ID FADB_ECO27 Reviewed; 729 AA.
AC B7UNH4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 36.
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=E2348C_4158;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/JB.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
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.
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DR EMBL; FM180568; CAS11706.1; -; Genomic_DNA.
DR RefSeq; YP_002331616.1; NC_011601.1.
DR ProteinModelPortal; B7UNH4; -.
DR SMR; B7UNH4; 1-715.
DR STRING; 574521.E2348C_4158; -.
DR EnsemblBacteria; CAS11706; CAS11706; E2348C_4158.
DR GeneID; 7062071; -.
DR KEGG; ecg:E2348C_4158; -.
DR PATRIC; 18347533; VBIEscCol90278_4241.
DR eggNOG; COG1250; -.
DR KO; K01825; -.
DR OMA; NDQFVKG; -.
DR ProtClustDB; PRK11730; -.
DR BioCyc; ECOL574521:GJAO-4312-MONOMER; -.
DR UniPathway; UPA00659; -.
DR GO; GO:0016507; C:mitochondrial 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:0000166; F:nucleotide binding; IEA:InterPro.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
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; 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 1 729 Fatty acid oxidation complex subunit
FT alpha.
FT /FTId=PRO_1000186032.
FT NP_BIND 400 402 NAD (By similarity).
FT NP_BIND 427 429 NAD (By similarity).
FT REGION 1 189 Enoyl-CoA hydratase/isomerase (By
FT similarity).
FT REGION 311 729 3-hydroxyacyl-CoA dehydrogenase (By
FT similarity).
FT BINDING 296 296 Substrate (By similarity).
FT BINDING 324 324 NAD; via amide nitrogen (By similarity).
FT BINDING 343 343 NAD (By similarity).
FT BINDING 407 407 NAD (By similarity).
FT BINDING 453 453 NAD (By similarity).
FT BINDING 500 500 Substrate (By similarity).
FT BINDING 660 660 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 729 AA; 79609 MW; 3F038E5A7A99E50B CRC64;
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK
IGLVDGVVKA EKLVEGAMAI LRQAINGDLD WKAKRQPKLE PLKLSKIEAA MSFTIAKGMV
AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
GKAKKLTKDV ETPKQAAVLG TGIMGGGIAY QSAWKDVPVV MKDINDKSLT LGMTEAAKLL
NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRP
DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFNANR FGQKNGLGFW RYKEDSKGKP
KKEEDAAVDD LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY
GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA
RPVGDLKTA
//
