ID FADB_SHEFN Reviewed; 716 AA.
AC Q08A39;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 01-MAY-2013, entry version 54.
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=Sfri_0013;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI69876.1; -; Genomic_DNA.
DR RefSeq; YP_748714.1; NC_008345.1.
DR ProteinModelPortal; Q08A39; -.
DR SMR; Q08A39; 1-714.
DR STRING; 318167.Sfri_0013; -.
DR EnsemblBacteria; ABI69876; ABI69876; Sfri_0013.
DR GeneID; 4277696; -.
DR KEGG; sfr:Sfri_0013; -.
DR PATRIC; 23493733; VBISheFri14343_0013.
DR eggNOG; COG1250; -.
DR HOGENOM; HOG000261344; -.
DR KO; K01825; -.
DR OMA; NDQFVKG; -.
DR ProtClustDB; PRK11730; -.
DR BioCyc; SFRI318167:GIXS-13-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; 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.
DR SUPFAM; SSF48179; 6DGDH_C_like; 2.
DR TIGRFAMs; TIGR02437; FadB; 1.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; FALSE_NEG.
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 1 716 Fatty acid oxidation complex subunit
FT alpha.
FT /FTId=PRO_1000069575.
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 311 716 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 716 AA; 76897 MW; 28434AB7ABC1166C CRC64;
MIYQSPTIQV ELLEDNIAKL CFNAQGSVNK FDRETIASLD AALDSIKQNT NIKALLLTSA
KSTFIVGADI TEFLTLFQQD DATLLAWVEQ ANAVFNKLED LPFPTASAIN GFALGGGCET
ILATDLRVAD TNARIGLPET KLGLIPGFGG TVRLPRVIGA DNALEWITTA KDQRPEDALK
VGAIDAVVAP ENLEAAAIQM LHDALNGSLD WQARRTKKQS PLQLPKLEAM MSFATAKGMV
FSVAGKHYPA PMAAVNVVEQ AAGLDRDGAL KVEALAFIKL AKTDVAQALI GIFLNDQFVK
GKAKKAGKLA KDVNQAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALE LGLNEAAKIL
TTQVARGRST PEKMAKVLNN ITPSLDYAAI KNSDIVVEAV VEHPKVKATV LAEVEGYVSE
DAIIASNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEIIRGEHSS EETIATVVAY
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLAEGADF AAVDKVMEKQ FGWPMGPAYL
LDVVGLDTGH HAQAVMAEGF PDRMGKNGKD AIDIMFENKR LGQKNTKGFY AYSVDRRGKP
KKDIDPTSYE LLSAEFGELK AFESDDIIAR CMIPMIIETV RCLEEGIIAS PAEGDMGLVY
GIGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT DAMRALAANN GSYYQA
//
