SitesBLAST
Comparing WP_011383118.1 NCBI__GCF_000009985.1:WP_011383118.1 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, 93% coverage: 15:257/260 of query aligns to 17:256/259 of 5zaiC
- active site: A65 (= A63), F70 (≠ M68), S82 (≠ A83), R86 (≠ S87), G110 (= G111), E113 (≠ G114), P132 (≠ S133), E133 (= E134), I138 (= I139), P140 (= P141), G141 (≠ A142), A226 (≠ R226), F236 (≠ R236)
- binding coenzyme a: K24 (≠ R22), L25 (≠ H23), A63 (= A61), G64 (= G62), A65 (= A63), D66 (= D64), I67 (≠ L65), P132 (≠ S133), R166 (≠ L166), F248 (= F249), K251 (= K252)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 98% coverage: 4:257/260 of query aligns to 5:254/257 of 6slbAAA
- active site: Q64 (≠ A63), F69 (≠ W67), L80 (≠ A83), N84 (≠ S87), A108 (≠ G111), S111 (≠ G114), A130 (≠ S133), F131 (≠ E134), L136 (≠ I139), P138 (= P141), D139 (vs. gap), A224 (≠ S224), G234 (≠ A234)
- binding (~{E})-6-[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]-6-oxidanylidene-hex-3-enoic acid: R58 (≠ K57), A62 (= A61), Q64 (≠ A63), D65 (= D64), L66 (= L65), Y76 (= Y74), A108 (≠ G111), F131 (≠ E134), D139 (vs. gap)
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, 95% coverage: 10:255/260 of query aligns to 32:276/285 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)
33% identity, 93% coverage: 15:257/260 of query aligns to 24:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 98% coverage: 4:257/260 of query aligns to 2:242/245 of 6slaAAA
- active site: Q61 (≠ A63), L68 (≠ A83), N72 (≠ S87), A96 (≠ G111), S99 (≠ G114), A118 (≠ S133), F119 (≠ E134), L124 (≠ I139), P126 (= P141), N127 (vs. gap), A212 (≠ S224), G222 (≠ A234)
- binding ~{S}-[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]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ H23), A59 (= A61), Q61 (≠ A63), D62 (= D64), L63 (= L65), L68 (≠ A83), Y71 (≠ L86), A94 (≠ Y109), G95 (= G110), A96 (≠ G111), F119 (≠ E134), I122 (≠ L137), L124 (≠ I139), N127 (vs. gap), F234 (= F249), K237 (= K252)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 98% coverage: 4:257/260 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (= A63), M70 (= M71), T80 (vs. gap), F84 (≠ Q84), G108 (= G111), E111 (≠ G114), P130 (≠ S133), E131 (= E134), V136 (≠ I139), P138 (= P141), G139 (≠ A142), L224 (≠ I233), F234 (vs. gap)
- binding acetoacetyl-coenzyme a: Q23 (≠ E21), A24 (≠ R22), L25 (≠ H23), A27 (= A25), A63 (= A61), G64 (= G62), A65 (= A63), D66 (= D64), I67 (≠ L65), K68 (= K69), M70 (= M71), F84 (≠ Q84), G107 (= G110), G108 (= G111), E111 (≠ G114), P130 (≠ S133), E131 (= E134), P138 (= P141), G139 (≠ A142), M140 (≠ V143)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 98% coverage: 4:257/260 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (= A63), M70 (= M71), T80 (vs. gap), F84 (≠ Q84), G108 (= G111), E111 (≠ G114), P130 (≠ S133), E131 (= E134), V136 (≠ I139), P138 (= P141), G139 (≠ A142), L224 (≠ I233), F234 (vs. gap)
- binding coenzyme a: L25 (≠ H23), A63 (= A61), I67 (≠ L65), K68 (= K69), Y104 (≠ A107), P130 (≠ S133), E131 (= E134), L134 (= L137)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
32% identity, 96% coverage: 9:257/260 of query aligns to 20:266/273 of Q5HH38
- R34 (≠ H23) binding in other chain
- SGGD-Q 73:77 (≠ AGADLE 61:66) binding in other chain
- S149 (≠ I139) binding in other chain
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 98% coverage: 4:257/260 of query aligns to 5:253/256 of 3h81A
- active site: A64 (= A63), M69 (= M71), T79 (vs. gap), F83 (≠ Q84), G107 (= G111), E110 (≠ G114), P129 (≠ S133), E130 (= E134), V135 (≠ I139), P137 (= P141), G138 (≠ A142), L223 (≠ I233), F233 (vs. gap)
- binding calcium ion: F233 (vs. gap), Q238 (≠ G242)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
31% identity, 95% coverage: 10:255/260 of query aligns to 32:276/285 of 4i42A
- active site: G86 (≠ A63), R91 (≠ M68), Y97 (= Y74), H105 (≠ D82), L109 (= L86), G133 (= G111), V136 (≠ G114), G156 (≠ E134), S161 (≠ I139), D163 (≠ P141), G164 (≠ A142), A250 (≠ T229), Y258 (≠ R237)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R22), R45 (≠ H23), S84 (≠ A61), G85 (= G62), G86 (≠ A63), D87 (= D64), Q88 (≠ L65), K89 (≠ E66), Y97 (= Y74), V108 (≠ A85), Y129 (≠ A107), G133 (= G111), T155 (≠ S133), S161 (≠ I139), T254 (≠ I233), F270 (= F249), K273 (= K252)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 95% coverage: 10:255/260 of query aligns to 32:276/285 of P0ABU0
- R45 (≠ H23) binding in other chain
- SGGDQK 84:89 (≠ AGADLE 61:66) binding in other chain
- K89 (≠ E66) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M68) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y74) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAYGG 107:111) binding in other chain
- Q154 (≠ L132) 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 132:134) binding
- T155 (≠ S133) binding in other chain
- G156 (≠ E134) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ I139) binding in other chain
- W184 (≠ A161) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R237) binding
- R267 (≠ I246) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F249) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K252) binding ; mutation to A: Impairs protein folding.
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)
31% identity, 95% coverage: 10:257/260 of query aligns to 85:330/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
31% identity, 95% coverage: 10:255/260 of query aligns to 28:272/281 of 3t88A
- active site: G82 (≠ A63), R87 (≠ M68), Y93 (= Y74), H101 (≠ D82), L105 (= L86), G129 (= G111), V132 (≠ G114), G152 (≠ E134), S157 (≠ I139), D159 (≠ P141), G160 (≠ A142), A246 (≠ T229), Y254 (≠ R237)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E21), V40 (≠ R22), R41 (≠ H23), A43 (= A25), S80 (≠ A61), G81 (= G62), G82 (≠ A63), D83 (= D64), Q84 (≠ L65), K85 (≠ E66), Y93 (= Y74), V104 (≠ A85), L105 (= L86), Y125 (≠ A107), G129 (= G111), T151 (≠ S133), V155 (≠ L137), F158 (≠ I140), D159 (≠ P141), T250 (≠ I233), Y254 (≠ R237), F266 (= F249), K269 (= K252)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 96% coverage: 9:257/260 of query aligns to 14:257/260 of 2hw5C
- active site: A68 (= A63), M73 (= M68), S83 (= S87), L87 (vs. gap), G111 (= G111), E114 (≠ G114), P133 (≠ S133), E134 (= E134), T139 (≠ I139), P141 (= P141), G142 (vs. gap), K227 (≠ R226), F237 (≠ R237)
- binding crotonyl coenzyme a: K26 (≠ E21), A27 (≠ R22), L28 (≠ H23), A30 (= A25), K62 (= K57), I70 (≠ L65), F109 (≠ Y109)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 4:257/260 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (= A63), M69 (= M68), T75 (≠ A85), F79 (≠ L90), G103 (= G111), E106 (≠ G114), P125 (≠ S133), E126 (= E134), V131 (≠ I139), P133 (= P141), G134 (≠ A142), L219 (≠ I233), F229 (vs. gap)
- binding Butyryl Coenzyme A: F225 (vs. gap), F241 (= F249)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
31% identity, 95% coverage: 10:255/260 of query aligns to 28:257/266 of 3h02A
- active site: G82 (≠ A63), H86 (≠ E77), L90 (≠ A81), G114 (= G111), V117 (≠ G114), G137 (≠ E134), S142 (≠ I139), D144 (≠ P141), G145 (≠ A142), A231 (≠ T229), Y239 (≠ R237)
- binding bicarbonate ion: G113 (= G110), Q135 (≠ L132), G137 (≠ E134), W165 (≠ A161)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 93% coverage: 16:257/260 of query aligns to 19:258/261 of 5jbxB
- active site: A67 (= A63), R72 (≠ M71), L84 (≠ A83), R88 (≠ S87), G112 (= G111), E115 (≠ G114), T134 (≠ S133), E135 (= E134), I140 (= I139), P142 (= P141), G143 (vs. gap), A228 (= A227), L238 (≠ R237)
- binding coenzyme a: S24 (≠ E21), R25 (= R22), R26 (≠ H23), A28 (= A25), A65 (= A61), D68 (= D64), L69 (= L65), K70 (= K69), L110 (≠ Y109), G111 (= G110), T134 (≠ S133), E135 (= E134), L138 (= L137), R168 (≠ L166)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
31% identity, 95% coverage: 10:255/260 of query aligns to 29:259/268 of 4elxA
- active site: G83 (≠ A63), H88 (≠ E77), L92 (≠ A81), G116 (= G111), V119 (≠ G114), G139 (≠ E134), S144 (≠ I139), D146 (≠ P141), G147 (≠ A142), A233 (≠ T229), Y241 (≠ R237)
- binding chloride ion: G115 (= G110), G139 (≠ E134), W167 (≠ A161)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
32% identity, 96% coverage: 9:257/260 of query aligns to 13:251/254 of 2dubA
- active site: A67 (= A63), M72 (= M68), S82 (= S75), G105 (= G111), E108 (≠ G114), P127 (≠ S133), E128 (= E134), T133 (≠ I139), P135 (= P141), G136 (vs. gap), K221 (≠ I233), F231 (vs. gap)
- binding octanoyl-coenzyme a: K25 (≠ E21), A26 (≠ R22), L27 (≠ H23), A29 (= A25), A65 (= A61), A67 (= A63), D68 (= D64), I69 (≠ L65), K70 (≠ E66), G105 (= G111), E108 (≠ G114), P127 (≠ S133), E128 (= E134), G136 (vs. gap), A137 (= A142)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 96% coverage: 9:257/260 of query aligns to 14:255/258 of 1mj3A
- active site: A68 (= A63), M73 (= M68), S83 (≠ A85), L85 (≠ S87), G109 (= G111), E112 (≠ G114), P131 (≠ S133), E132 (= E134), T137 (≠ I139), P139 (= P141), G140 (vs. gap), K225 (≠ I233), F235 (vs. gap)
- binding hexanoyl-coenzyme a: K26 (≠ E21), A27 (≠ R22), L28 (≠ H23), A30 (= A25), A66 (= A61), G67 (= G62), A68 (= A63), D69 (= D64), I70 (≠ L65), G109 (= G111), P131 (≠ S133), E132 (= E134), L135 (= L137), G140 (vs. gap)
Query Sequence
>WP_011383118.1 NCBI__GCF_000009985.1:WP_011383118.1
MSALLVTTHDGVRTITLNRAERHNAFDDALIAELAAAFRDAATAPGIRAVVLDSTGKSFS
AGADLEWMKRMAGYSHEENLADAQALSDMLEAIDACPRPVIGVVQGAAYGGGVGLVACCD
LAVAAEGATFCLSEVKLGIIPAVISPYVVRAMGGRAARRYAVTAELFDAAEAKATGLVHE
VVPAEHLAEVRDKWLARVKGNGPQAMSAAKGLIRRAADQPLDESLRAWTAGQIAERRASD
EGKEGIRAFLEKRKPAWIEG
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