SitesBLAST
Comparing WP_012405853.1 NCBI__GCF_000020045.1:WP_012405853.1 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)
36% identity, 89% coverage: 31:268/268 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (≠ G78), F70 (= F83), S82 (≠ A99), R86 (= R103), G110 (≠ V119), E113 (= E122), P132 (= P141), E133 (= E142), I138 (≠ Q147), P140 (= P149), G141 (= G150), A226 (≠ E235), F236 (≠ R245)
- binding coenzyme a: K24 (≠ P37), L25 (≠ F38), A63 (≠ S76), G64 (= G77), A65 (≠ G78), D66 (= D79), I67 (= I80), P132 (= P141), R166 (= R175), F248 (= F257), K251 (= K260)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 86% coverage: 39:268/268 of query aligns to 27:261/261 of 5jbxB
- active site: A67 (≠ G78), R72 (≠ F83), L84 (vs. gap), R88 (≠ A95), G112 (≠ V119), E115 (= E122), T134 (≠ P141), E135 (= E142), I140 (≠ Q147), P142 (= P149), G143 (= G150), A228 (≠ E235), L238 (≠ R245)
- binding coenzyme a: A28 (≠ V40), A65 (≠ S76), D68 (= D79), L69 (≠ I80), K70 (= K81), L110 (≠ F117), G111 (= G118), T134 (≠ P141), E135 (= E142), L138 (= L145), R168 (= R175)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 88% coverage: 31:265/268 of query aligns to 16:249/250 of 3q0gD
- active site: A64 (≠ G78), M69 (≠ F83), T75 (≠ E89), F79 (≠ K93), G103 (≠ V119), E106 (= E122), P125 (= P141), E126 (= E142), V131 (≠ Q147), P133 (= P149), G134 (= G150), L219 (≠ E235), F229 (≠ R245)
- binding Butyryl Coenzyme A: F225 (≠ Y241), F241 (= F257)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 88% coverage: 31:265/268 of query aligns to 17:254/255 of 3q0jC
- active site: A65 (≠ G78), M70 (≠ F83), T80 (≠ K93), F84 (vs. gap), G108 (≠ V119), E111 (= E122), P130 (= P141), E131 (= E142), V136 (≠ Q147), P138 (= P149), G139 (= G150), L224 (≠ E235), F234 (≠ R245)
- binding acetoacetyl-coenzyme a: Q23 (vs. gap), A24 (≠ P37), L25 (≠ F38), A27 (≠ V40), A63 (≠ S76), G64 (= G77), A65 (≠ G78), D66 (= D79), I67 (= I80), K68 (= K81), M70 (≠ F83), F84 (vs. gap), G107 (= G118), G108 (≠ V119), E111 (= E122), P130 (= P141), E131 (= E142), P138 (= P149), G139 (= G150), M140 (≠ S151)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 88% coverage: 31:265/268 of query aligns to 17:254/255 of 3q0gC
- active site: A65 (≠ G78), M70 (≠ F83), T80 (≠ K93), F84 (vs. gap), G108 (≠ V119), E111 (= E122), P130 (= P141), E131 (= E142), V136 (≠ Q147), P138 (= P149), G139 (= G150), L224 (≠ E235), F234 (≠ R245)
- binding coenzyme a: L25 (≠ F38), A63 (≠ S76), I67 (= I80), K68 (= K81), Y104 (≠ F115), P130 (= P141), E131 (= E142), L134 (= L145)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 88% coverage: 31:265/268 of query aligns to 16:253/256 of 3h81A
- active site: A64 (≠ G78), M69 (≠ F83), T79 (≠ K93), F83 (vs. gap), G107 (≠ V119), E110 (= E122), P129 (= P141), E130 (= E142), V135 (≠ Q147), P137 (= P149), G138 (= G150), L223 (≠ E235), F233 (≠ R245)
- binding calcium ion: F233 (≠ R245), Q238 (≠ F250)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 88% coverage: 31:266/268 of query aligns to 20:258/260 of 2hw5C
- active site: A68 (≠ G78), M73 (≠ F83), S83 (≠ V91), L87 (≠ A95), G111 (≠ V119), E114 (= E122), P133 (= P141), E134 (= E142), T139 (≠ Q147), P141 (= P149), G142 (= G150), K227 (≠ E235), F237 (≠ R245)
- binding crotonyl coenzyme a: K26 (vs. gap), A27 (≠ P37), L28 (≠ F38), A30 (≠ V40), K62 (≠ E72), I70 (= I80), F109 (= F117)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
30% identity, 91% coverage: 26:268/268 of query aligns to 7:257/257 of 6slbAAA
- active site: Q64 (≠ G78), F69 (= F83), L80 (≠ V91), N84 (≠ A95), A108 (≠ V119), S111 (≠ E122), A130 (≠ P141), F131 (≠ E142), L136 (≠ Q147), P138 (= P149), D139 (≠ G150), A224 (≠ E235), 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 (≠ E72), A62 (≠ S76), Q64 (≠ G78), D65 (= D79), L66 (≠ I80), Y76 (vs. gap), A108 (≠ V119), F131 (≠ E142), D139 (≠ G150)
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)
29% identity, 88% coverage: 31:266/268 of query aligns to 24:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
29% identity, 91% coverage: 26:268/268 of query aligns to 4:245/245 of 6slaAAA
- active site: Q61 (≠ G78), L68 (≠ V91), N72 (≠ A95), A96 (≠ V119), S99 (≠ E122), A118 (≠ P141), F119 (≠ E142), L124 (≠ Q147), P126 (= P149), N127 (≠ G150), A212 (≠ E235), 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 (≠ F38), A59 (≠ S76), Q61 (≠ G78), D62 (= D79), L63 (≠ I80), L68 (≠ V91), Y71 (≠ L94), A94 (≠ F117), G95 (= G118), A96 (≠ V119), F119 (≠ E142), I122 (≠ L145), L124 (≠ Q147), N127 (≠ G150), F234 (= F257), K237 (= K260)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 88% coverage: 31:266/268 of query aligns to 18:256/258 of 1ey3A
- active site: A66 (≠ G78), M71 (≠ F83), S81 (≠ V91), L85 (≠ A95), G109 (≠ V119), E112 (= E122), P131 (= P141), E132 (= E142), T137 (≠ Q147), P139 (= P149), G140 (= G150), K225 (≠ E235), F235 (≠ R245)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P37), L26 (≠ F38), A28 (≠ V40), A64 (≠ S76), G65 (= G77), A66 (≠ G78), D67 (= D79), I68 (= I80), L85 (≠ A95), W88 (≠ I98), G109 (≠ V119), P131 (= P141), L135 (= L145), G140 (= G150)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
30% identity, 88% coverage: 31:266/268 of query aligns to 20:256/258 of 1mj3A
- active site: A68 (≠ G78), M73 (≠ F83), S83 (≠ K93), L85 (≠ A95), G109 (≠ V119), E112 (= E122), P131 (= P141), E132 (= E142), T137 (≠ Q147), P139 (= P149), G140 (= G150), K225 (≠ E235), F235 (≠ R245)
- binding hexanoyl-coenzyme a: K26 (vs. gap), A27 (≠ P37), L28 (≠ F38), A30 (≠ V40), A66 (≠ S76), G67 (= G77), A68 (≠ G78), D69 (= D79), I70 (= I80), G109 (≠ V119), P131 (= P141), E132 (= E142), L135 (= L145), G140 (= G150)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 88% coverage: 31:266/268 of query aligns to 20:258/260 of 1dubA
- active site: A68 (≠ G78), M73 (≠ F83), S83 (≠ V91), L87 (≠ A95), G111 (≠ V119), E114 (= E122), P133 (= P141), E134 (= E142), T139 (≠ Q147), P141 (= P149), G142 (= G150), K227 (≠ E235), F237 (≠ R245)
- binding acetoacetyl-coenzyme a: K26 (≠ P37), A27 (vs. gap), L28 (≠ F38), A30 (≠ V40), A66 (≠ S76), A68 (≠ G78), D69 (= D79), I70 (= I80), Y107 (≠ F115), G110 (= G118), G111 (≠ V119), E114 (= E122), P133 (= P141), E134 (= E142), L137 (= L145), G142 (= G150), F233 (≠ Y241), F249 (= F257)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 88% coverage: 31:266/268 of query aligns to 19:252/254 of 2dubA
- active site: A67 (≠ G78), M72 (≠ F83), S82 (≠ K93), G105 (≠ V119), E108 (= E122), P127 (= P141), E128 (= E142), T133 (≠ Q147), P135 (= P149), G136 (= G150), K221 (≠ E235), F231 (≠ R245)
- binding octanoyl-coenzyme a: K25 (≠ P37), A26 (vs. gap), L27 (≠ F38), A29 (≠ V40), A65 (≠ S76), A67 (≠ G78), D68 (= D79), I69 (= I80), K70 (= K81), G105 (≠ V119), E108 (= E122), P127 (= P141), E128 (= E142), G136 (= G150), A137 (≠ S151)
P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
31% identity, 88% coverage: 31:266/268 of query aligns to 50:288/290 of P14604
- E144 (= E122) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E142) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
33% identity, 86% coverage: 39:268/268 of query aligns to 101:339/339 of Q13825
- K105 (≠ M43) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 43:57, 27% identical) RNA-binding
- K109 (≠ D47) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ A51) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ S173) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
33% identity, 64% coverage: 29:199/268 of query aligns to 12:181/723 of Q08426
- V40 (≠ D57) to G: in dbSNP:rs1062551
- I41 (≠ E58) to R: in dbSNP:rs1062552
- T75 (≠ K93) to I: in dbSNP:rs1062553
- K165 (≠ E183) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- K171 (≠ E189) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
Sites not aligning to the query:
- 3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
- 274 A → T: in dbSNP:rs2302819
- 325 A → G: in dbSNP:rs1062555
- 346 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- 584 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- 598 K → T: in dbSNP:rs1042437
- 606 T → P: in dbSNP:rs1042438
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
34% identity, 53% coverage: 29:171/268 of query aligns to 11:153/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
29% identity, 82% coverage: 46:265/268 of query aligns to 38:261/268 of 4elxA
- active site: G83 (= G78), H88 (= H90), L92 (= L94), G116 (≠ V119), V119 (≠ E122), G139 (≠ E142), S144 (≠ Q147), D146 (≠ P149), G147 (= G150), A233 (≠ E237), Y241 (≠ R245)
- binding chloride ion: G115 (= G118), G139 (≠ E142), W167 (≠ V170)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
28% identity, 88% coverage: 29:265/268 of query aligns to 31:274/281 of 3t88A
- active site: G82 (= G78), R87 (vs. gap), Y93 (≠ F83), H101 (≠ V91), L105 (≠ A95), G129 (≠ V119), V132 (≠ E122), G152 (≠ E142), S157 (≠ Q147), D159 (≠ P149), G160 (= G150), A246 (≠ E237), Y254 (≠ R245)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ P37), V40 (≠ F38), R41 (vs. gap), A43 (≠ V40), S80 (= S76), G81 (= G77), G82 (= G78), D83 (= D79), Q84 (≠ I80), K85 (= K81), Y93 (≠ F83), V104 (≠ L94), L105 (≠ A95), Y125 (≠ F115), G129 (≠ V119), T151 (≠ P141), V155 (≠ L145), F158 (≠ I148), D159 (≠ P149), T250 (≠ Y241), Y254 (≠ R245), F266 (= F257), K269 (= K260)
Query Sequence
>WP_012405853.1 NCBI__GCF_000020045.1:WP_012405853.1
MTDLTHRGQTLLQELDGFSIEIDAQRERADIILDRPPFNVISMHARDQLRAAFEALDEDE
RVRVIVVRARGEHFSSGGDIKGFLEASPEHVSKLAWNIAAPARCSKPVIAANRGFCFGVG
FELSLACDFRIATETTFYALPEQKLGQIPGSGGSARLQQMVGIGRTKDIVMRSRRIPGKQ
AYEWGIAVECVADSELEAATDALADELRAFSPLAQRTAKKLLNDTEDSPLSIAIELEGHC
YSRLRASEDFREGVEAFHGKRKPVFRGK
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