SitesBLAST
Comparing RR42_RS22630 RR42_RS22630 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
54% identity, 99% coverage: 3:690/696 of query aligns to 1:688/692 of 6iunB
- active site: A60 (= A62), F65 (= F67), E73 (≠ Q75), H77 (≠ R79), G101 (= G103), E104 (= E106), E124 (= E126), G132 (= G134), K248 (≠ D250), S407 (= S409), H428 (= H430), E440 (= E442), N478 (= N480)
- binding nicotinamide-adenine-dinucleotide: G300 (= G302), T301 (= T303), M302 (= M304), E321 (= E323), T322 (≠ Q324), Y365 (≠ D367), 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)
44% identity, 98% coverage: 5:689/696 of query aligns to 3:705/723 of Q08426
- E3 (≠ Q5) 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 (≠ T41) to G: in dbSNP:rs1062551
- I41 (≠ Q42) to R: in dbSNP:rs1062552
- T75 (= T77) to I: in dbSNP:rs1062553
- K165 (≠ A167) 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 (≠ A173) 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 (= A274) to T: in dbSNP:rs2302819
- A325 (≠ L321) to G: in dbSNP:rs1062555
- K346 (≠ I342) 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 (≠ A571) 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 (≠ A584) to T: in dbSNP:rs1042437
- T606 (≠ E592) to P: in dbSNP:rs1042438
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
46% identity, 97% coverage: 12:689/696 of query aligns to 17:710/727 of 3zwaA
- active site: A67 (= A62), F72 (= F67), G82 (≠ R79), G106 (= G103), E109 (= E106), P128 (= P125), E129 (= E126), P136 (= P133), G137 (= G134), K255 (≠ D250), S416 (= S409), H437 (= H430), E449 (= E442), N487 (= N480)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V22), A65 (≠ G60), G66 (= G61), A67 (= A62), D68 (= D63), I69 (= I64), L104 (= L101), E109 (= E106), R124 (≠ S121), E129 (= E126), L132 (= L129), G137 (= G134), Y162 (≠ P159)
3zw9A Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with (2s,3s)-3-hydroxy-2- methylbutanoyl-coa (see paper)
46% identity, 97% coverage: 12:689/696 of query aligns to 14:707/723 of 3zw9A
- active site: A64 (= A62), F69 (= F67), G79 (≠ R79), G103 (= G103), E106 (= E106), P125 (= P125), E126 (= E126), P133 (= P133), G134 (= G134), K252 (≠ D250), S413 (= S409), H434 (= H430), E446 (= E442), N484 (= N480)
- binding nicotinamide-adenine-dinucleotide: L305 (= L299), 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 (= V22), A62 (≠ G60), G63 (= G61), A64 (= A62), I66 (= I64), G102 (= G102), G103 (= G103), E106 (= E106), E126 (= E126), P133 (= P133), Y159 (≠ P159)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
46% identity, 97% coverage: 12:689/696 of query aligns to 16:709/725 of 5omoA
- active site: A66 (= A62), F71 (= F67), G81 (≠ R79), G105 (= G103), E108 (= E106), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134), K254 (≠ D250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding (s)-3-hydroxydecanoyl-coa: P25 (= P21), V26 (= V22), A28 (≠ G24), P31 (≠ D27), A64 (≠ G60), A66 (= A62), D67 (= D63), I68 (= I64), L103 (= L101), G105 (= G103), E108 (= E106), P127 (= P125), E128 (= E126), Y161 (≠ P159), F260 (= F256), K280 (≠ R276)
- binding 3-keto-decanoyl-coa: S415 (= S409), N486 (= N480), K519 (≠ A513), M520 (= M514), V525 (≠ M519), Y658 (= Y640)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
46% identity, 97% coverage: 12:689/696 of query aligns to 16:709/725 of 5mgbA
- active site: A66 (= A62), F71 (= F67), G81 (≠ R79), G105 (= G103), E108 (= E106), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134), K254 (≠ D250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding acetoacetyl-coenzyme a: P25 (= P21), V26 (= V22), A64 (≠ G60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), G105 (= G103), E128 (= E126), Y161 (≠ P159)
- binding nicotinamide-adenine-dinucleotide: L307 (= L299), G308 (= G300), G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ Q324), 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)
46% identity, 97% coverage: 12:689/696 of query aligns to 16:709/725 of 3zwcA
- active site: A66 (= A62), F71 (= F67), G81 (≠ R79), G105 (= G103), E108 (= E106), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134), K254 (≠ D250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V22), A64 (≠ G60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), G77 (≠ S73), L78 (≠ A74), L80 (= L78), V101 (= V99), G104 (= G102), G105 (= G103), E108 (= E106), E128 (= E126), 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)
46% identity, 97% coverage: 12:689/696 of query aligns to 16:709/725 of 2x58A
- active site: A66 (= A62), F71 (= F67), G81 (≠ R79), G105 (= G103), E108 (= E106), P127 (= P125), E128 (= E126), P135 (= P133), G136 (= G134), K254 (≠ D250), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding adenosine-5'-diphosphate: G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ Q324), Q336 (≠ A328), V386 (= V380), L392 (≠ V386)
- binding coenzyme a: V26 (= V22), A28 (≠ G24), A64 (≠ G60), A66 (= A62), D67 (= D63), I68 (= I64), E128 (= E126)
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
46% identity, 97% coverage: 12:689/696 of query aligns to 16:707/723 of 6zibAAA
- active site: A66 (= A62), F71 (= F67), G81 (≠ R79), G105 (= G103), E108 (= E106), P127 (= P125), E128 (= E126), G136 (= G134), K254 (≠ D250), S413 (= S409), H434 (= H430), E446 (= E442), N484 (= N480)
- binding acetoacetyl-coenzyme a: P25 (= P21), V26 (= V22), A64 (≠ G60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), G104 (= G102), G105 (= G103), E128 (= E126), Y161 (≠ P159)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ Q324), Q336 (≠ A328), A383 (= A379), V384 (= V380), F385 (= F381), E386 (= E382), N411 (= N407), H434 (= H430)
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
46% identity, 97% coverage: 12:689/696 of query aligns to 17:703/716 of 6z5oAAA
- active site: A67 (= A62), F72 (= F67), G82 (≠ R79), G106 (= G103), E109 (= E106), P128 (= P125), E129 (= E126), G137 (= G134), K255 (≠ D250), S409 (= S409), H430 (= H430), E442 (= E442), N480 (= N480)
- binding coenzyme a: P26 (= P21), V27 (= V22), A65 (≠ G60), D68 (= D63), I69 (= I64), P128 (= P125), Y162 (≠ P159), F277 (= F272), K281 (≠ R276)
- binding nicotinamide-adenine-dinucleotide: G309 (= G300), G311 (= G302), T312 (= T303), M313 (= M304), E332 (= E323), S333 (≠ Q324), Q337 (≠ A328), A379 (= A379), V380 (= V380), F381 (= F381), E382 (= E382), K387 (= K387), N407 (= N407), S409 (= S409), H430 (= H430)
- binding nicotinamide: A67 (= A62), E109 (= E106), E129 (= E126), P136 (= P133), F261 (= F256)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
46% identity, 97% coverage: 12:689/696 of query aligns to 16:707/723 of 6zicAAA
- active site: A66 (= A62), F71 (= F67), G81 (≠ R79), G105 (= G103), E108 (= E106), P127 (= P125), E128 (= E126), G136 (= G134), K254 (≠ D250), S413 (= S409), H434 (= H430), E446 (= E442), N484 (= N480)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P21), V26 (= V22), A28 (≠ G24), A66 (= A62), D67 (= D63), I68 (= I64), G104 (= G102), G105 (= G103), E108 (= E106), E128 (= E126), Y161 (≠ P159)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G300), G310 (= G302), T311 (= T303), M312 (= M304), E331 (= E323), S332 (≠ Q324), Q336 (≠ A328), A383 (= A379), V384 (= V380), F385 (= F381), E386 (= E382), L390 (≠ V386), K391 (= K387), N411 (= N407), S413 (= S409), H434 (= H430)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
45% identity, 97% coverage: 12:689/696 of query aligns to 16:709/725 of 3zwbA
- active site: A66 (= A62), G81 (≠ R79), G105 (= G103), E108 (= E106), P127 (= P125), A128 (≠ E126), P135 (= P133), G136 (= G134), S415 (= S409), H436 (= H430), E448 (= E442), N486 (= N480)
- binding (2E)-Hexenoyl-CoA: P25 (= P21), V26 (= V22), A28 (≠ G24), A64 (≠ G60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), V101 (= V99), L103 (= L101), G105 (= G103), E108 (= E106), G136 (= G134), Y161 (≠ P159), K280 (≠ R276)
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)
31% identity, 98% coverage: 4:682/696 of query aligns to 41:750/763 of P40939
- V282 (≠ A218) 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 (= L271) 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
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
34% identity, 89% coverage: 39:658/696 of query aligns to 45:680/715 of 1wdlA
- active site: A69 (= A62), N89 (≠ Q75), N93 (≠ R79), G117 (= G103), E120 (= E106), P139 (= P125), E140 (= E126), P147 (= P133), G148 (= G134), S430 (= S409), H451 (= H430), E463 (= E442), N501 (= N480)
- binding nicotinamide-adenine-dinucleotide: A322 (= A301), I324 (≠ T303), M325 (= M304), D344 (≠ E323), I345 (≠ Q324), 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, 89% coverage: 39:658/696 of query aligns to 45:680/715 of P28793
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
34% identity, 89% coverage: 39:658/696 of query aligns to 45:672/707 of 1wdmA
- active site: A69 (= A62), N89 (≠ Q75), N93 (≠ R79), G117 (= G103), E120 (= E106), P139 (= P125), E140 (= E126), P147 (= P133), G148 (= G134), S430 (= S409), H451 (= H430), E463 (= E442), N501 (= N480)
- binding acetyl coenzyme *a: K142 (≠ N128), D297 (≠ E275), M459 (= M438), N501 (= N480), P534 (≠ A513), Y652 (≠ H638), L658 (≠ A644)
- binding nicotinamide-adenine-dinucleotide: G321 (= G300), A322 (= A301), I324 (≠ T303), M325 (= M304), D344 (≠ E323), V401 (= V380), E403 (= E382), N428 (= N407), S430 (= S409), N454 (≠ S433)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
33% identity, 99% coverage: 8:693/696 of query aligns to 9:702/707 of 6yswA
- active site: A66 (= A62), I71 (≠ F67), A84 (vs. gap), Q88 (≠ R79), G112 (= G103), E115 (= E106), P136 (= P125), E137 (= E126), G145 (= G134), D264 (= D250), S422 (= S409), H443 (= H430), E455 (= E442), N493 (= N480)
- binding coenzyme a: E23 (vs. gap), M25 (≠ V22), A66 (= A62), D67 (= D63), I68 (= I64), P136 (= P125), E137 (= E126), L140 (= L129), T290 (≠ R276), K293 (≠ P279)
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
32% identity, 94% coverage: 12:663/696 of query aligns to 17:685/719 of 6tnmA
- active site: A68 (= A62), F73 (= F67), G116 (= G103), E119 (= E106), P138 (= P125), E139 (= E126), G147 (= G134), N271 (≠ D250), S429 (= S409), H450 (= H430), E462 (= E442), N500 (= N480)
- binding adenosine-5'-triphosphate: D343 (≠ E323), I344 (≠ Q324), V400 (= V380), V401 (≠ F381), V406 (= V386), K584 (= K561)
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)
32% identity, 94% coverage: 12:663/696 of query aligns to 17:685/729 of P21177
- G116 (= G103) 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.
7o4uA Structure of the alpha subunit of mycobacterium tuberculosis beta- oxidation trifunctional enzyme in complex with oxidized nicotinamide adenine dinucleotide (see paper)
29% identity, 98% coverage: 3:683/696 of query aligns to 3:710/711 of 7o4uA
Query Sequence
>RR42_RS22630 RR42_RS22630 3-hydroxyacyl-CoA dehydrogenase
MPTVQYGRQGRIAILLLDNPPVNGLGDTVRLGLFDGIAQATQDDAVAAIVILGAGKVFCG
GADIRQFNAPAASAQPTLRQVIARIEQSAKPVVAAIHGVALGGGMELALGCHYRIASADA
SLGLPEVNLGLVPGGGGTQRLPRLIGVPAALELIQGGKPVRGDKAVALGMADALIDGDPL
AAAMAFAERVAGLPGAHPVIARRPCADAAGVDFAARSAAVSAKARNALAQRAAIACVQAA
TRLPIDAGLDDERARFDQLVASTESKALRHLFFAEREAPKVAALPAGASLRTVARVGILG
AGTMGAGIAMAFANAGIAVTLLEQQQAALDRGLAMIRRNYEITAAKGKLTAQEIAQRMAC
ITPTLADAALADADLVIEAVFEDMAVKKAVFARLDALCKPGAILATNTSRLSIDVIAAST
SRPQDVIGLHFFSPANVMKLLEVVQGERTAPEVIATCMKMARAIGKIPVLVRVCEGFVGN
RMLTPYWREAGFLLEEGASPQQVDGALTRFGMAMGPLAMADLAGMDINWATRKRLAPTRP
AHLRYSKVADRICEQGRFGQKTNAGYYRYEAGSRAPLPDPAVDALIRACAAEAGIERREV
SDEEIVERCMLALANEGARILEEGIARRAADIDVVYVHGYGFPAWRGGPMFHAETIGLGR
TLEKIRALNAIHGEHWTPAPLLVRLVAQGRETFAAG
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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