SitesBLAST
Comparing H281DRAFT_00916 H281DRAFT_00916 short chain enoyl-CoA hydratase /3-hydroxyacyl-CoA dehydrogenase 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)
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
75% identity, 99% coverage: 5:694/694 of query aligns to 4:692/692 of 6iunB
- active site: A60 (= A61), F65 (= F66), E73 (= E74), H77 (≠ A78), G101 (= G102), E104 (= E105), E124 (= E125), G132 (= G133), K248 (≠ A250), S407 (= S409), H428 (= H430), E440 (= E442), N478 (= N480)
- binding nicotinamide-adenine-dinucleotide: G300 (= G302), T301 (= T303), M302 (= M304), E321 (= E323), T322 (= T324), Y365 (= Y367), A377 (= A379), V378 (= V380), E380 (= E382), V384 (= V386), V388 (= V390), N405 (= N407), S407 (= S409)
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)
43% identity, 99% coverage: 4:689/694 of query aligns to 3:705/723 of Q08426
- E3 (≠ D4) to 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
- V40 (≠ Q40) to G: in dbSNP:rs1062551
- I41 (≠ N41) to R: in dbSNP:rs1062552
- T75 (= T76) to I: in dbSNP:rs1062553
- K165 (≠ R166) 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 (≠ E172) 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.
- A274 (≠ G274) to T: in dbSNP:rs2302819
- A325 (≠ L321) to G: in dbSNP:rs1062555
- K346 (= K346) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- K584 (= K569) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- K598 (≠ D583) to T: in dbSNP:rs1042437
- T606 (≠ E591) to P: in dbSNP:rs1042438
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
41% identity, 98% coverage: 11:689/694 of query aligns to 16:707/723 of 6zibAAA
- active site: A66 (= A61), F71 (= F66), G81 (≠ A78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), G136 (= G133), K254 (≠ A250), S413 (= S409), H434 (= H430), E446 (= E442), N484 (= N480)
- binding acetoacetyl-coenzyme a: P25 (= P20), V26 (= V21), A64 (≠ G59), G65 (= G60), A66 (= A61), D67 (= D62), I68 (= I63), G104 (= G101), G105 (= G102), E128 (= E125), Y161 (≠ P158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ T324), Q336 (≠ A328), A383 (= A379), V384 (= V380), F385 (= F381), E386 (= E382), N411 (= N407), H434 (= H430)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
41% identity, 98% coverage: 11:689/694 of query aligns to 16:707/723 of 6zicAAA
- active site: A66 (= A61), F71 (= F66), G81 (≠ A78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), G136 (= G133), K254 (≠ A250), S413 (= S409), H434 (= H430), E446 (= E442), N484 (= N480)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P20), V26 (= V21), A28 (≠ G23), A66 (= A61), D67 (= D62), I68 (= I63), G104 (= G101), G105 (= G102), E108 (= E105), E128 (= E125), Y161 (≠ P158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G300), G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ T324), Q336 (≠ A328), A383 (= A379), V384 (= V380), F385 (= F381), E386 (= E382), L390 (≠ V386), K391 (= K387), N411 (= N407), S413 (= S409), H434 (= H430)
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
41% identity, 98% coverage: 11:689/694 of query aligns to 17:703/716 of 6z5oAAA
- active site: A67 (= A61), F72 (= F66), G82 (≠ A78), G106 (= G102), E109 (= E105), P128 (= P124), E129 (= E125), G137 (= G133), K255 (≠ A250), S409 (= S409), H430 (= H430), E442 (= E442), N480 (= N480)
- binding coenzyme a: P26 (= P20), V27 (= V21), A65 (≠ G59), D68 (= D62), I69 (= I63), P128 (= P124), Y162 (≠ P158), F277 (= F272), K281 (≠ R276)
- binding nicotinamide-adenine-dinucleotide: G309 (= G300), G311 (= G302), T312 (= T303), M313 (= M304), E332 (= E323), S333 (≠ T324), Q337 (≠ A328), A379 (= A379), V380 (= V380), F381 (= F381), E382 (= E382), K387 (= K387), N407 (= N407), S409 (= S409), H430 (= H430)
- binding nicotinamide: A67 (= A61), E109 (= E105), E129 (= E125), P136 (= P132), F261 (= F256)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
41% identity, 98% coverage: 11:689/694 of query aligns to 17:710/727 of 3zwaA
- active site: A67 (= A61), F72 (= F66), G82 (≠ A78), G106 (= G102), E109 (= E105), P128 (= P124), E129 (= E125), P136 (= P132), G137 (= G133), K255 (≠ A250), S416 (= S409), H437 (= H430), E449 (= E442), N487 (= N480)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V21), A65 (≠ G59), G66 (= G60), A67 (= A61), D68 (= D62), I69 (= I63), L104 (≠ M100), E109 (= E105), R124 (≠ Q120), E129 (= E125), L132 (= L128), G137 (= G133), Y162 (≠ P158)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
41% identity, 98% coverage: 11:689/694 of query aligns to 16:709/725 of 5omoA
- active site: A66 (= A61), F71 (= F66), G81 (≠ A78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (≠ A250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding (s)-3-hydroxydecanoyl-coa: P25 (= P20), V26 (= V21), A28 (≠ G23), P31 (≠ L26), A64 (≠ G59), A66 (= A61), D67 (= D62), I68 (= I63), L103 (≠ M100), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), Y161 (≠ P158), F260 (= F256), K280 (≠ R276)
- binding 3-keto-decanoyl-coa: S415 (= S409), N486 (= N480), K519 (≠ A513), M520 (= M514), V525 (≠ M519), Y658 (= Y639)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
41% identity, 98% coverage: 11:689/694 of query aligns to 16:709/725 of 5mgbA
- active site: A66 (= A61), F71 (= F66), G81 (≠ A78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (≠ A250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding acetoacetyl-coenzyme a: P25 (= P20), V26 (= V21), A64 (≠ G59), G65 (= G60), A66 (= A61), D67 (= D62), I68 (= I63), G105 (= G102), E128 (= E125), Y161 (≠ P158)
- binding nicotinamide-adenine-dinucleotide: L307 (≠ I299), G308 (= G300), G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ T324), Q336 (≠ A328), V386 (= V380), F387 (= F381), E388 (= E382), N413 (= N407), S415 (= S409), H436 (= H430)
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
41% identity, 98% coverage: 11:689/694 of query aligns to 16:709/725 of 3zwcA
- active site: A66 (= A61), F71 (= F66), G81 (≠ A78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (≠ A250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V21), A64 (≠ G59), G65 (= G60), A66 (= A61), D67 (= D62), I68 (= I63), G77 (≠ E74), L78 (≠ P75), L80 (= L77), V101 (= V98), G104 (= G101), G105 (= G102), E108 (= E105), E128 (= E125), F260 (= F256)
- binding nicotinamide-adenine-dinucleotide: G308 (= G300), G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), Q336 (≠ A328), A385 (= A379), V386 (= V380), F387 (= F381), E388 (= E382), K393 (= K387), N413 (= N407), S415 (= S409), H436 (= H430)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
41% identity, 98% coverage: 11:689/694 of query aligns to 16:709/725 of 2x58A
- active site: A66 (= A61), F71 (= F66), G81 (≠ A78), G105 (= G102), E108 (= E105), P127 (= P124), E128 (= E125), P135 (= P132), G136 (= G133), K254 (≠ A250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding adenosine-5'-diphosphate: G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ T324), Q336 (≠ A328), V386 (= V380), L392 (≠ V386)
- binding coenzyme a: V26 (= V21), A28 (≠ G23), A64 (≠ G59), A66 (= A61), D67 (= D62), I68 (= I63), E128 (= E125)
3zw9A Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with (2s,3s)-3-hydroxy-2- methylbutanoyl-coa (see paper)
41% identity, 98% coverage: 11:689/694 of query aligns to 14:707/723 of 3zw9A
- active site: A64 (= A61), F69 (= F66), G79 (≠ A78), G103 (= G102), E106 (= E105), P125 (= P124), E126 (= E125), P133 (= P132), G134 (= G133), K252 (≠ A250), S413 (= S409), H434 (= H430), E446 (= E442), N484 (= N480)
- binding nicotinamide-adenine-dinucleotide: L305 (≠ I299), G306 (= G300), G308 (= G302), T309 (= T303), M310 (= M304), E329 (= E323), Q334 (≠ A328), A383 (= A379), V384 (= V380), F385 (= F381), E386 (= E382), N411 (= N407), S413 (= S409), H434 (= H430)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (= V21), A62 (≠ G59), G63 (= G60), A64 (= A61), I66 (= I63), G102 (= G101), G103 (= G102), E106 (= E105), E126 (= E125), P133 (= P132), Y159 (≠ P158)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
41% identity, 98% coverage: 11:689/694 of query aligns to 16:709/725 of 3zwbA
- active site: A66 (= A61), G81 (≠ A78), G105 (= G102), E108 (= E105), P127 (= P124), A128 (≠ E125), P135 (= P132), G136 (= G133), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding (2E)-Hexenoyl-CoA: P25 (= P20), V26 (= V21), A28 (≠ G23), A64 (≠ G59), G65 (= G60), A66 (= A61), D67 (= D62), I68 (= I63), V101 (= V98), L103 (≠ M100), G105 (= G102), E108 (= E105), G136 (= G133), Y161 (≠ P158), K280 (≠ R276)
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
34% identity, 98% coverage: 16:694/694 of query aligns to 24:715/715 of 1wdlA
- active site: A69 (= A61), N89 (vs. gap), N93 (vs. gap), G117 (= G102), E120 (= E105), P139 (= P124), E140 (= E125), P147 (= P132), G148 (= G133), S430 (= S409), H451 (= H430), E463 (= E442), N501 (= N480)
- binding nicotinamide-adenine-dinucleotide: A322 (= A301), I324 (≠ T303), M325 (= M304), D344 (≠ E323), I345 (≠ T324), A400 (= A379), V401 (= V380), E403 (= E382), N428 (= N407), T429 (= T408), S430 (= S409)
P28793 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi (see paper)
34% identity, 98% coverage: 16:694/694 of query aligns to 24:715/715 of P28793
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
34% identity, 98% coverage: 16:694/694 of query aligns to 24:707/707 of 1wdmA
- active site: A69 (= A61), N89 (vs. gap), N93 (vs. gap), G117 (= G102), E120 (= E105), P139 (= P124), E140 (= E125), P147 (= P132), G148 (= G133), S430 (= S409), H451 (= H430), E463 (= E442), N501 (= N480)
- binding acetyl coenzyme *a: K142 (= K127), D297 (≠ E275), M459 (= M438), N501 (= N480), P534 (≠ A513), Y652 (≠ T637), L658 (= L643)
- binding nicotinamide-adenine-dinucleotide: G321 (= G300), A322 (= A301), I324 (≠ T303), M325 (= M304), D344 (≠ E323), V401 (= V380), E403 (= E382), N428 (= N407), S430 (= S409), N454 (≠ S433)
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
34% identity, 94% coverage: 8:656/694 of query aligns to 14:679/729 of P21177
- G116 (= G102) mutation to F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
- G322 (= G302) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H430) active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
34% identity, 94% coverage: 8:656/694 of query aligns to 14:679/719 of 6tnmA
- active site: A68 (= A61), F73 (= F66), G116 (= G102), E119 (= E105), P138 (= P124), E139 (= E125), G147 (= G133), N271 (≠ A250), S429 (= S409), H450 (= H430), E462 (= E442), N500 (= N480)
- binding adenosine-5'-triphosphate: D343 (≠ E323), I344 (≠ T324), V400 (= V380), V401 (≠ F381), V406 (= V386), K584 (= K560)
P40939 Trifunctional enzyme subunit alpha, mitochondrial; 78 kDa gastrin-binding protein; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Homo sapiens (Human) (see 5 papers)
32% identity, 96% coverage: 3:667/694 of query aligns to 41:736/763 of P40939
- V282 (= V220) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (= I234) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (≠ A271) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E442) active site, For hydroxyacyl-coenzyme A dehydrogenase activity; to Q: in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137852769
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
34% identity, 99% coverage: 9:692/694 of query aligns to 11:702/707 of 6yswA
- active site: A66 (= A61), I71 (≠ F66), A84 (= A78), Q88 (vs. gap), G112 (= G102), E115 (= E105), P136 (= P124), E137 (= E125), G145 (= G133), D264 (≠ A250), S422 (= S409), H443 (= H430), E455 (= E442), N493 (= N480)
- binding coenzyme a: E23 (vs. gap), M25 (≠ V21), A66 (= A61), D67 (= D62), I68 (= I63), P136 (= P124), E137 (= E125), L140 (= L128), T290 (≠ R276), K293 (≠ S279)
8pf8A Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-72
31% identity, 92% coverage: 9:647/694 of query aligns to 22:687/729 of 8pf8A
- binding [2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boronic acid: G76 (= G60), F169 (≠ I144), N173 (≠ A148), S177 (≠ N151), I193 (≠ S167), F313 (= F273)
- binding bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]-bis(oxidanyl)boranuide: M39 (≠ L24), N40 (≠ G25), E41 (≠ L26), T81 (≠ E65), D92 (vs. gap), V93 (vs. gap)
- binding [(2~{R})-2,3-bis(oxidanyl)propoxy]-[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]borinic acid: M39 (≠ L24), G77 (≠ A61), D78 (= D62), M82 (vs. gap), V93 (vs. gap)
- binding (2~{R})-3-bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boranyloxypropane-1,2-diol: T152 (≠ K127), R184 (≠ P158), A311 (= A271), F312 (= F272), I673 (≠ M633)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_00916 H281DRAFT_00916 short chain enoyl-CoA hydratase /3-hydroxyacyl-CoA dehydrogenase
MAVDYTTHDGVAVITLNNPPVNGLGLSTRAGIVEGIERAQNDAAIKAIVLTGAGKAFSGG
ADITEFNTPKATQEPTLATVIKTVEGSPKPVVAAIHSVAMGGGLELALGAHYRIAAPGAQ
IALPEVKLGILPGAGGTQRLPRAIGLEAALNMIVSGAPVMSQDLARSGLFDELADGDLTE
AALAFARKVGAKEGPHPKVRERKIEHPNAEGFIQFARNSVATVAKNFPAPLKCIDAVEAG
VKNGFDKGLAVERECFVALVQTPESRALRHAFFGERAASKIPDVPADTPVREIRQVAVIG
AGTMGGGIAMNFISAGIPVTLLETKQEALDRGLATIRKNYEATVKKGKLKPEALEERMAL
ITPTLSYDDLKNADLIVEAVFEELGVKEQVFKRLDEVAKSGAILASNTSTLDVDKIAAFT
RRPQDVVGMHFFSPANVMKLLEVVRGKETAKDVLATVMKLAKKIKKTAVVSGVCDGFIGN
RMIEQYIRQALFMLDEGALPAQVDRAIEKFGFAMGPFRMSDLAGNDIGWAIRKRRYEEHP
EMHYSKIADRLCETGRFGQKTGGGWYDYKAGDRTAHPSKLVDDMIVAYSNETNTQRRKIG
DDEIVERLVFALVNEGAKILEEGIASKPSDIDMVYLTGYGFPLYRGGPMLYADTVGLYNV
ERAIRRYASQPNGDAWQLAPSIAELAAQGRGFNG
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