ID   FABI_AQUAE              Reviewed;         270 AA.
AC   O67505;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH];
DE            EC=1.3.1.9;
DE   AltName: Full=NADH-dependent enoyl-ACP reductase;
GN   Name=fabI; OrderedLocusNames=aq_1552;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG   Southeast collaboratory for structural genomics (SECSG);
RT   "Crystal structure of enoyl-[acyl-carrier-protein] reductase (NADH)
RT   from Aquifex aeolicus VF5.";
RL   Submitted (APR-2007) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NAD(+) = trans-
CC       2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. FabI subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE000657; AAC07465.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70434; G70434.
DR   RefSeq; NP_214070.1; -.
DR   PDB; 2P91; X-ray; 2.00 A; A/B/C/D=1-270.
DR   PDBsum; 2P91; -.
DR   GeneID; 1193128; -.
DR   GenomeReviews; AE000657_GR; aq_1552.
DR   KEGG; aae:aq_1552; -.
DR   NMPDR; fig|224324.1.peg.1085; -.
DR   HOGENOM; O67505; -.
DR   BioCyc; AAEO224324:AQ_1552-MON; -.
DR   BRENDA; 1.3.1.9; 189781.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NAD...; IEA:EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   PANTHER; PTHR19410:SF12; Enoyl-ACP_rdct; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Fatty acid biosynthesis;
KW   Lipid synthesis; NAD; Oxidoreductase.
FT   CHAIN         1    270       Enoyl-[acyl-carrier-protein] reductase
FT                                [NADH].
FT                                /FTId=PRO_0000054894.
FT   NP_BIND      10     36       NAD (By similarity).
FT   ACT_SITE    156    156       Proton acceptor (By similarity).
FT   TURN          3      6
FT   STRAND        8     11
FT   HELIX        20     30
FT   STRAND       34     41
FT   HELIX        42     44
FT   HELIX        45     54
FT   STRAND       60     62
FT   HELIX        68     81
FT   STRAND       87     90
FT   HELIX        97    100
FT   HELIX       104    106
FT   HELIX       109    119
FT   HELIX       121    130
FT   HELIX       131    134
FT   STRAND      140    145
FT   HELIX       147    149
FT   TURN        154    157
FT   HELIX       158    178
FT   TURN        179    181
FT   STRAND      183    189
FT   HELIX       203    213
FT   HELIX       222    232
FT   HELIX       235    237
FT   STRAND      244    248
FT   HELIX       251    253
SQ   SEQUENCE   270 AA;  29725 MW;  2ACD6C85EE16DC68 CRC64;
     MGLLEGKRAL ITGVANERSI AYGIAKSFHR EGAQLAFTYA TPKLEKRVRE IAKGFGSDLV
     VKCDVSLDED IKNLKKFLEE NWGSLDIIVH SIAYAPKEEF KGGVIDTSRE GFKIAMDISV
     YSLIALTREL LPLMEGRNGA IVTLSYYGAE KVVPHYNVMG IAKAALESTV RYLAYDIAKH
     GHRINAISAG PVKTLAAYSI TGFHLLMEHT TKVNPFGKPI TIEDVGDTAV FLCSDWARAI
     TGEVVHVDNG YHIMGVFGRE EEIKKEVYGD
//