SitesBLAST
Comparing H281DRAFT_01344 FitnessBrowser__Burk376:H281DRAFT_01344 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)
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)
35% identity, 95% coverage: 13:260/261 of query aligns to 20:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
28% identity, 100% coverage: 1:260/261 of query aligns to 1:257/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (≠ A89), R86 (vs. gap), G110 (= G113), E113 (≠ G116), P132 (≠ S135), E133 (= E136), I138 (≠ L141), P140 (= P143), G141 (≠ A144), A226 (= A232), F236 (≠ R239)
- binding coenzyme a: K24 (≠ V24), L25 (≠ R25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), P132 (≠ S135), R166 (≠ Q168), F248 (= F251), K251 (= K254)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 97% coverage: 8:261/261 of query aligns to 12:265/266 of O53561
- K135 (≠ R131) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 131:138, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R138) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 99% coverage: 1:259/261 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (= M70), T80 (≠ N81), F84 (≠ M86), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (≠ I228), F234 (≠ A240)
- binding acetoacetyl-coenzyme a: Q23 (≠ D23), A24 (≠ V24), L25 (≠ R25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), K68 (≠ N68), M70 (= M70), F84 (≠ M86), G107 (≠ A112), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), P138 (= P143), G139 (≠ A144), M140 (≠ T145)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 99% coverage: 1:259/261 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M70), T80 (≠ N81), F84 (≠ M86), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (≠ I228), F234 (≠ A240)
- binding coenzyme a: L25 (≠ R25), A63 (= A63), I67 (≠ L67), K68 (≠ N68), Y104 (≠ D109), P130 (≠ S135), E131 (= E136), L134 (= L139)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 98% coverage: 3:259/261 of query aligns to 2:253/256 of 3h81A
- active site: A64 (= A65), M69 (= M70), T79 (≠ N81), F83 (≠ M86), G107 (= G113), E110 (≠ G116), P129 (≠ S135), E130 (= E136), V135 (≠ L141), P137 (= P143), G138 (≠ A144), L223 (≠ I228), F233 (≠ A240)
- binding calcium ion: F233 (≠ A240), Q238 (≠ R245)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
33% identity, 80% coverage: 5:213/261 of query aligns to 7:218/246 of 6p5uE
- active site: M67 (≠ A65), Y72 (= Y76), D77 (≠ N81), R89 (vs. gap), A93 (vs. gap), G117 (= G113), T120 (≠ G116), E140 (= E136), I145 (≠ L141), P147 (= P143), A148 (= A144)
- binding coenzyme a: D25 (= D23), K26 (≠ V24), R27 (= R25), A29 (= A27), A65 (= A63), M67 (≠ A65), D68 (= D66), L69 (= L67), W113 (≠ D109), F115 (≠ Y111), S139 (= S135), W143 (≠ L139)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 98% coverage: 3:259/261 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (≠ N81), F79 (≠ M86), G103 (= G113), E106 (≠ G116), P125 (≠ S135), E126 (= E136), V131 (≠ L141), P133 (= P143), G134 (≠ A144), L219 (≠ I228), F229 (≠ A240)
- binding Butyryl Coenzyme A: F225 (≠ A236), F241 (= F251)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 99% coverage: 2:260/261 of query aligns to 3:259/261 of 5jbxB
- active site: A67 (= A65), R72 (≠ M73), L84 (≠ A85), R88 (≠ A89), G112 (= G113), E115 (≠ G116), T134 (≠ S135), E135 (= E136), I140 (≠ L141), P142 (= P143), G143 (≠ A144), A228 (≠ I228), L238 (≠ A236)
- binding coenzyme a: S24 (≠ D23), R25 (≠ V24), R26 (= R25), A28 (= A27), A65 (= A63), D68 (= D66), L69 (= L67), K70 (= K71), L110 (≠ Y111), G111 (≠ A112), T134 (≠ S135), E135 (= E136), L138 (= L139), R168 (≠ Q168)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
30% identity, 93% coverage: 14:257/261 of query aligns to 34:276/285 of Q7CQ56
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
29% identity, 93% coverage: 14:257/261 of query aligns to 30:272/281 of 3t88A
- active site: G82 (≠ A65), R87 (≠ M70), Y93 (= Y76), H101 (≠ D84), L105 (= L88), G129 (= G113), V132 (≠ G116), G152 (≠ E136), S157 (≠ L141), D159 (≠ P143), G160 (≠ A144), A246 (≠ I228), Y254 (≠ A236)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D23), V40 (= V24), R41 (= R25), A43 (= A27), S80 (≠ A63), G81 (= G64), G82 (≠ A65), D83 (= D66), Q84 (≠ L67), K85 (≠ N68), Y93 (= Y76), V104 (≠ L87), L105 (= L88), Y125 (≠ D109), G129 (= G113), T151 (≠ S135), V155 (≠ L139), F158 (≠ I142), D159 (≠ P143), T250 (≠ A232), Y254 (≠ A236), F266 (= F251), K269 (= K254)
7xwvA Feruloyl-coa hydratase/lyase complexed with vanillin and coenzyme a (see paper)
31% identity, 86% coverage: 4:228/261 of query aligns to 5:234/244 of 7xwvA
- binding coenzyme a: T24 (≠ D23), K25 (≠ V24), R26 (= R25), A64 (= A63), G65 (= G64), M66 (≠ A65), D67 (= D66), L68 (= L67), W111 (≠ D109), F113 (≠ Y111), G114 (≠ A112), G115 (= G113), S137 (= S135)
- binding 4-hydroxy-3-methoxybenzaldehyde: M66 (≠ A65), Y71 (≠ W69), F72 (≠ M70), E138 (= E136), G146 (≠ A144), G147 (≠ T145)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
29% identity, 93% coverage: 14:257/261 of query aligns to 34:276/285 of 4i42A
- active site: G86 (≠ A65), R91 (≠ M70), Y97 (= Y76), H105 (≠ D84), L109 (= L88), G133 (= G113), V136 (≠ G116), G156 (≠ E136), S161 (≠ L141), D163 (≠ P143), G164 (≠ A144), A250 (≠ I228), Y258 (≠ A236)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V24), R45 (= R25), S84 (≠ A63), G85 (= G64), G86 (≠ A65), D87 (= D66), Q88 (≠ L67), K89 (≠ N68), Y97 (= Y76), V108 (≠ L87), Y129 (≠ D109), G133 (= G113), T155 (≠ S135), S161 (≠ L141), T254 (≠ A232), F270 (= F251), K273 (= K254)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
29% identity, 93% coverage: 14:257/261 of query aligns to 34:276/285 of P0ABU0
- R45 (= R25) binding in other chain
- SGGDQK 84:89 (≠ AGADLN 63:68) binding in other chain
- K89 (≠ N68) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M70) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y76) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ DAYAG 109:113) binding in other chain
- Q154 (≠ L134) 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 134:136) binding
- T155 (≠ S135) binding in other chain
- G156 (≠ E136) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L141) binding in other chain
- W184 (≠ F163) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ A236) binding
- R267 (= R245) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F251) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K254) binding ; mutation to A: Impairs protein folding.
7xwtB Crystal structure of feruoyl-coa hydratase/lyase complexed with coa from sphingomonas paucimobilis (see paper)
31% identity, 86% coverage: 4:228/261 of query aligns to 6:235/277 of 7xwtB
- binding acetyl coenzyme *a: T25 (≠ D23), K26 (≠ V24), R27 (= R25), A29 (= A27), A65 (= A63), G66 (= G64), M67 (≠ A65), D68 (= D66), L69 (= L67), F73 (≠ M70), F114 (≠ Y111), G116 (= G113), S138 (= S135), W142 (≠ L139)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
31% identity, 81% coverage: 2:212/261 of query aligns to 6:214/244 of 6l3pA
- active site: M69 (≠ A65), Y74 (≠ M70), R86 (≠ A83), Q90 (≠ L87), G114 (= G113), S117 (≠ G116), S136 (= S135), E137 (= E136), I142 (≠ L141), P144 (= P143), G145 (≠ A144)
- binding coenzyme a: K28 (≠ V24), R29 (= R25), A31 (= A27), A67 (= A63), M69 (≠ A65), D70 (= D66), L71 (= L67), G113 (≠ A112)
Sites not aligning to the query:
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
30% identity, 98% coverage: 2:257/261 of query aligns to 11:264/273 of Q5HH38
- R34 (= R25) binding in other chain
- SGGDQ 73:77 (≠ AGADL 63:67) binding in other chain
- S149 (≠ L141) binding in other chain
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
29% identity, 98% coverage: 2:257/261 of query aligns to 6:251/260 of 2uzfA
- active site: G70 (≠ A65), R80 (= R82), L84 (≠ M86), G108 (= G113), V111 (≠ G116), T130 (≠ S135), G131 (≠ E136), S136 (≠ L141), D138 (≠ P143), A139 (= A144), A225 (≠ I228), Y233 (≠ A236)
- binding acetoacetyl-coenzyme a: V28 (= V24), R29 (= R25), S68 (≠ A63), G69 (= G64), G70 (≠ A65), D71 (= D66), Y104 (≠ D109), G108 (= G113)
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, 97% coverage: 3:256/261 of query aligns to 8:266/276 of O69762
- K29 (≠ V24) binding
- A68 (= A63) binding
- M70 (≠ A65) binding
- L72 (= L67) binding
- Y75 (≠ W69) binding
- G120 (= G113) binding
- S123 (≠ G116) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S135) binding
- E143 (= E136) mutation to A: Abolishes catalytic activity.
- W146 (≠ L139) binding
- G151 (≠ A144) binding
- Y239 (≠ I228) 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
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
29% identity, 93% coverage: 14:257/261 of query aligns to 30:257/266 of 3h02A
- active site: G82 (≠ A65), H86 (≠ W69), L90 (≠ M73), G114 (= G113), V117 (≠ G116), G137 (≠ E136), S142 (≠ L141), D144 (≠ P143), G145 (≠ A144), A231 (≠ I228), Y239 (≠ A236)
- binding bicarbonate ion: G113 (≠ A112), Q135 (≠ L134), G137 (≠ E136), W165 (≠ F163)
Query Sequence
>H281DRAFT_01344 FitnessBrowser__Burk376:H281DRAFT_01344
MHYETLNVEFAGHVATVTLNRPDVRNAFNETMIAELTSAFTALDTRDDVRAVVLAANGKA
FCAGADLNWMKKMAAYSDEENRADAMLLANMLSSIYRCSKPVIARVNGDAYAGGMGLISA
CDIVVAVESARFCLSEARLGLIPATIAPYVVRALGEQASRRYFITAEQFDCATALRLGFV
GEAVSAGQLDATVQQIAQTLCANGPQAVRNCKRLVQDMAGRKLNDALIEDTAARIARTRA
GAEGREGVASFLEKRTPAWRD
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