ID   FADB_ENTS8              Reviewed;         729 AA.
AC   A7MQP0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 14.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha;
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase;
DE              EC=4.2.1.17;
DE              EC=5.3.3.8;
DE              EC=5.1.2.3;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35;
GN   Name=fadB; OrderedLocusNames=ESA_03714;
OS   Enterobacter sakazakii (strain ATCC BAA-894).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of an hydroxyacyl-CoA by
CC       addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA
CC       epimerase and 3-hydroxyacyl-CoA dehydrogenase activities (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA.
CC   -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC       CoA.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (fadB) and two beta
CC       chains (fadA) (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family.
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DR   EMBL; CP000783; ABU78911.1; -; Genomic_DNA.
DR   RefSeq; YP_001439747.1; -.
DR   GeneID; 5552271; -.
DR   GenomeReviews; CP000783_GR; ESA_03714.
DR   KEGG; esa:ESA_03714; -.
DR   OMA; A7MQP0; RIDEIAM.
DR   GO; GO:0016507; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:HAMAP.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:HAMAP.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:HAMAP.
DR   GO; GO:0009062; P:fatty acid catabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01621; -; 1.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR001753; Crotonase_core.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   TIGRFAMs; TIGR02437; FadB; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    729       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_1000069563.
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase (By
FT                                similarity).
FT   REGION      311    729       3-hydroxyacyl-CoA dehydrogenase (By
FT                                similarity).
SQ   SEQUENCE   729 AA;  79184 MW;  94EAC780BCF49DC1 CRC64;
     MLYKGDTLYL NWLEDGIAEL VFDAPGSVNK LDTATVASLG HALDVLEKQH DLKALLLRSE
     KAAFIVGADI TEFLSLFQVP AEQLSQWLHF ANSVFNRLED LPVPTLCAIN GYALGGGCEC
     VLATDFRLAT PDARIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIAAG KDITADAALK
     VGLVDAVVKP EKLIEGALRM LRQAIDGELD WQARRQPKLE PLRLSKIEAT MSFTIAKGMV
     MQTAGKHYPA PMTAVKTIEA AAGLGRDEAL ALENKSFVPL ARSSEARALV GIFLNDQYVK
     GLAKKLTKET ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINEKSLT LGISEASKLL
     NKQLERGKID GLKLAGVIAT IHPTLDYAGF ERADVVVEAV VENPKVKKAV LAETEEKVRP
     DTVIASNTST IPISELASVL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS DATIAKVVSW
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RQIDKVMEKQ FGWPMGPAYL
     LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDAGR FGQKNGKGFY AYQEDSKGKP
     RKVPDDAVDS LLAEVSQPKR AFSDEEIVAR MMIPMVNEVV RCLEEGIIAS PAEADMALVY
     GLGFPPFHGG AFRWLDTQGS AKYLDMAQHY QHLGPLYEAP AGLRDKASHN APYYPQVEPA
     QPVGELQTA
//