binding
- E143 (= E157) mutation to A: Abolishes catalytic activity.
- W146 (≠ L160) binding
- G151 (≠ A165) binding
- Y239 (≠ S251) binding ; mutation to 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 63% coverage: 22:203/288 of query aligns to 3:187/247 of 2vssB
- active site: M67 (≠ A86), Y72 (≠ W90), D77 (≠ Q94), R89 (≠ A106), Q93 (≠ A110), G117 (= G134), S120 (≠ G137), S139 (= S156), E140 (= E157), I145 (≠ L162), P147 (= P164), G148 (≠ A165)
- binding acetyl coenzyme *a: E25 (= E44), K26 (≠ V45), R27 (≠ H46), A29 (= A48), A65 (= A84), M67 (≠ A86), D68 (= D87), W113 (≠ A130), F115 (= F132), G117 (= G134), S139 (= S156), E140 (= E157)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 63% coverage: 22:203/288 of query aligns to 4:188/246 of 2vssD
- active site: M68 (≠ A86), Y73 (≠ W90), D78 (≠ Q94), R90 (≠ A106), Q94 (≠ A110), G118 (= G134), S121 (≠ G137), S140 (= S156), E141 (= E157), I146 (≠ L162), P148 (= P164), G149 (≠ A165)
- binding acetyl coenzyme *a: E26 (= E44), K27 (≠ V45), R28 (≠ H46), A30 (= A48), A66 (= A84), M68 (≠ A86), D69 (= D87), L70 (= L88), F74 (≠ M91), W114 (≠ A130), F116 (= F132), S140 (= S156)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A86), Y73 (≠ W90), F74 (≠ M91), Q96 (≠ L112), E141 (= E157), G149 (≠ A165), N150 (vs. gap)
Sites not aligning to the query:
1ef9A The crystal structure of methylmalonyl coa decarboxylase complexed with 2s-carboxypropyl coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 4:258/261 of 1ef9A
- active site: H66 (≠ A86), L71 (≠ M91), D82 (= D100), R86 (≠ K107), G110 (= G134), E113 (≠ G137), P133 (≠ E157), V138 (≠ L162), Y140 (≠ P164), N141 (≠ A165), E228 (= E252), Y238 (vs. gap)
- binding 2-carboxypropyl-coenzyme a: A64 (= A84), H66 (≠ A86), D67 (= D87), I68 (≠ L88), H69 (≠ N89), W108 (≠ F132), G110 (= G134), T132 (≠ S156), P133 (≠ E157), K253 (= K273)
P52045 Methylmalonyl-CoA decarboxylase; MMCD; Transcarboxylase; EC 4.1.1.- from Escherichia coli (strain K12) (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 4:258/261 of P52045
- G110 (= G134) binding
- T132 (≠ S156) binding
- K253 (= K273) binding
6n97A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- amino(dethia)-coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 3:257/260 of 6n97A
- active site: H65 (≠ A86), L70 (≠ M91), G109 (= G134), E112 (≠ G137), P132 (≠ E157), V137 (≠ L162), Y139 (≠ P164), E227 (= E252), Y237 (vs. gap)
- binding (2R)-sulfonatepropionyl-amino(dethia)-CoA: L24 (≠ H46), K59 (= K80), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), L135 (= L160), Y139 (≠ P164), F249 (= F270), K252 (= K273)
- binding (2S)-sulfonatepropionyl-amino(dethia)-CoA: L24 (≠ H46), K59 (= K80), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), L135 (= L160), Y139 (≠ P164), F249 (= F270), K252 (= K273)
6n96A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- oxa(dethia)-coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 3:257/260 of 6n96A
- active site: H65 (≠ A86), L70 (≠ M91), G109 (= G134), E112 (≠ G137), P132 (≠ E157), V137 (≠ L162), Y139 (≠ P164), E227 (= E252), 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 (= K80), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), H68 (≠ N89), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), L135 (= L160), V137 (≠ L162), Y139 (≠ P164), F249 (= F270), K252 (= K273)
- 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 (= K80), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), H68 (≠ N89), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), L135 (= L160), V137 (≠ L162), Y139 (≠ P164), F249 (= F270), K252 (= K273)
6n95A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 3:257/260 of 6n95A
- active site: H65 (≠ A86), L70 (≠ M91), G109 (= G134), E112 (≠ G137), P132 (≠ E157), V137 (≠ L162), Y139 (≠ P164), E227 (= E252), Y237 (vs. gap)
- binding (2R)-sulfonatepropionyl-CoA: K23 (≠ V45), L24 (≠ H46), K59 (= K80), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), H68 (≠ N89), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), L135 (= L160), Y139 (≠ P164), F249 (= F270), K252 (= K273)
- binding (2S)-sulfonatepropionyl-CoA: K23 (≠ V45), L24 (≠ H46), K59 (= K80), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), H68 (≠ N89), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), L135 (= L160), V137 (≠ L162), Y139 (≠ P164), F249 (= F270), K252 (= K273)
6n94A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- amino(dethia)-coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 3:257/260 of 6n94A
- active site: H65 (≠ A86), L70 (≠ M91), G109 (= G134), E112 (≠ G137), P132 (≠ E157), V137 (≠ L162), Y139 (≠ P164), E227 (= E252), 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 (≠ V45), L24 (≠ H46), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), H68 (≠ N89), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), Y139 (≠ P164)
6n93A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- oxa(dethia)-coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 3:257/260 of 6n93A
- active site: H65 (≠ A86), L70 (≠ M91), G109 (= G134), E112 (≠ G137), P132 (≠ E157), V137 (≠ L162), Y139 (≠ P164), E227 (= E252), 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 (≠ H46), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), H68 (≠ N89), W107 (≠ F132), T131 (≠ S156), L135 (= L160), F249 (= F270), K252 (= K273)
6n92F Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 3:257/260 of 6n92F
- active site: H65 (≠ A86), L70 (≠ M91), G109 (= G134), E112 (≠ G137), P132 (≠ E157), V137 (≠ L162), Y139 (≠ P164), E227 (= E252), 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 (≠ E44), K23 (≠ V45), L24 (≠ H46), A63 (= A84), H65 (≠ A86), D66 (= D87), S105 (≠ A130), W107 (≠ F132), W107 (≠ F132), G108 (= G133), G109 (= G134), T127 (≠ S152), F128 (= F153), S129 (≠ C154), T131 (≠ S156), P132 (≠ E157), Y139 (≠ P164), S164 (≠ E188), P165 (≠ R189), F249 (= F270)
- binding (2E)-2-(hydroxyimino)propanoic acid: E240 (≠ D261)
Sites not aligning to the query:
6n92A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa (see paper)
28% identity, 88% coverage: 25:278/288 of query aligns to 3:257/260 of 6n92A
- active site: H65 (≠ A86), L70 (≠ M91), G109 (= G134), E112 (≠ G137), P132 (≠ E157), V137 (≠ L162), Y139 (≠ P164), E227 (= E252), 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 (≠ H46), A63 (= A84), H65 (≠ A86), D66 (= D87), I67 (≠ L88), H68 (≠ N89), W107 (≠ F132), G108 (= G133), G109 (= G134), T131 (≠ S156), P132 (≠ E157), Y139 (≠ P164), F249 (= F270), K252 (= K273)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
27% identity, 85% coverage: 33:278/288 of query aligns to 28:274/281 of 3t88A
- active site: G82 (≠ A86), R87 (≠ K96), Y93 (≠ N102), H101 (vs. gap), L105 (≠ A110), G129 (= G134), V132 (≠ G137), G152 (≠ E157), S157 (≠ L162), D159 (≠ P164), G160 (≠ A165), A246 (≠ D248), Y254 (≠ R258)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E44), V40 (= V45), R41 (≠ H46), A43 (= A48), S80 (≠ A84), G81 (= G85), G82 (≠ A86), D83 (= D87), Q84 (≠ K93), K85 (≠ Q94), Y93 (≠ N102), V104 (≠ L109), L105 (≠ A110), Y125 (≠ A130), G129 (= G134), T151 (≠ S156), V155 (≠ L160), F158 (≠ I163), D159 (≠ P164), T250 (≠ E252), Y254 (≠ R258), F266 (= F270), K269 (= K273)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
27% identity, 85% coverage: 33:278/288 of query aligns to 32:278/285 of 4i42A
- active site: G86 (≠ A86), R91 (≠ K96), Y97 (≠ N102), H105 (vs. gap), L109 (≠ A110), G133 (= G134), V136 (≠ G137), G156 (≠ E157), S161 (≠ L162), D163 (≠ P164), G164 (≠ A165), A250 (≠ D248), Y258 (≠ R258)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V45), R45 (≠ H46), S84 (≠ A84), G85 (= G85), G86 (≠ A86), D87 (= D87), Q88 (≠ K93), K89 (≠ Q94), Y97 (≠ N102), V108 (≠ L109), Y129 (≠ A130), G133 (= G134), T155 (≠ S156), S161 (≠ L162), T254 (≠ E252), F270 (= F270), K273 (= K273)
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, 85% coverage: 33:278/288 of query aligns to 32:278/285 of P0ABU0
- R45 (≠ H46) binding in other chain
- SGGD-----QK 84:89 (≠ AGADLNWMRKQ 84:94) binding in other chain
- K89 (≠ Q94) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ K96) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ N102) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAFGG 130:134) binding in other chain
- Q154 (≠ L155) 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 155:157) binding
- T155 (≠ S156) binding in other chain
- G156 (≠ E157) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L162) binding in other chain
- W184 (≠ M184) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R258) binding
- R267 (≠ L267) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F270) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K273) binding ; mutation to A: Impairs protein folding.
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
26% identity, 90% coverage: 19:278/288 of query aligns to 7:266/273 of Q5HH38
- R34 (≠ H46) binding in other chain
- SGGDQ 73:77 (≠ AGADL 84:88) binding in other chain
- S149 (≠ L162) binding in other chain
Query Sequence
>201057 FitnessBrowser__MR1:201057
MTDTQHQNTSTQSLGHLQHALGHLQHVSYALDNGVGELILNRAEVHNAFDEVMISEMIAV
LGYFAERQDCKLLLLKANGKNFSAGADLNWMRKQAKMDFDQNLNDAKALAKLMQDLDTFP
KPTIALVQGAAFGGALGLICASDIAIATERASFCLSEVKLGLIPAVISPYVARAMGNRAS
RRYMLTAERFDAQTALKLNVIHEINDDLEAAAQPIITALLANSPQGMAWVKTLLTRLEDG
VIDQDTIDYTSERIARIRVSDEGQEGLNAFFEKRQPNWHTPTDTQGVL
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