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Database: UniProt
Entry: B7UNH4
LinkDB: B7UNH4
Original site: B7UNH4 
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-OCT-2014, entry version 46.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01621};
DE              EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621};
DE              EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621};
DE              EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621};
DE              EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621};
GN   Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621};
GN   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: 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. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC       CoA. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01621}.
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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; NPIVVND; -.
DR   OrthoDB; EOG6M9F0M; -.
DR   BioCyc; ECOL574521:GJAO-4312-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; 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; SSF48179; 2.
DR   SUPFAM; SSF52096; SSF52096; 1.
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. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   NP_BIND     427    429       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   REGION      311    729       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   ACT_SITE    450    450       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     296    296       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     324    324       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     343    343       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     407    407       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     453    453       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     500    500       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     660    660       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   SITE        119    119       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   SITE        139    139       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
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
//
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