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Database: UniProt/TrEMBL
Entry: D5CFR0_ENTCC
LinkDB: D5CFR0_ENTCC
Original site: D5CFR0_ENTCC 
ID   D5CFR0_ENTCC            Unreviewed;       729 AA.
AC   D5CFR0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   29-OCT-2014, entry version 29.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01621};
GN   Name=fadB {ECO:0000256|HAMAP-Rule:MF_01621};
GN   OrderedLocusNames=ECL_04951 {ECO:0000313|EMBL:ADF64473.1};
OS   Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 /
OS   NBRC 13535 / NCDC 279-56).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=716541 {ECO:0000313|EMBL:ADF64473.1, ECO:0000313|Proteomes:UP000002363};
RN   [1] {ECO:0000313|EMBL:ADF64473.1, ECO:0000313|Proteomes:UP000002363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56
RC   {ECO:0000313|Proteomes:UP000002363};
RX   PubMed=20207761; DOI=10.1128/JB.00067-10;
RA   Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT   "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT   strain ATCC 13047.";
RL   J. Bacteriol. 192:2463-2464(2010).
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:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00079501}.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00079495}.
CC   -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC       CoA. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00079430}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00079416}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00079425}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00079424}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00079502}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01621}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|HAMAP-Rule:MF_01621}.
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DR   EMBL; CP001918; ADF64473.1; -; Genomic_DNA.
DR   RefSeq; YP_003615422.1; NC_014121.1.
DR   ProteinModelPortal; D5CFR0; -.
DR   EnsemblBacteria; ADF64473; ADF64473; ECL_04951.
DR   GeneID; 9127416; -.
DR   KEGG; enc:ECL_04951; -.
DR   PATRIC; 38460811; VBIEntClo148801_5086.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   BioCyc; ECLO716541:GH13-5011-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; -; 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; 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 {ECO:0000313|Proteomes:UP000002363};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00079512};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00079503};
KW   Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00079420};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00079510};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00079415};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00079419};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00079440};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00079460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002363}.
FT   NP_BIND     400    402       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   NP_BIND     427    429       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   REGION      311    729       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   ACT_SITE    450    450       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     296    296       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     324    324       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     343    343       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     407    407       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     453    453       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     500    500       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     660    660       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   SITE        119    119       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   SITE        139    139       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
SQ   SEQUENCE   729 AA;  79682 MW;  14FE1996320BA245 CRC64;
     MLYKGDTLYL NWLEDGIAEL VFDAPGSVNK LDTATVASLG QALDVLEKQT DLKGLLLRSN
     KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTLSAVN GYALGGGCEC
     VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGAEQAQK
     IGLVDGVVKP EKLIEGSLAI LRQAINGDLD WKAKRQPKLE PLKLSKIEAA MSFTIAKGMV
     MQTAGKHYPA PITAVKTIEA AARFGRDEAL KLENQSFVPL AHTNEARALV GIFLNDQFVK
     GKAKQLTKNV ETPKHAAVLG AGIMGGGIAY QSAWKGVPVV MKDISEKSLT LGMTEAAKLL
     NKQLERGKID GLKLSGVIST IQPVLEYTGF DRVDVVVEAV VENPKVKKAV LAETEEKVRP
     ETVLASNTST IPISELASVL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS DDTIAKVVAW
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL
     LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP
     KKEEDPAVDS LLAGVSQPKR DFTDDEIIAR MMIPMINEVV RCLEEGIIAS PAEADMALVY
     GLGFPPFHGG AFRWLDTLGS ARYLDMVQQY QHLGPLYDVP EGLRNKARHN ESYYPAVEPA
     RPVGELKTA
//
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