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 29-MAY-2013, entry version 53.
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: Catalyzes the formation of a hydroxyacyl-CoA by addition
CC of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase
CC and 3-hydroxyacyl-CoA dehydrogenase activities (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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; NDQFVKG; -.
DR ProtClustDB; PRK11730; -.
DR BioCyc; AHYD380703:GH2M-139-MONOMER; -.
DR UniPathway; UPA00659; -.
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:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 2.
DR Gene3D; 3.40.50.720; -; 1.
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; 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; 6DGDH_C_like; 2.
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 1 715 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 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
//
