SitesBLAST
Comparing CCNA_02251 FitnessBrowser__Caulo:CCNA_02251 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 91% coverage: 24:277/279 of query aligns to 6:256/259 of 5zaiC
- active site: A65 (= A82), F70 (≠ M87), S82 (≠ R99), R86 (≠ L103), G110 (= G130), E113 (≠ G133), P132 (≠ S152), E133 (= E153), I138 (≠ L158), P140 (= P160), G141 (≠ A161), A226 (= A250), F236 (vs. gap)
- binding coenzyme a: K24 (= K41), L25 (≠ K42), A63 (= A80), G64 (= G81), A65 (= A82), D66 (= D83), I67 (≠ L84), P132 (≠ S152), R166 (≠ V185), F248 (= F269), K251 (≠ R272)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
29% identity, 89% coverage: 30:277/279 of query aligns to 13:258/261 of 5jbxB
- active site: A67 (= A82), R72 (≠ M87), L84 (≠ A102), R88 (≠ A106), G112 (= G130), E115 (≠ G133), T134 (≠ S152), E135 (= E153), I140 (≠ L158), P142 (= P160), G143 (vs. gap), A228 (≠ I246), L238 (≠ R257)
- binding coenzyme a: S24 (≠ D40), R25 (≠ K41), R26 (≠ K42), A28 (= A44), A65 (= A80), D68 (= D83), L69 (= L84), K70 (≠ S85), L110 (≠ F128), G111 (= G129), T134 (≠ S152), E135 (= E153), L138 (= L156), R168 (≠ V185)
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, 96% coverage: 10:277/279 of query aligns to 13:278/285 of Q7CQ56
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)
27% identity, 87% coverage: 36:277/279 of query aligns to 26:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
27% identity, 92% coverage: 22:277/279 of query aligns to 21:274/281 of 3t88A
- active site: G82 (≠ A82), R87 (≠ M87), Y93 (≠ W93), H101 (≠ A102), L105 (≠ A106), G129 (= G130), V132 (≠ G133), G152 (≠ E153), S157 (vs. gap), D159 (≠ T159), G160 (≠ P160), A246 (≠ S249), Y254 (≠ R257)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D40), V40 (≠ K41), R41 (≠ K42), A43 (= A44), S80 (≠ A80), G81 (= G81), G82 (≠ A82), D83 (= D83), Q84 (≠ L84), K85 (≠ S85), Y93 (≠ W93), V104 (≠ L105), L105 (≠ A106), Y125 (≠ P126), G129 (= G130), T151 (≠ S152), V155 (≠ L156), F158 (≠ L158), D159 (≠ T159), T250 (≠ I253), Y254 (≠ R257), F266 (= F269), K269 (≠ R272)
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: 22:277/279 of query aligns to 25:278/285 of 4i42A
- active site: G86 (≠ A82), R91 (≠ M87), Y97 (≠ W93), H105 (≠ A102), L109 (≠ A106), G133 (= G130), V136 (≠ G133), G156 (≠ E153), S161 (vs. gap), D163 (≠ T159), G164 (≠ P160), A250 (≠ S249), Y258 (≠ R257)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K41), R45 (≠ K42), S84 (≠ A80), G85 (= G81), G86 (≠ A82), D87 (= D83), Q88 (≠ L84), K89 (≠ S85), Y97 (≠ W93), V108 (≠ L105), Y129 (≠ P126), G133 (= G130), T155 (≠ S152), S161 (vs. gap), T254 (≠ I253), F270 (= F269), K273 (≠ R272)
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: 22:277/279 of query aligns to 25:278/285 of P0ABU0
- R45 (≠ K42) binding in other chain
- SGGDQK 84:89 (≠ AGADLS 80:85) binding in other chain
- K89 (≠ S85) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M87) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ W93) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ PAFGG 126:130) binding in other chain
- Q154 (≠ F151) 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 (≠ FSE 151:153) binding
- T155 (≠ S152) binding in other chain
- G156 (≠ E153) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (vs. gap) binding in other chain
- W184 (≠ F180) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R257) binding
- R267 (≠ V266) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F269) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (≠ R272) binding ; mutation to A: Impairs protein folding.
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
29% identity, 90% coverage: 30:279/279 of query aligns to 19:270/275 of 4i52A
- active site: G77 (≠ A82), R82 (≠ M87), Y87 (≠ E92), R95 (= R99), L99 (= L103), G123 (= G130), V126 (≠ G133), G146 (≠ E153), S151 (≠ L158), D153 (≠ P160), G154 (≠ A161), A240 (≠ S249), Y248 (≠ R257)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ D40), K30 (= K41), R31 (≠ K42), A33 (= A44), S75 (≠ A80), G76 (= G81), G77 (≠ A82), D78 (= D83), Q79 (≠ L84), L96 (≠ Q100), V98 (≠ A102), Y119 (≠ P126), I121 (≠ F128), G123 (= G130), T145 (≠ S152), V149 (≠ L156), S151 (≠ L158), F152 (≠ T159)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
29% identity, 90% coverage: 30:279/279 of query aligns to 19:270/275 of 4i4zA
- active site: G77 (≠ A82), R82 (≠ M87), Y87 (≠ E92), R95 (= R99), L99 (= L103), G123 (= G130), V126 (≠ G133), G146 (≠ E153), S151 (≠ L158), D153 (≠ P160), G154 (≠ A161), A240 (≠ S249), Y248 (≠ R257)
- binding Salicylyl CoA: H29 (≠ D40), K30 (= K41), R31 (≠ K42), S75 (≠ A80), G76 (= G81), G77 (≠ A82), D78 (= D83), Q79 (≠ L84), Y87 (≠ E92), V98 (≠ A102), G123 (= G130), T145 (≠ S152), V149 (≠ L156), S151 (≠ L158), F260 (= F269), K263 (≠ R272)
- binding bicarbonate ion: G122 (= G129), Q144 (≠ F151), T145 (≠ S152), G146 (≠ E153), W174 (≠ F180)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
33% identity, 66% coverage: 29:212/279 of query aligns to 14:200/246 of 6p5uE
- active site: M67 (≠ A82), Y72 (≠ W93), D77 (≠ N98), R89 (≠ K110), A93 (vs. gap), G117 (= G130), T120 (≠ G133), E140 (= E153), I145 (≠ L158), P147 (= P160), A148 (= A161)
- binding coenzyme a: D25 (= D40), K26 (= K41), R27 (≠ K42), A29 (= A44), A65 (= A80), M67 (≠ A82), D68 (= D83), L69 (= L84), W113 (≠ P126), F115 (= F128), S139 (= S152), W143 (≠ L156)
Sites not aligning to the query:
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
28% identity, 96% coverage: 10:277/279 of query aligns to 9:259/266 of 3h02A
- active site: G82 (≠ A82), H86 (≠ A102), L90 (≠ A106), G114 (= G130), V117 (≠ G133), G137 (≠ E153), S142 (vs. gap), D144 (≠ T159), G145 (≠ P160), A231 (≠ S249), Y239 (≠ R257)
- binding bicarbonate ion: G113 (= G129), Q135 (≠ F151), G137 (≠ E153), W165 (≠ F180)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
30% identity, 79% coverage: 11:230/279 of query aligns to 48:275/327 of Q62651
- D176 (≠ G133) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E153) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (vs. gap) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
31% identity, 69% coverage: 22:214/279 of query aligns to 8:201/719 of 6tnmA
Sites not aligning to the query:
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
31% identity, 69% coverage: 22:214/279 of query aligns to 8:201/729 of P21177
- G116 (= G130) mutation to F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
Sites not aligning to the query:
- 322 G→A: 10-fold increase in KM for NADH.
- 450 active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
27% identity, 92% coverage: 22:277/279 of query aligns to 22:260/267 of 4elwA
- active site: G83 (≠ A82), L91 (≠ A106), G115 (= G130), V118 (≠ G133), G138 (≠ E153), S143 (vs. gap), D145 (≠ T159), G146 (≠ P160), A232 (≠ S249), Y240 (≠ R257)
- binding nitrate ion: G114 (= G129), T137 (≠ S152), G138 (≠ E153), F144 (≠ L158), W166 (≠ F180)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
29% identity, 90% coverage: 30:279/279 of query aligns to 19:256/261 of 4emlA
- active site: G77 (≠ A82), R81 (= R99), L85 (= L103), G109 (= G130), V112 (≠ G133), G132 (≠ E153), S137 (≠ L158), D139 (≠ P160), G140 (≠ A161), A226 (≠ S249), Y234 (≠ R257)
- binding bicarbonate ion: G108 (= G129), Q130 (≠ F151), G132 (≠ E153), W160 (≠ F180)
- binding chloride ion: D184 (≠ A205), R185 (≠ S206), E187 (= E208), E188 (≠ G209)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 88% coverage: 34:278/279 of query aligns to 17:255/255 of 3q0jC
- active site: A65 (= A82), M70 (= M87), T80 (vs. gap), F84 (≠ A106), G108 (= G130), E111 (≠ G133), P130 (≠ S152), E131 (= E153), V136 (≠ L158), P138 (= P160), G139 (≠ A161), L224 (≠ I246), F234 (≠ V258)
- binding acetoacetyl-coenzyme a: Q23 (≠ D40), A24 (≠ K41), L25 (≠ K42), A27 (= A44), A63 (= A80), G64 (= G81), A65 (= A82), D66 (= D83), I67 (≠ L84), K68 (≠ S85), M70 (= M87), F84 (≠ A106), G107 (= G129), G108 (= G130), E111 (≠ G133), P130 (≠ S152), E131 (= E153), P138 (= P160), G139 (≠ A161), M140 (≠ T162)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 88% coverage: 34:278/279 of query aligns to 17:255/255 of 3q0gC
- active site: A65 (= A82), M70 (= M87), T80 (vs. gap), F84 (≠ A106), G108 (= G130), E111 (≠ G133), P130 (≠ S152), E131 (= E153), V136 (≠ L158), P138 (= P160), G139 (≠ A161), L224 (≠ I246), F234 (≠ V258)
- binding coenzyme a: L25 (≠ K42), A63 (= A80), I67 (≠ L84), K68 (≠ S85), Y104 (≠ P126), P130 (≠ S152), E131 (= E153), L134 (= L156)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 88% coverage: 34:278/279 of query aligns to 16:254/256 of 3h81A
- active site: A64 (= A82), M69 (= M87), T79 (vs. gap), F83 (≠ A106), G107 (= G130), E110 (≠ G133), P129 (≠ S152), E130 (= E153), V135 (≠ L158), P137 (= P160), G138 (≠ A161), L223 (≠ I246), F233 (≠ V258)
- binding calcium ion: F233 (≠ V258), Q238 (= Q263)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
27% identity, 92% coverage: 22:277/279 of query aligns to 22:261/268 of 4elxA
- active site: G83 (≠ A82), H88 (≠ A102), L92 (≠ A106), G116 (= G130), V119 (≠ G133), G139 (≠ E153), S144 (vs. gap), D146 (≠ T159), G147 (≠ P160), A233 (≠ S249), Y241 (≠ R257)
- binding chloride ion: G115 (= G129), G139 (≠ E153), W167 (≠ F180)
Query Sequence
>CCNA_02251 FitnessBrowser__Caulo:CCNA_02251
MTNPIADPIVEVPDTDAMSPLVHMDSTPEGAVTVWINRPDKKNAFDAATIAALRQTFETL
HGAEGVRIVFLRGVGGAFSAGADLSWMASAVEWDEDDNRQDALELAHMLKALHDIPALTV
ALVEGPAFGGGAGLVAACDHALALVDAKFAFSEVKLGLTPATISPYVIQALGPRTAKLLF
ATGRVFDADDAWGFGLVDEVFEDVASLEGARDALIAEMAPCAPGAIGDAKALVNDFVGQK
LDKGLIDESARRIARRRVSPEGQEGVRAFLARRKPSWVE
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