SitesBLAST
Comparing AO356_26645 FitnessBrowser__pseudo5_N2C3_1:AO356_26645 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)
34% identity, 89% coverage: 30:267/267 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (≠ G77), F70 (= F82), S82 (≠ A98), R86 (= R102), G110 (≠ V118), E113 (= E121), P132 (= P140), E133 (= E141), I138 (≠ Q146), P140 (= P148), G141 (= G149), A226 (≠ E234), F236 (≠ R244)
- binding coenzyme a: K24 (≠ P36), L25 (= L37), A63 (≠ S75), G64 (= G76), A65 (≠ G77), D66 (= D78), I67 (= I79), P132 (= P140), R166 (= R174), F248 (= F256), K251 (= K259)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
30% identity, 86% coverage: 38:266/267 of query aligns to 27:260/261 of 5jbxB
- active site: A67 (≠ G77), R72 (≠ F82), L84 (vs. gap), R88 (≠ A94), G112 (≠ V118), E115 (= E121), T134 (≠ P140), E135 (= E141), I140 (≠ Q146), P142 (= P148), G143 (= G149), A228 (≠ E234), L238 (≠ R244)
- binding coenzyme a: A28 (≠ V39), A65 (≠ S75), D68 (= D78), L69 (≠ I79), K70 (= K80), L110 (≠ F116), G111 (= G117), T134 (≠ P140), E135 (= E141), L138 (= L144), R168 (= R174)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 88% coverage: 30:264/267 of query aligns to 20:257/260 of 2hw5C
- active site: A68 (≠ G77), M73 (≠ F82), S83 (≠ V90), L87 (≠ A94), G111 (≠ V118), E114 (= E121), P133 (= P140), E134 (= E141), T139 (≠ Q146), P141 (= P148), G142 (= G149), K227 (≠ E234), F237 (≠ R244)
- binding crotonyl coenzyme a: K26 (≠ A35), A27 (≠ P36), L28 (= L37), A30 (≠ V39), K62 (≠ E71), I70 (= I79), F109 (= F116)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
30% identity, 88% coverage: 30:264/267 of query aligns to 20:255/258 of 1mj3A
- active site: A68 (≠ G77), M73 (≠ F82), S83 (≠ K92), L85 (≠ A94), G109 (≠ V118), E112 (= E121), P131 (= P140), E132 (= E141), T137 (≠ Q146), P139 (= P148), G140 (= G149), K225 (≠ E234), F235 (≠ R244)
- binding hexanoyl-coenzyme a: K26 (≠ A35), A27 (≠ P36), L28 (= L37), A30 (≠ V39), A66 (≠ S75), G67 (= G76), A68 (≠ G77), D69 (= D78), I70 (= I79), G109 (≠ V118), P131 (= P140), E132 (= E141), L135 (= L144), G140 (= G149)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 88% coverage: 30:264/267 of query aligns to 20:257/260 of 1dubA
- active site: A68 (≠ G77), M73 (≠ F82), S83 (≠ V90), L87 (≠ A94), G111 (≠ V118), E114 (= E121), P133 (= P140), E134 (= E141), T139 (≠ Q146), P141 (= P148), G142 (= G149), K227 (≠ E234), F237 (≠ R244)
- binding acetoacetyl-coenzyme a: K26 (≠ A35), A27 (≠ P36), L28 (= L37), A30 (≠ V39), A66 (≠ S75), A68 (≠ G77), D69 (= D78), I70 (= I79), Y107 (= Y114), G110 (= G117), G111 (≠ V118), E114 (= E121), P133 (= P140), E134 (= E141), L137 (= L144), G142 (= G149), F233 (≠ Y240), F249 (= F256)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
30% identity, 88% coverage: 30:264/267 of query aligns to 18:255/258 of 1ey3A
- active site: A66 (≠ G77), M71 (≠ F82), S81 (≠ V90), L85 (≠ A94), G109 (≠ V118), E112 (= E121), P131 (= P140), E132 (= E141), T137 (≠ Q146), P139 (= P148), G140 (= G149), K225 (≠ E234), F235 (≠ R244)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A35), L26 (= L37), A28 (≠ V39), A64 (≠ S75), G65 (= G76), A66 (≠ G77), D67 (= D78), I68 (= I79), L85 (≠ A94), W88 (≠ V97), G109 (≠ V118), P131 (= P140), L135 (= L144), G140 (= G149)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 88% coverage: 30:264/267 of query aligns to 19:251/254 of 2dubA
- active site: A67 (≠ G77), M72 (≠ F82), S82 (≠ K92), G105 (≠ V118), E108 (= E121), P127 (= P140), E128 (= E141), T133 (≠ Q146), P135 (= P148), G136 (= G149), K221 (≠ E234), F231 (≠ R244)
- binding octanoyl-coenzyme a: K25 (≠ A35), A26 (≠ P36), L27 (= L37), A29 (≠ V39), A65 (≠ S75), A67 (≠ G77), D68 (= D78), I69 (= I79), K70 (= K80), G105 (≠ V118), E108 (= E121), P127 (= P140), E128 (= E141), G136 (= G149), A137 (≠ S150)
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)
30% identity, 88% coverage: 30:264/267 of query aligns to 50:287/290 of P14604
- E144 (= E121) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E141) 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 88% coverage: 30:264/267 of query aligns to 16:249/250 of 3q0gD
- active site: A64 (≠ G77), M69 (≠ F82), T75 (≠ E88), F79 (≠ K92), G103 (≠ V118), E106 (= E121), P125 (= P140), E126 (= E141), V131 (≠ Q146), P133 (= P148), G134 (= G149), L219 (≠ E234), F229 (≠ R244)
- binding Butyryl Coenzyme A: F225 (≠ Y240), F241 (= F256)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
29% identity, 91% coverage: 23:266/267 of query aligns to 5:256/257 of 6slbAAA
- active site: Q64 (≠ G77), F69 (= F82), L80 (≠ V90), N84 (≠ A94), A108 (≠ V118), S111 (≠ E121), A130 (≠ P140), F131 (≠ E141), L136 (≠ Q146), P138 (= P148), D139 (≠ G149), A224 (≠ E234), G234 (≠ R244)
- 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 (≠ E71), A62 (≠ S75), Q64 (≠ G77), D65 (= D78), L66 (≠ I79), Y76 (vs. gap), A108 (≠ V118), F131 (≠ E141), D139 (≠ G149)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
28% identity, 88% coverage: 30:264/267 of query aligns to 16:253/256 of 3h81A
- active site: A64 (≠ G77), M69 (≠ F82), T79 (≠ K92), F83 (vs. gap), G107 (≠ V118), E110 (= E121), P129 (= P140), E130 (= E141), V135 (≠ Q146), P137 (= P148), G138 (= G149), L223 (≠ E234), F233 (≠ R244)
- binding calcium ion: F233 (≠ R244), Q238 (≠ F249)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
28% identity, 88% coverage: 30:264/267 of query aligns to 17:254/255 of 3q0jC
- active site: A65 (≠ G77), M70 (≠ F82), T80 (≠ K92), F84 (vs. gap), G108 (≠ V118), E111 (= E121), P130 (= P140), E131 (= E141), V136 (≠ Q146), P138 (= P148), G139 (= G149), L224 (≠ E234), F234 (≠ R244)
- binding acetoacetyl-coenzyme a: Q23 (vs. gap), A24 (≠ P36), L25 (= L37), A27 (≠ V39), A63 (≠ S75), G64 (= G76), A65 (≠ G77), D66 (= D78), I67 (= I79), K68 (= K80), M70 (≠ F82), F84 (vs. gap), G107 (= G117), G108 (≠ V118), E111 (= E121), P130 (= P140), E131 (= E141), P138 (= P148), G139 (= G149), M140 (≠ S150)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
28% identity, 88% coverage: 30:264/267 of query aligns to 17:254/255 of 3q0gC
- active site: A65 (≠ G77), M70 (≠ F82), T80 (≠ K92), F84 (vs. gap), G108 (≠ V118), E111 (= E121), P130 (= P140), E131 (= E141), V136 (≠ Q146), P138 (= P148), G139 (= G149), L224 (≠ E234), F234 (≠ R244)
- binding coenzyme a: L25 (= L37), A63 (≠ S75), I67 (= I79), K68 (= K80), Y104 (= Y114), P130 (= P140), E131 (= E141), L134 (= L144)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
29% identity, 91% coverage: 23:266/267 of query aligns to 2:244/245 of 6slaAAA
- active site: Q61 (≠ G77), L68 (≠ V90), N72 (≠ A94), A96 (≠ V118), S99 (≠ E121), A118 (≠ P140), F119 (≠ E141), L124 (≠ Q146), P126 (= P148), N127 (≠ G149), A212 (≠ E234), G222 (≠ R244)
- 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 (= L37), A59 (≠ S75), Q61 (≠ G77), D62 (= D78), L63 (≠ I79), L68 (≠ V90), Y71 (≠ L93), A94 (≠ F116), G95 (= G117), A96 (≠ V118), F119 (≠ E141), I122 (≠ L144), L124 (≠ Q146), N127 (≠ G149), F234 (= F256), K237 (= K259)
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: 38:267/267 of query aligns to 106:339/339 of Q13825
- K109 (≠ S41) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ Q50) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (= A172) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
- 105 K→N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 RNA-binding
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)
28% identity, 87% coverage: 30:260/267 of query aligns to 24:261/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
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)
32% identity, 64% coverage: 28:199/267 of query aligns to 12:182/723 of Q08426
- V40 (≠ D56) to G: in dbSNP:rs1062551
- I41 (≠ A57) to R: in dbSNP:rs1062552
- T75 (≠ K92) to I: in dbSNP:rs1062553
- K165 (≠ A182) 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 (≠ E188) 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
30% identity, 64% coverage: 28:199/267 of query aligns to 11:182/692 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
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
29% identity, 75% coverage: 19:218/267 of query aligns to 9:218/246 of 2vssD
- active site: M68 (≠ G77), Y73 (≠ F82), D78 (≠ E84), R90 (vs. gap), Q94 (≠ K92), G118 (≠ V118), S121 (≠ E121), S140 (≠ P140), E141 (= E141), I146 (≠ Q146), P148 (= P148), G149 (= G149)
- binding acetyl coenzyme *a: E26 (vs. gap), K27 (≠ P36), R28 (≠ L37), A30 (≠ V39), A66 (≠ S75), M68 (≠ G77), D69 (= D78), L70 (≠ I79), F74 (vs. gap), W114 (≠ Y114), F116 (= F116), S140 (≠ P140)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ G77), Y73 (≠ F82), F74 (vs. gap), Q96 (≠ A94), E141 (= E141), G149 (= G149), N150 (≠ S150)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
29% identity, 75% coverage: 19:218/267 of query aligns to 8:217/247 of 2vssB
- active site: M67 (≠ G77), Y72 (≠ F82), D77 (≠ E84), R89 (vs. gap), Q93 (≠ K92), G117 (≠ V118), S120 (≠ E121), S139 (≠ P140), E140 (= E141), I145 (≠ Q146), P147 (= P148), G148 (= G149)
- binding acetyl coenzyme *a: E25 (vs. gap), K26 (≠ P36), R27 (≠ L37), A29 (≠ V39), A65 (≠ S75), M67 (≠ G77), D68 (= D78), W113 (≠ Y114), F115 (= F116), G117 (≠ V118), S139 (≠ P140), E140 (= E141)
Sites not aligning to the query:
Query Sequence
>AO356_26645 FitnessBrowser__pseudo5_N2C3_1:AO356_26645
MQQQAIQQFLDTQFDGFQVEVDVSRERADIILNRAPLNVISMGQRDELRQVFEALDAHKG
VRVIVLRSVGEHFSSGGDIKGFLEASPEHVSKLAWNVAAPARCEKPVIVANRGYTFGVGF
ELSLACDFRIASQTTRYALPEQNLGQIPGSGGSARLQKIIGITRTKHMVMRAKRITGDQA
YAWGIATEVVPDTELESTVDALVDELRRFSPLAQRTAKKLINDNEDAPLTVAIEMEGHCY
SRLRSSKDFKEGVEAFHSKRTAVFIGE
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