SitesBLAST
Comparing 6938954 FitnessBrowser__SB2B:6938954 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)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
40% identity, 98% coverage: 4:245/246 of query aligns to 4:247/247 of 7borA
- active site: N63 (= N63), F68 (= F68), D77 (≠ N77), G81 (≠ V81), I105 (= I105), T108 (= T108), F128 (= F128), L133 (= L133), P135 (= P135), E136 (= E136), A222 (≠ H220), L232 (= L230)
- binding coenzyme a: D21 (≠ E21), K22 (= K22), A25 (= A25), S61 (= S61), I65 (≠ V65), V103 (= V103), F128 (= F128), L131 (= L131), F244 (= F242), R247 (≠ K245)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
40% identity, 91% coverage: 1:225/246 of query aligns to 2:227/257 of 6slbAAA
- active site: Q64 (≠ N63), F69 (= F68), L80 (vs. gap), N84 (≠ V81), A108 (≠ I105), S111 (≠ T108), A130 (≠ P127), F131 (= F128), L136 (= L133), P138 (= P135), D139 (≠ E136), A224 (≠ E222)
- 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 (≠ N57), A62 (≠ S61), Q64 (≠ N63), D65 (= D64), L66 (≠ V65), Y76 (≠ H78), A108 (≠ I105), F131 (= F128), D139 (≠ E136)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
40% identity, 90% coverage: 4:225/246 of query aligns to 2:215/245 of 6slaAAA
- active site: Q61 (≠ N63), L68 (= L69), N72 (≠ E73), A96 (≠ I105), S99 (≠ T108), A118 (≠ P127), F119 (= F128), L124 (= L133), P126 (= P135), N127 (≠ E136), A212 (≠ E222)
- 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 (≠ R23), A59 (≠ S61), Q61 (≠ N63), D62 (= D64), L63 (≠ V65), L68 (= L69), Y71 (≠ S72), A94 (≠ V103), G95 (= G104), A96 (≠ I105), F119 (= F128), I122 (≠ L131), L124 (= L133), N127 (≠ E136)
Sites not aligning to the query:
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
32% identity, 97% coverage: 8:245/246 of query aligns to 21:263/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 94% coverage: 15:245/246 of query aligns to 17:251/259 of 5zaiC
- active site: A65 (≠ N63), F70 (= F68), S82 (≠ H78), R86 (= R82), G110 (≠ I105), E113 (≠ T108), P132 (= P127), E133 (≠ F128), I138 (≠ L133), P140 (= P135), G141 (≠ E136), A226 (≠ H220), F236 (≠ L230)
- binding coenzyme a: K24 (= K22), L25 (≠ R23), A63 (≠ S61), G64 (= G62), A65 (≠ N63), D66 (= D64), I67 (≠ V65), P132 (= P127), R166 (≠ P161), F248 (= F242), K251 (= K245)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
29% identity, 95% coverage: 12:245/246 of query aligns to 17:252/260 of 2hw5C
- active site: A68 (≠ N63), M73 (≠ L69), S83 (≠ P79), L87 (= L84), G111 (≠ I105), E114 (≠ T108), P133 (= P127), E134 (≠ F128), T139 (≠ L133), P141 (= P135), G142 (≠ E136), K227 (≠ H220), F237 (≠ L230)
- binding crotonyl coenzyme a: K26 (≠ E21), A27 (≠ K22), L28 (≠ R23), A30 (= A25), K62 (≠ N57), I70 (≠ V65), F109 (≠ V103)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
26% identity, 85% coverage: 1:209/246 of query aligns to 5:221/246 of 6p5uE
- active site: M67 (≠ N63), Y72 (≠ F68), D77 (≠ E73), R89 (≠ F83), A93 (≠ L87), G117 (≠ I105), T120 (= T108), E140 (≠ F128), I145 (≠ L133), P147 (= P135), A148 (≠ E136)
- binding coenzyme a: D25 (≠ E21), K26 (= K22), R27 (= R23), A29 (= A25), A65 (≠ S61), M67 (≠ N63), D68 (= D64), L69 (≠ V65), W113 (≠ S101), F115 (≠ V103), S139 (≠ P127), W143 (≠ L131)
Sites not aligning to the query:
Q9Y232 Chromodomain Y-like protein; CDY-like; Crotonyl-CoA hydratase; EC 4.2.1.- from Homo sapiens (Human) (see 5 papers)
26% identity, 92% coverage: 4:229/246 of query aligns to 344:569/598 of Q9Y232
- S521 (≠ N174) mutation to A: Abolishes CoA-binding and ability to inhibit histone crotonylation.
Sites not aligning to the query:
- 2 T → A: in dbSNP:rs3812179
- 9 S → P: in dbSNP:rs3812178
- 48 V → A: in dbSNP:rs13196069
- 60 A → G: in dbSNP:rs28360500
- 61:309 Interaction with EZH2
- 135 modified: N6,N6,N6-trimethyllysine; by EHMT2; alternate; modified: N6,N6-dimethyllysine; by EHMT2; alternate; modified: N6-methyllysine; by EHMT2; alternate
- 205 S→A: No impact on recruitment to DNA double strand breaks.
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
28% identity, 83% coverage: 15:219/246 of query aligns to 69:290/327 of Q62651
- D176 (≠ T108) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F128) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ E136) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 94% coverage: 14:245/246 of query aligns to 20:258/266 of O53561
- K135 (= K123) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 123:130, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N130) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
27% identity, 95% coverage: 12:245/246 of query aligns to 17:250/258 of 1mj3A
- active site: A68 (≠ N63), M73 (≠ L69), S83 (≠ P79), L85 (≠ V81), G109 (≠ I105), E112 (≠ T108), P131 (= P127), E132 (≠ F128), T137 (≠ L133), P139 (= P135), G140 (≠ E136), K225 (≠ H220), F235 (≠ L230)
- binding hexanoyl-coenzyme a: K26 (≠ E21), A27 (≠ K22), L28 (≠ R23), A30 (= A25), A66 (≠ S61), G67 (= G62), A68 (≠ N63), D69 (= D64), I70 (≠ V65), G109 (≠ I105), P131 (= P127), E132 (≠ F128), L135 (= L131), G140 (≠ E136)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
27% identity, 98% coverage: 4:245/246 of query aligns to 5:244/250 of 3q0gD
- active site: A64 (≠ N63), M69 (≠ F68), T75 (≠ P79), F79 (= F83), G103 (≠ I105), E106 (≠ T108), P125 (= P127), E126 (≠ F128), V131 (≠ L133), P133 (= P135), G134 (≠ E136), L219 (≠ H220), F229 (≠ L230)
- binding Butyryl Coenzyme A: F225 (= F226), F241 (= F242)
Q9WTK2 Chromodomain Y-like protein; CDY-like; Crotonyl-CoA hydratase; Putative histone acetyltransferase Cdyl; EC 4.2.1.-; EC 2.3.1.48 from Mus musculus (Mouse) (see paper)
25% identity, 92% coverage: 4:229/246 of query aligns to 339:564/593 of Q9WTK2
- S516 (≠ N174) mutation to A: Abolishes CoA-binding. No effect on transcriptional repressor activity.
Sites not aligning to the query:
- 588:589 RK→AA: Abolishes CoA-binding. No effect on transcriptional repressor activity.
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
27% identity, 98% coverage: 4:245/246 of query aligns to 6:249/255 of 3q0jC
- active site: A65 (≠ N63), M70 (≠ L69), T80 (≠ P79), F84 (= F83), G108 (≠ I105), E111 (≠ T108), P130 (= P127), E131 (≠ F128), V136 (≠ L133), P138 (= P135), G139 (≠ E136), L224 (≠ H220), F234 (≠ L230)
- binding acetoacetyl-coenzyme a: Q23 (≠ E21), A24 (≠ K22), L25 (≠ R23), A27 (= A25), A63 (≠ S61), G64 (= G62), A65 (≠ N63), D66 (= D64), I67 (≠ V65), K68 (≠ A66), M70 (≠ L69), F84 (= F83), G107 (= G104), G108 (≠ I105), E111 (≠ T108), P130 (= P127), E131 (≠ F128), P138 (= P135), G139 (≠ E136), M140 (≠ A137)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
27% identity, 98% coverage: 4:245/246 of query aligns to 6:249/255 of 3q0gC
- active site: A65 (≠ N63), M70 (≠ L69), T80 (≠ P79), F84 (= F83), G108 (≠ I105), E111 (≠ T108), P130 (= P127), E131 (≠ F128), V136 (≠ L133), P138 (= P135), G139 (≠ E136), L224 (≠ H220), F234 (≠ L230)
- binding coenzyme a: L25 (≠ R23), A63 (≠ S61), I67 (≠ V65), K68 (≠ A66), Y104 (≠ S101), P130 (= P127), E131 (≠ F128), L134 (= L131)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
27% identity, 98% coverage: 4:245/246 of query aligns to 5:248/256 of 3h81A
- active site: A64 (≠ N63), M69 (≠ L69), T79 (≠ P79), F83 (= F83), G107 (≠ I105), E110 (≠ T108), P129 (= P127), E130 (≠ F128), V135 (≠ L133), P137 (= P135), G138 (≠ E136), L223 (≠ H220), F233 (≠ L230)
- binding calcium ion: F233 (≠ L230), Q238 (≠ A235)
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
27% identity, 85% coverage: 11:218/246 of query aligns to 17:227/244 of 6l3pA
- active site: M69 (≠ N63), Y74 (≠ F68), R86 (≠ H78), Q90 (≠ R82), G114 (≠ I105), S117 (≠ T108), S136 (≠ P127), E137 (≠ F128), I142 (≠ L133), P144 (= P135), G145 (≠ E136)
- binding coenzyme a: K28 (= K22), R29 (= R23), A31 (= A25), A67 (≠ S61), M69 (≠ N63), D70 (= D64), L71 (≠ V65), G113 (= G104)
Sites not aligning to the query:
O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
26% identity, 80% coverage: 10:206/246 of query aligns to 17:221/276 of O69762
- K29 (= K22) binding
- A68 (≠ S61) binding
- M70 (≠ N63) binding
- L72 (≠ V65) binding
- Y75 (≠ F68) binding
- G120 (≠ I105) binding
- S123 (≠ T108) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ P127) binding
- E143 (≠ F128) mutation to A: Abolishes catalytic activity.
- W146 (≠ L131) binding
- G151 (≠ E136) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 239 binding ; Y→F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
26% identity, 80% coverage: 10:206/246 of query aligns to 15:219/246 of 2vssD
- active site: M68 (≠ N63), Y73 (≠ F68), D78 (≠ E73), R90 (≠ H78), Q94 (≠ R82), G118 (≠ I105), S121 (≠ T108), S140 (≠ P127), E141 (≠ F128), I146 (≠ L133), P148 (= P135), G149 (≠ E136)
- binding acetyl coenzyme *a: E26 (= E21), K27 (= K22), R28 (= R23), A30 (= A25), A66 (≠ S61), M68 (≠ N63), D69 (= D64), L70 (≠ V65), F74 (≠ L69), W114 (≠ S101), F116 (≠ V103), S140 (≠ P127)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ N63), Y73 (≠ F68), F74 (≠ L69), Q96 (≠ L84), E141 (≠ F128), G149 (≠ E136), N150 (≠ A137)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
26% identity, 80% coverage: 10:206/246 of query aligns to 14:218/247 of 2vssB
- active site: M67 (≠ N63), Y72 (≠ F68), D77 (≠ E73), R89 (≠ H78), Q93 (≠ R82), G117 (≠ I105), S120 (≠ T108), S139 (≠ P127), E140 (≠ F128), I145 (≠ L133), P147 (= P135), G148 (≠ E136)
- binding acetyl coenzyme *a: E25 (= E21), K26 (= K22), R27 (= R23), A29 (= A25), A65 (≠ S61), M67 (≠ N63), D68 (= D64), W113 (≠ S101), F115 (≠ V103), G117 (≠ I105), S139 (≠ P127), E140 (≠ F128)
Sites not aligning to the query:
Query Sequence
>6938954 FitnessBrowser__SB2B:6938954
MSKILVKDLDGVRVISFNRPEKRNALDLDMYRQLTEYLMQGESDNDIRAFLLTGEANCFT
SGNDVADFLQNSELGPNHPAVRFLYCLLELRKPLVAAVSGSAVGIGTTLLLHCDLVYADN
SAKFQLPFVNLALVPEAGASILLPELVGYQKAAELLLLAEPFDAETALSLKLINALCSKE
ELQQTALDKARKLASQPPQALQQTRQLMRPHKHRVQHQMHLELEAFGERLKSDEAKARFQ
AFLTKS
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