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Database: UniProt
Entry: A0KEL1
LinkDB: A0KEL1
Original site: A0KEL1 
ID   FADB_AERHH              Reviewed;         715 AA.
AC   A0KEL1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   11-JUN-2014, entry version 61.
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=5.1.2.3;
DE              EC=5.3.3.8;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35;
GN   Name=fadB; OrderedLocusNames=AHA_0139;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / NCIB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Involved in the aerobic and anaerobic degradation of
CC       long-chain fatty acids via beta-oxidation cycle. Catalyzes the
CC       formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA.
CC       It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as
CC       substrate (By 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; CP000462; ABK38031.1; -; Genomic_DNA.
DR   RefSeq; YP_854676.1; NC_008570.1.
DR   ProteinModelPortal; A0KEL1; -.
DR   SMR; A0KEL1; 1-715.
DR   STRING; 380703.AHA_0139; -.
DR   EnsemblBacteria; ABK38031; ABK38031; AHA_0139.
DR   GeneID; 4490320; -.
DR   KEGG; aha:AHA_0139; -.
DR   PATRIC; 20777742; VBIAerHyd135212_0132.
DR   eggNOG; COG1250; -.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; AKGMVMQ; -.
DR   OrthoDB; EOG6M9F0M; -.
DR   BioCyc; AHYD380703:GH2M-139-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 2.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.226.10; -; 2.
DR   HAMAP; MF_01621; FadB; 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; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02437; FadB; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
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    715       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_1000069557.
FT   NP_BIND     401    403       NAD (By similarity).
FT   NP_BIND     428    430       NAD (By similarity).
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase (By
FT                                similarity).
FT   REGION      311    715       3-hydroxyacyl-CoA dehydrogenase (By
FT                                similarity).
FT   ACT_SITE    451    451       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
FT   BINDING     325    325       NAD; via amide nitrogen (By similarity).
FT   BINDING     344    344       NAD (By similarity).
FT   BINDING     408    408       NAD (By similarity).
FT   BINDING     454    454       NAD (By similarity).
FT   BINDING     501    501       Substrate (By similarity).
FT   BINDING     661    661       Substrate (By similarity).
FT   SITE        119    119       Important for catalytic activity (By
FT                                similarity).
FT   SITE        139    139       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   715 AA;  76523 MW;  41DF8B6A84E7751A CRC64;
     MIYQGETLTV SYLEDGIAEL RFDAPGSVNK LDRATLLSLS EAIAALQQER ELKGLILTSG
     KDAFIVGADI TEFLELFDLP QADLLGWLKK ANDIFSAIED LPVPTLSAIK GHALGGGCET
     ILSTDFRLAD TSAKIGLPET KLGIMPGFGG TVRLPRVIGA DNALEWITTG KDYRADDALK
     VGAIDAVVAP DALQSAAVQM IKDAVKGKLD WQGRRAAKKA PLRLSKLEAM MSFTTAAGMV
     AAVAGKHYPA PMTAVKTVEA AAGMSRDEAL AVEAQGFIKL AKTDVAKALV GIFLNDQHIK
     ALAKKAAKQA AKATSHAAVL GAGIMGGGIA YQSASKGIPA VMKDINEKAL ALGMGEATKL
     LNGQLEKGRI DGIKMGQVLS AITPTLSYDN VKHVDVVVEA VVENPKVKAA VLGEVEGIIG
     EDAVLASNTS TIPISLLAKE LKRPQNFCGM HFFNPVHRMP LVEIIRGEQT SDETINRVVA
     YAAAMGKSPV VVNDCPGFFV NRVLFPYFFG FNKLVADGAD FAAVDKVMEK EFGWPMGPAY
     LLDVVGIDTG HHAGDVMAQG FPARMSKEGR TAIDVMYEVN RFGQKNGKGF YAYEQDKKGK
     PKKVADAASY ELLAPIAKPK QDFDKDAIIA RMMIPMINEV VLCLEEGIVA TPAEADIALV
     YGLGFPPFRG GVFRYLDTIG LDRYVAMADQ YADLGPLYRV SDKLREMAAQ GKTFY
//
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