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Database: UniProt
Entry: A6TGM4
LinkDB: A6TGM4
Original site: A6TGM4 
ID   FADB_KLEP7              Reviewed;         729 AA.
AC   A6TGM4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   11-JUN-2014, 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=KPN78578_42840; ORFNames=KPN_04340;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH
OS   78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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 (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; CP000647; ABR79708.1; -; Genomic_DNA.
DR   RefSeq; YP_001337975.1; NC_009648.1.
DR   ProteinModelPortal; A6TGM4; -.
DR   SMR; A6TGM4; 1-714.
DR   STRING; 272620.KPN_04340; -.
DR   EnsemblBacteria; ABR79708; ABR79708; KPN_04340.
DR   GeneID; 5338716; -.
DR   KEGG; kpn:KPN_04340; -.
DR   PATRIC; 20463142; VBIKlePne13394_4398.
DR   eggNOG; COG1250; -.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; AKGMVMQ; -.
DR   OrthoDB; EOG6M9F0M; -.
DR   BioCyc; KPNE272620:GKDC-4377-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_1000069564.
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   ACT_SITE    450    450       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity (By 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;  79287 MW;  343B3315323919BB CRC64;
     MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG HALDVLEKQS DLKGLLLRSE
     KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTISAVN GYALGGGCEC
     VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIAAG KDVGADQALK
     IGLVDGVVAA EKLRDGALAI LRQAMNGDLD WKAKRQPKLE PLKLSKIEAA MSFTIAKGMV
     AQTAGKHYPA PITAVKTIEA AARLGREEAL VLENKSFVPL AHTNEARALV GIFLNDQYVK
     AKAKKLTKDV ETPKHAAVLG AGIMGGGIAY QSAWKGVPVV MKDISDKSLT LGMTEAAKLL
     NKQLERGKID GLKLAGVIST IQPTLEYSGF DRVDVVVEAV VENPKVKKAV LAETESKVRP
     DTVLASNTST IPISELASVL QRPENFCGMH FFNPVHRMPL VEVIRGEKTS DNTIAKVVAW
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL
     LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKDDSKGKP
     KKEEDAAVDS LLADVSQPKR DFSDEEIIAR MMIPMVNEVV RCLEEGIIAS PAEADMALVY
     GLGFPPFHGG AFRWLDTIGS AKYLDMAQQY QHLGPLYEVP AGLRDKARHN EAYYPQVEPA
     RPVGALKTA
//
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