SitesBLAST
Comparing RR42_RS26900 FitnessBrowser__Cup4G11:RR42_RS26900 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)
32% identity, 99% coverage: 1:260/262 of query aligns to 1:257/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (≠ A85), R86 (≠ A89), 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 (= R168), F248 (= F251), K251 (= K254)
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)
33% identity, 95% coverage: 13:262/262 of query aligns to 20:268/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 99% coverage: 1:259/262 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (= M73), T80 (= T87), F84 (≠ L92), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (= L228), F234 (≠ I238)
- binding acetoacetyl-coenzyme a: Q23 (≠ D23), A24 (≠ V24), L25 (≠ R25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), K68 (= K71), M70 (= M73), F84 (≠ L92), 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
35% identity, 99% coverage: 1:259/262 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M73), T80 (= T87), F84 (≠ L92), G108 (= G113), E111 (≠ G116), P130 (≠ S135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ A144), L224 (= L228), F234 (≠ I238)
- binding coenzyme a: L25 (≠ R25), A63 (= A63), I67 (≠ L67), K68 (= K71), Y104 (≠ D109), P130 (≠ S135), E131 (= E136), L134 (= L139)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 98% coverage: 3:259/262 of query aligns to 2:253/256 of 3h81A
- active site: A64 (= A65), M69 (= M73), T79 (= T87), F83 (≠ L92), G107 (= G113), E110 (≠ G116), P129 (≠ S135), E130 (= E136), V135 (≠ L141), P137 (= P143), G138 (≠ A144), L223 (= L228), F233 (≠ I238)
- binding calcium ion: F233 (≠ I238), Q238 (≠ G244)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
34% identity, 90% coverage: 3:238/262 of query aligns to 5:245/246 of 6p5uE
- active site: M67 (≠ A65), Y72 (= Y76), D77 (≠ N81), R89 (≠ H93), A93 (= A97), G117 (= G113), T120 (≠ G116), E140 (= E136), I145 (≠ L141), P147 (= P143), A148 (= A144), A236 (= A229)
- 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:
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
31% identity, 98% coverage: 2:259/262 of query aligns to 11:266/273 of Q5HH38
- R34 (= R25) binding in other chain
- SGGDQ 73:77 (≠ AGADL 63:67) binding in other chain
- S149 (≠ L141) binding in other chain
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 3:259/262 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (= T87), F79 (≠ L92), G103 (= G113), E106 (≠ G116), P125 (≠ S135), E126 (= E136), V131 (≠ L141), P133 (= P143), G134 (≠ A144), L219 (= L228), F229 (≠ I238)
- binding Butyryl Coenzyme A: F225 (≠ R234), F241 (= F251)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 95% coverage: 13:260/262 of query aligns to 17:264/266 of O53561
- K135 (≠ N131) 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.
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
31% identity, 98% coverage: 2:259/262 of query aligns to 6:253/260 of 2uzfA
- active site: G70 (≠ A65), R80 (= R82), L84 (= L86), G108 (= G113), V111 (≠ G116), T130 (≠ S135), G131 (≠ E136), S136 (≠ L141), D138 (≠ P143), A139 (= A144), A225 (≠ T231), Y233 (≠ R239)
- binding acetoacetyl-coenzyme a: V28 (= V24), R29 (= R25), S68 (≠ A63), G69 (= G64), G70 (≠ A65), D71 (= D66), Y104 (≠ D109), G108 (= G113)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
31% identity, 94% coverage: 14:259/262 of query aligns to 34:278/285 of Q7CQ56
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 93% coverage: 18:260/262 of query aligns to 19:259/261 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 (= A229), L238 (≠ R239)
- 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 (= R168)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 94% coverage: 14:259/262 of query aligns to 30:274/281 of 3t88A
- active site: G82 (≠ A65), R87 (≠ M70), Y93 (= Y76), H101 (≠ A85), L105 (≠ A89), G129 (= G113), V132 (≠ G116), G152 (≠ E136), S157 (≠ L141), D159 (≠ P143), G160 (≠ A144), A246 (≠ T231), Y254 (≠ R239)
- 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 (≠ L88), L105 (≠ A89), Y125 (≠ D109), G129 (= G113), T151 (≠ S135), V155 (≠ L139), F158 (≠ L142), D159 (≠ P143), T250 (≠ I235), Y254 (≠ R239), F266 (= F251), K269 (= K254)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 94% coverage: 14:259/262 of query aligns to 34:278/285 of 4i42A
- active site: G86 (≠ A65), R91 (≠ M70), Y97 (= Y76), H105 (≠ A85), L109 (≠ A89), G133 (= G113), V136 (≠ G116), G156 (≠ E136), S161 (≠ L141), D163 (≠ P143), G164 (≠ A144), A250 (≠ T231), Y258 (≠ R239)
- 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 (≠ L88), Y129 (≠ D109), G133 (= G113), T155 (≠ S135), S161 (≠ L141), T254 (≠ I235), 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)
30% identity, 94% coverage: 14:259/262 of query aligns to 34:278/285 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 (≠ DTYAG 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 (≠ R239) binding
- R267 (≠ V248) 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.
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
36% identity, 76% coverage: 12:209/262 of query aligns to 9:189/224 of 3p85A
- active site: L62 (≠ A65), L67 (≠ M70), P68 (≠ K71), G92 (= G113), E95 (≠ G116), T114 (≠ S135), H115 (≠ E136), L120 (= L141), P122 (= P143), T123 (≠ A144)
- binding calcium ion: D43 (≠ E46), D45 (≠ T48)
Sites not aligning to the query:
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 98% coverage: 2:259/262 of query aligns to 8:268/275 of 4i52A
- active site: G77 (≠ A65), R82 (≠ K71), Y87 (= Y76), R95 (= R82), L99 (= L86), G123 (= G113), V126 (≠ G116), G146 (≠ E136), S151 (≠ L141), D153 (≠ P143), G154 (≠ A144), A240 (≠ S219), Y248 (≠ D230)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ D23), K30 (≠ V24), R31 (= R25), A33 (= A27), S75 (≠ A63), G76 (= G64), G77 (≠ A65), D78 (= D66), Q79 (≠ L67), L96 (≠ S83), V98 (≠ A85), Y119 (≠ D109), I121 (≠ Y111), G123 (= G113), T145 (≠ S135), V149 (≠ L139), S151 (≠ L141), F152 (≠ L142)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
30% identity, 98% coverage: 2:259/262 of query aligns to 8:268/275 of 4i4zA
- active site: G77 (≠ A65), R82 (≠ K71), Y87 (= Y76), R95 (= R82), L99 (= L86), G123 (= G113), V126 (≠ G116), G146 (≠ E136), S151 (≠ L141), D153 (≠ P143), G154 (≠ A144), A240 (≠ S219), Y248 (≠ D230)
- binding Salicylyl CoA: H29 (≠ D23), K30 (≠ V24), R31 (= R25), S75 (≠ A63), G76 (= G64), G77 (≠ A65), D78 (= D66), Q79 (≠ L67), Y87 (= Y76), V98 (≠ A85), G123 (= G113), T145 (≠ S135), V149 (≠ L139), S151 (≠ L141), F260 (= F251), K263 (= K254)
- binding bicarbonate ion: G122 (≠ A112), Q144 (≠ L134), T145 (≠ S135), G146 (≠ E136), W174 (≠ F163)
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 98% coverage: 2:259/262 of query aligns to 73:330/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
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)
30% identity, 97% coverage: 3:256/262 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 (≠ L228) 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
Query Sequence
>RR42_RS26900 FitnessBrowser__Cup4G11:RR42_RS26900
MEFTTLTVTAAQHVATVTLNRPDVRNAFNETVIAELTGAFRALGSEPTVRAIVLAGNGPA
FCAGADLNWMKKMAGYSHDENRSDALTLAQMLHTIWACPKPVIARIHGDTYAGGVGLVAA
CDIAVAAQTVNFCLSEARLGLLPATISPYVIRAMGEQAARRYFITAERFGAAEALRLGFV
HEVVPGDMLDAKVSEIAAALVANSPNAVRESKRLVQEVSGRAIDDALLADTAERIAAIRA
SDEGREGVRSFLEKRSPSWRPA
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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