(data stored in ACNUC7421 zone)

SWISSPROT: FADB_SHESH

ID   FADB_SHESH              Reviewed;         716 AA.
AC   A8FP63;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 74.
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=Ssed_0023;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000821; ABV34636.1; -; Genomic_DNA.
DR   RefSeq; WP_012004162.1; NC_009831.1.
DR   ProteinModelPortal; A8FP63; -.
DR   SMR; A8FP63; -.
DR   STRING; 425104.Ssed_0023; -.
DR   EnsemblBacteria; ABV34636; ABV34636; Ssed_0023.
DR   KEGG; sse:Ssed_0023; -.
DR   eggNOG; ENOG4108EIM; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; DYKAKRQ; -.
DR   OrthoDB; POG091H00UW; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002015; Chromosome.
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-EC.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 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; IPR013328; 6PGD_dom_2.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
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;
DR   PRODOM; A8FP63.
DR   SWISS-2DPAGE; A8FP63.
KW   Complete proteome; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    716       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_1000088085.
FT   NP_BIND     400    402       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    716       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     429    429       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   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   716 AA;  77021 MW;  AD91C405CB10CF8A CRC64;
     MIYQSPTIQV ELLEDNIARL CFNASGSVNK LDRETINSLD AALDAIQQDS HIQALVLTSA
     KGAFIVGADI TEFLGLFAQE DSVLLPWIAE ANVVFNKLED LPFPTISAIN GFALGGGFET
     VLATDFRIAD TTAKIGLPET KLGLIPGFGG TVRLPRLIGT DNALEWITSG KDQRPEAALK
     VGAIDAVVAP ENLQASAIKM LKDALAEKLD WQSRRARKQA ALTLPKLEAM MSFATAKGMV
     FKIAGKHYPA PMAAISVIEQ AARCGRADAL KVEHQAFVKL AKTDVAQALI GIFLNDQLVK
     GKAKKAGKLA KNIDTAAVLG AGIMGGGIAY QSASKGTPII MKDIAQPALE LGLGEASKLL
     AAQIKRGRST PQKMAKVLNN ITATLDYTPV KDVDVVVEAV VEHPKVKSMV LAEVEQNVSD
     DAIITSNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEVIRGENSS EETIASVVAY
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLADGADF AAIDKVMEKQ FGWPMGPAYL
     LDVVGIDTGH HAQAVMAEGF PDRMGKNGKD AIDIMFEAER FGQKNSKGFY AYSVDRRGKP
     KKDVDPTSYE LLGAEFGELK AFESEDIIAR TMIPMIIETV RCLEEGIIAT PAEADMGLVF
     GLGFPPFRGG VFRYIDTMGV ANFVALADKY AHLGGLYQVT DAMRELAANN GSYYQS
//

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