SitesBLAST
Comparing WP_086510402.1 NCBI__GCF_002151265.1:WP_086510402.1 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)
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, 90% coverage: 16:263/277 of query aligns to 33:276/285 of Q7CQ56
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
34% identity, 74% coverage: 14:219/277 of query aligns to 15:215/244 of 6l3pA
- active site: M69 (≠ A71), Y74 (= Y82), R86 (= R92), Q90 (= Q96), G114 (= G119), S117 (≠ G122), S136 (= S141), E137 (= E142), I142 (≠ L147), P144 (= P149), G145 (≠ A150)
- binding coenzyme a: K28 (≠ V27), R29 (≠ H28), A31 (= A30), A67 (= A69), M69 (≠ A71), D70 (= D72), L71 (= L73), G113 (= G118)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
27% identity, 89% coverage: 20:265/277 of query aligns to 17:256/259 of 5zaiC
- active site: A65 (= A71), F70 (≠ M76), S82 (= S91), R86 (≠ S95), G110 (= G119), E113 (≠ G122), P132 (≠ S141), E133 (= E142), I138 (≠ L147), P140 (= P149), G141 (≠ A150), A226 (≠ T237), F236 (vs. gap)
- binding coenzyme a: K24 (≠ V27), L25 (≠ H28), A63 (= A69), G64 (= G70), A65 (= A71), D66 (= D72), I67 (≠ L73), P132 (≠ S141), R166 (≠ V174), F248 (= F257), K251 (= K260)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
33% identity, 78% coverage: 9:224/277 of query aligns to 9:223/246 of 6p5uE
- active site: M67 (≠ A71), Y72 (= Y82), D77 (≠ N87), R89 (vs. gap), A93 (vs. gap), G117 (= G119), T120 (≠ G122), E140 (= E142), I145 (≠ L147), P147 (= P149), A148 (= A150)
- binding coenzyme a: D25 (= D26), K26 (≠ V27), R27 (≠ H28), A29 (= A30), A65 (= A69), M67 (≠ A71), D68 (= D72), L69 (= L73), W113 (≠ A115), F115 (= F117), S139 (= S141), W143 (≠ I145)
Sites not aligning to the query:
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
30% identity, 90% coverage: 16:263/277 of query aligns to 29:257/266 of 3h02A
- active site: G82 (≠ A71), H86 (≠ R78), L90 (≠ Y82), G114 (= G119), V117 (≠ G122), G137 (≠ E142), S142 (vs. gap), D144 (≠ S148), G145 (≠ P149), A231 (≠ T237), Y239 (≠ R245)
- binding bicarbonate ion: G113 (= G118), Q135 (≠ L140), G137 (≠ E142), W165 (≠ A169)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 90% coverage: 16:265/277 of query aligns to 12:254/257 of 6slbAAA
- active site: Q64 (≠ A71), F69 (≠ Y82), L80 (= L88), N84 (≠ S95), A108 (≠ G119), S111 (≠ G122), A130 (≠ S141), F131 (≠ E142), L136 (= L147), P138 (= P149), D139 (vs. gap), A224 (≠ R234), G234 (≠ R245)
- 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 (≠ K65), A62 (= A69), Q64 (≠ A71), D65 (= D72), L66 (= L73), Y76 (≠ F84), A108 (≠ G119), F131 (≠ E142), D139 (vs. gap)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
29% identity, 90% coverage: 16:263/277 of query aligns to 33:276/285 of 4i42A
- active site: G86 (≠ A71), R91 (≠ E81), Y97 (≠ N87), H105 (vs. gap), L109 (≠ S95), G133 (= G119), V136 (≠ G122), G156 (≠ E142), S161 (vs. gap), D163 (≠ S148), G164 (≠ P149), A250 (≠ T237), Y258 (≠ R245)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V27), R45 (≠ H28), S84 (≠ A69), G85 (= G70), G86 (≠ A71), D87 (= D72), Q88 (≠ R78), K89 (≠ M79), Y97 (≠ N87), V108 (≠ L94), Y129 (≠ A115), G133 (= G119), T155 (≠ S141), S161 (vs. gap), T254 (≠ I241), F270 (= F257), K273 (= K260)
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, 90% coverage: 16:263/277 of query aligns to 33:276/285 of P0ABU0
- R45 (≠ H28) binding in other chain
- SGGD-----QK 84:89 (≠ AGADLGWMKRM 69:79) binding in other chain
- K89 (≠ M79) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ E81) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ N87) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAFGG 115:119) binding in other chain
- Q154 (≠ L140) 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 140:142) binding hydrogencarbonate
- T155 (≠ S141) binding in other chain
- G156 (≠ E142) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (vs. gap) binding in other chain
- W184 (≠ A169) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R245) binding substrate
- R267 (≠ L254) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F257) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K260) binding substrate; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
29% identity, 90% coverage: 16:263/277 of query aligns to 29:272/281 of 3t88A
- active site: G82 (≠ A71), R87 (≠ E81), Y93 (≠ N87), H101 (vs. gap), L105 (≠ S95), G129 (= G119), V132 (≠ G122), G152 (≠ E142), S157 (vs. gap), D159 (≠ S148), G160 (≠ P149), A246 (≠ T237), Y254 (≠ R245)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D26), V40 (= V27), R41 (≠ H28), A43 (= A30), S80 (≠ A69), G81 (= G70), G82 (≠ A71), D83 (= D72), Q84 (≠ R78), K85 (≠ M79), Y93 (≠ N87), V104 (≠ L94), L105 (≠ S95), Y125 (≠ A115), G129 (= G119), T151 (≠ S141), V155 (≠ I145), F158 (≠ L147), D159 (≠ S148), T250 (≠ I241), Y254 (≠ R245), F266 (= F257), K269 (= K260)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
29% identity, 90% coverage: 16:263/277 of query aligns to 30:258/267 of 4elwA
- active site: G83 (≠ A71), L91 (≠ Y82), G115 (= G119), V118 (≠ G122), G138 (≠ E142), S143 (vs. gap), D145 (≠ S148), G146 (≠ P149), A232 (≠ T237), Y240 (≠ R245)
- binding nitrate ion: G114 (= G118), T137 (≠ S141), G138 (≠ E142), F144 (≠ L147), W166 (≠ A169)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 90% coverage: 16:265/277 of query aligns to 9:242/245 of 6slaAAA
- active site: Q61 (≠ A71), L68 (≠ S91), N72 (≠ S95), A96 (≠ G119), S99 (≠ G122), A118 (≠ S141), F119 (≠ E142), L124 (= L147), P126 (= P149), N127 (vs. gap), A212 (≠ R234), G222 (≠ R245)
- 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 (≠ H28), A59 (= A69), Q61 (≠ A71), D62 (= D72), L63 (= L73), L68 (≠ S91), Y71 (≠ L94), A94 (≠ F117), G95 (= G118), A96 (≠ G119), F119 (≠ E142), I122 (= I145), L124 (= L147), N127 (vs. gap), F234 (= F257), K237 (= K260)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 91% coverage: 13:265/277 of query aligns to 10:253/256 of 3h81A
- active site: A64 (= A71), M69 (= M79), T79 (≠ S91), F83 (≠ S95), G107 (= G119), E110 (≠ G122), P129 (≠ S141), E130 (= E142), V135 (≠ L147), P137 (= P149), G138 (≠ A150), L223 (≠ R234), F233 (≠ R245)
- binding calcium ion: F233 (≠ R245), Q238 (≠ G250)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 91% coverage: 13:265/277 of query aligns to 11:254/255 of 3q0jC
- active site: A65 (= A71), M70 (= M79), T80 (≠ S91), F84 (≠ S95), G108 (= G119), E111 (≠ G122), P130 (≠ S141), E131 (= E142), V136 (≠ L147), P138 (= P149), G139 (≠ A150), L224 (≠ R234), F234 (≠ R245)
- binding acetoacetyl-coenzyme a: Q23 (≠ D26), A24 (≠ V27), L25 (≠ H28), A27 (= A30), A63 (= A69), G64 (= G70), A65 (= A71), D66 (= D72), I67 (≠ L73), K68 (= K77), M70 (= M79), F84 (≠ S95), G107 (= G118), G108 (= G119), E111 (≠ G122), P130 (≠ S141), E131 (= E142), P138 (= P149), G139 (≠ A150), M140 (≠ V151)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 91% coverage: 13:265/277 of query aligns to 11:254/255 of 3q0gC
- active site: A65 (= A71), M70 (= M79), T80 (≠ S91), F84 (≠ S95), G108 (= G119), E111 (≠ G122), P130 (≠ S141), E131 (= E142), V136 (≠ L147), P138 (= P149), G139 (≠ A150), L224 (≠ R234), F234 (≠ R245)
- binding coenzyme a: L25 (≠ H28), A63 (= A69), I67 (≠ L73), K68 (= K77), Y104 (≠ A115), P130 (≠ S141), E131 (= E142), L134 (≠ I145)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 95% coverage: 6:267/277 of query aligns to 2:259/260 of 2hw5C
- active site: A68 (= A71), M73 (= M79), S83 (≠ D90), L87 (= L94), G111 (= G119), E114 (≠ G122), P133 (≠ S141), E134 (= E142), T139 (≠ L147), P141 (= P149), G142 (vs. gap), K227 (≠ R239), F237 (vs. gap)
- binding crotonyl coenzyme a: K26 (≠ D26), A27 (≠ V27), L28 (≠ H28), A30 (= A30), K62 (= K65), I70 (≠ L73), F109 (= F117)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
28% identity, 90% coverage: 16:263/277 of query aligns to 17:251/260 of 2uzfA
- active site: G70 (≠ A71), R80 (≠ E81), L84 (≠ A89), G108 (= G119), V111 (≠ G122), T130 (≠ S141), G131 (≠ E142), S136 (vs. gap), D138 (≠ S148), A139 (≠ P149), A225 (≠ C238), Y233 (≠ V246)
- binding acetoacetyl-coenzyme a: V28 (= V27), R29 (≠ H28), S68 (≠ A69), G69 (= G70), G70 (≠ A71), D71 (= D72), Y104 (≠ A115), G108 (= G119)
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
27% identity, 90% coverage: 16:263/277 of query aligns to 30:259/268 of 4elxA
- active site: G83 (≠ A71), H88 (≠ M76), L92 (≠ V80), G116 (= G119), V119 (≠ G122), G139 (≠ E142), S144 (vs. gap), D146 (≠ S148), G147 (≠ P149), A233 (≠ T237), Y241 (≠ R245)
- binding chloride ion: G115 (= G118), G139 (≠ E142), W167 (≠ A169)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 91% coverage: 13:265/277 of query aligns to 10:249/250 of 3q0gD
- active site: A64 (= A71), M69 (= M79), T75 (≠ E85), F79 (vs. gap), G103 (= G119), E106 (≠ G122), P125 (≠ S141), E126 (= E142), V131 (≠ L147), P133 (= P149), G134 (≠ A150), L219 (≠ R234), F229 (≠ R245)
- binding Butyryl Coenzyme A: F225 (≠ I241), F241 (= F257)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
28% identity, 90% coverage: 16:263/277 of query aligns to 22:264/273 of Q5HH38
- R34 (≠ H28) binding in other chain
- SGGD---Q 73:77 (≠ AGADLGWM 69:76) binding in other chain
- S149 (vs. gap) binding in other chain
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)
32% identity, 89% coverage: 20:265/277 of query aligns to 24:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Query Sequence
>WP_086510402.1 NCBI__GCF_002151265.1:WP_086510402.1
MTDTDSFSQLSIDERGVARLTLNRPDVHNAFDDSLIAELNEHLDKLHDAARHGEVRVVVL
GSEGKSFSAGADLGWMKRMVEYDFEGNLADSRKLSQLMHGLDTLPCPTVCRVQGAAFGGA
VGLAACCDIVIASEKAKFCLSEVKIGLSPAVISPYVQRALGSRQMRRYALTAEVIDADKA
LELGLAHQIVGHDHIDEAVEAMIATLLAGSPQAQRATKSLLAEVARDSDSKATREHTCRV
ISELRVSAEGQEGLTSFFEKRRPAWADDNTNSSERRS
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