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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]

 FADB_ECOLI              Reviewed;         729 AA.
P21177; Q2M8E9;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 2.
22-NOV-2017, entry version 163.
RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01621};
Includes:
RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01621};
EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621};
EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621};
EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621};
Includes:
RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621};
EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621};
Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621}; Synonyms=oldB;
OrderedLocusNames=b3846, JW3822;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1699931; DOI=10.1128/jb.172.11.6459-6468.1990;
Dirusso C.C.;
"Primary sequence of the Escherichia coli fadBA operon, encoding the
fatty acid-oxidizing multienzyme complex, indicates a high degree of
homology to eucaryotic enzymes.";
J. Bacteriol. 172:6459-6468(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
STRAIN=K12;
PubMed=2191949;
Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M.;
"Nucleotide sequence of the fadA gene. Primary structure of 3-
ketoacyl-coenzyme A thiolase from Escherichia coli and the structural
organization of the fadAB operon.";
J. Biol. Chem. 265:10424-10429(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=2204034; DOI=10.1093/nar/18.16.4937;
Nakahigashi K., Inokuchi H.;
"Nucleotide sequence of the fadA and fadB genes from Escherichia
coli.";
Nucleic Acids Res. 18:4937-4937(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1712230; DOI=10.1021/bi00241a023;
Yang X.Y.H., Schulz H., Elzinga M., Yang S.Y.;
"Nucleotide sequence of the promoter and fadB gene of the fadBA operon
and primary structure of the multifunctional fatty acid oxidation
protein from Escherichia coli.";
Biochemistry 30:6788-6795(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=1379743; DOI=10.1126/science.1379743;
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
"Analysis of the Escherichia coli genome: DNA sequence of the region
from 84.5 to 86.5 minutes.";
Science 257:771-778(1992).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[8]
FUNCTION, AND SUBUNIT.
PubMed=368024;
Pramanik A., Pawar S., Antonian E., Schulz H.;
"Five different enzymatic activities are associated with the
multienzyme complex of fatty acid oxidation from Escherichia coli.";
J. Bacteriol. 137:469-473(1979).
[9]
FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=1748662;
Smeland T.E., Cuebas D., Schulz H.;
"Epimerization of 3-hydroxy-4-trans-decenoyl coenzyme A by a
dehydration/hydration mechanism catalyzed by the multienzyme complex
of fatty acid oxidation from Escherichia coli.";
J. Biol. Chem. 266:23904-23908(1991).
[10]
FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, ACTIVE
SITE, MUTAGENESIS OF GLY-116, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8454629;
Yang S.Y., Elzinga M.;
"Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl
coenzyme A epimerase with an active site in the amino-terminal domain
of the multifunctional fatty acid oxidation protein from Escherichia
coli.";
J. Biol. Chem. 268:6588-6592(1993).
[11]
FUNCTION AS A DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVE SITE, NAD-BINDING, AND MUTAGENESIS OF GLY-322 AND
HIS-450.
PubMed=8755745; DOI=10.1021/bi960374y;
He X.Y., Yang S.Y.;
"Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A
dehydrogenase associated with the large alpha-subunit of the
multienzyme complex of fatty acid oxidation from Escherichia coli.";
Biochemistry 35:9625-9630(1996).
[12]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[13]
FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=12535077; DOI=10.1046/j.1365-2958.2003.03341.x;
Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.;
"A new Escherichia coli metabolic competency: growth on fatty acids by
a novel anaerobic beta-oxidation pathway.";
Mol. Microbiol. 47:793-805(2003).
-!- FUNCTION: Involved in the aerobic and anaerobic degradation of
long-chain fatty acids via beta-oxidation cycle. Catalyzes the
formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA.
It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as
substrate. {ECO:0000255|HAMAP-Rule:MF_01621,
ECO:0000269|PubMed:12535077, ECO:0000269|PubMed:1748662,
ECO:0000269|PubMed:368024, ECO:0000269|PubMed:8454629,
ECO:0000269|PubMed:8755745}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH. {ECO:0000255|HAMAP-Rule:MF_01621}.
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01621}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
hydroxybutanoyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01621}.
-!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CoA. {ECO:0000255|HAMAP-Rule:MF_01621}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=53 uM for crotonyl-CoA (for enoyl-CoA hydratase activity)
{ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629,
ECO:0000269|PubMed:8755745};
KM=8.7 mM for L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA
hydratase activity) {ECO:0000269|PubMed:1748662,
ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745};
KM=38 mM for D-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA
hydratase activity) {ECO:0000269|PubMed:1748662,
ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745};
KM=5.8 uM for 3-cis-tetradecenoyl-CoA (for Delta(3)-cis-
Delta(2)-trans-enoyl-CoA isomerase activity)
{ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629,
ECO:0000269|PubMed:8755745};
KM=69 uM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA
dehydrogenase activity) {ECO:0000269|PubMed:1748662,
ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745};
KM=2.0 uM for NADH (for 3-hydroxyacyl-CoA dehydrogenase
activity) {ECO:0000269|PubMed:1748662,
ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745};
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
{ECO:0000255|HAMAP-Rule:MF_01621}.
-!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
chains (FadA). {ECO:0000255|HAMAP-Rule:MF_01621,
ECO:0000269|PubMed:368024}.
-!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids
of, at least, 12 carbon atoms). When LCFAs are present in the
medium, they are converted to long-chain acyl-CoAs which bind to
FadR resulting in its release from the DNA and thus derepression
of the transcription.
-!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}.
-!- SIMILARITY: In the C-terminal section; belongs to the 3-
hydroxyacyl-CoA dehydrogenase family. {ECO:0000255|HAMAP-
Rule:MF_01621}.
-----------------------------------------------------------------------
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EMBL; M59368; AAA23750.1; -; Genomic_DNA.
EMBL; X52837; CAB40809.1; -; Genomic_DNA.
EMBL; M74164; AAA62777.1; -; Genomic_DNA.
EMBL; M87049; AAA67643.1; -; Genomic_DNA.
EMBL; U00096; AAC76849.1; -; Genomic_DNA.
EMBL; AP009048; BAE77457.1; -; Genomic_DNA.
PIR; A39592; A39592.
RefSeq; NP_418288.1; NC_000913.3.
RefSeq; WP_000965936.1; NZ_LN832404.1.
ProteinModelPortal; P21177; -.
SMR; P21177; -.
BioGrid; 4263448; 158.
DIP; DIP-9560N; -.
IntAct; P21177; 7.
STRING; 316385.ECDH10B_4035; -.
PaxDb; P21177; -.
PRIDE; P21177; -.
EnsemblBacteria; AAC76849; AAC76849; b3846.
EnsemblBacteria; BAE77457; BAE77457; BAE77457.
GeneID; 948336; -.
KEGG; ecj:JW3822; -.
KEGG; eco:b3846; -.
PATRIC; fig|511145.12.peg.3960; -.
EchoBASE; EB0275; -.
EcoGene; EG10279; fadB.
eggNOG; ENOG4105DYT; Bacteria.
eggNOG; COG1024; LUCA.
eggNOG; COG1250; LUCA.
HOGENOM; HOG000261344; -.
InParanoid; P21177; -.
KO; K01825; -.
PhylomeDB; P21177; -.
BioCyc; EcoCyc:FADB-MONOMER; -.
BioCyc; MetaCyc:FADB-MONOMER; -.
UniPathway; UPA00659; -.
PRO; PR:P21177; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IDA:UniProtKB.
GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IDA:UniProtKB.
GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; IDA:EcoCyc.
Gene3D; 1.10.1040.10; -; 2.
HAMAP; MF_01621; FadB; 1.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR013328; 6PGD_dom2.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR001753; Crotonase_core_superfam.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR012799; FadB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00725; 3HCDH; 2.
Pfam; PF02737; 3HCDH_N; 1.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR02437; FadB; 1.
PROSITE; PS00067; 3HCDH; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Fatty acid metabolism;
Isomerase; Lipid degradation; Lipid metabolism; Lyase;
Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome.
CHAIN 1 729 Fatty acid oxidation complex subunit
alpha.
/FTId=PRO_0000109268.
NP_BIND 400 402 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
REGION 1 189 Enoyl-CoA hydratase/isomerase.
{ECO:0000255|HAMAP-Rule:MF_01621}.
REGION 311 729 3-hydroxyacyl-CoA dehydrogenase.
{ECO:0000255|HAMAP-Rule:MF_01621}.
ACT_SITE 450 450 For 3-hydroxyacyl-CoA dehydrogenase
activity. {ECO:0000255|HAMAP-
Rule:MF_01621,
ECO:0000269|PubMed:8454629,
ECO:0000269|PubMed:8755745}.
BINDING 296 296 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01621}.
BINDING 324 324 NAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01621,
ECO:0000305}.
BINDING 343 343 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
BINDING 407 407 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
BINDING 429 429 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
BINDING 453 453 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
BINDING 500 500 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01621}.
BINDING 660 660 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01621}.
SITE 119 119 Important for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_01621}.
SITE 139 139 Important for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_01621}.
MUTAGEN 116 116 G->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. {ECO:0000269|PubMed:8454629}.
MUTAGEN 322 322 G->A: 10-fold increase in KM for NADH.
{ECO:0000269|PubMed:8755745}.
MUTAGEN 450 450 H->A,Q: Almost complete loss of 3-
hydroxyacyl-CoA dehydrogenase activity.
{ECO:0000269|PubMed:8755745}.
CONFLICT 518 518 A -> R (in Ref. 1; AAA23750).
{ECO:0000305}.
CONFLICT 664 664 F -> L (in Ref. 3; CAB40809).
{ECO:0000305}.
CONFLICT 666 666 P -> A (in Ref. 3; CAB40809).
{ECO:0000305}.
SEQUENCE 729 AA; 79594 MW; 6F1055E402F6B129 CRC64;
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK
IGLVDGVVKA EKLVEGAKAV LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV
AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT LGMTEAAKLL
NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV VENPKVKKAV LAETEQKVRQ
DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP
KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY
GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA
RPVGDLKTA


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