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Database: UniProt
Entry: A4SH85_AERS4
LinkDB: A4SH85_AERS4
Original site: A4SH85_AERS4 
ID   A4SH85_AERS4            Unreviewed;       435 AA.
AC   A4SH85;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   20-JAN-2016, entry version 57.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|HAMAP-Rule:MF_01838};
DE            Short=ENR {ECO:0000256|HAMAP-Rule:MF_01838};
DE            EC=1.3.1.9 {ECO:0000256|HAMAP-Rule:MF_01838};
GN   Name=fabV {ECO:0000256|HAMAP-Rule:MF_01838};
GN   OrderedLocusNames=ASA_0047 {ECO:0000313|EMBL:ABO88257.1};
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO88257.1, ECO:0000313|Proteomes:UP000000225};
RN   [1] {ECO:0000313|Proteomes:UP000000225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A.,
RA   Kimball J., Munholland J., Murphy C., Sarty D., Williams J.,
RA   Nash J.H., Johnson S.C., Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights
RT   into the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
CC   -!- FUNCTION: Involved in the final reduction of the elongation cycle
CC       of fatty acid synthesis (FAS II). Catalyzes the reduction of a
CC       carbon-carbon double bond in an enoyl moiety that is covalently
CC       linked to an acyl carrier protein (ACP). {ECO:0000256|HAMAP-
CC       Rule:MF_01838}.
CC   -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a
CC       trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01838}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01838}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01838,
CC       ECO:0000256|SAAS:SAAS00341357}.
CC   -!- SIMILARITY: Belongs to the TER reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01838}.
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DR   EMBL; CP000644; ABO88257.1; -; Genomic_DNA.
DR   STRING; 382245.ASA_0047; -.
DR   EnsemblBacteria; ABO88257; ABO88257; ASA_0047.
DR   KEGG; asa:ASA_0047; -.
DR   PATRIC; 20786380; VBIAerSal2987_0060.
DR   eggNOG; COG3007; LUCA.
DR   eggNOG; ENOG4105RKW; Bacteria.
DR   HOGENOM; HOG000269390; -.
DR   KO; K00209; -.
DR   OMA; SAGWYNN; -.
DR   OrthoDB; EOG64N9T6; -.
DR   BioCyc; ASAL382245:GJJN-47-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000225; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.720; -; 2.
DR   HAMAP; MF_01838; FabV_reductase; 1.
DR   InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR   InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR   Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR   Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR   Pfam; PF12241; Enoyl_reductase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000225};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308828};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308833};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308838};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00308827};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00308822};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01838,
KW   ECO:0000256|SAAS:SAAS00008249}.
FT   DOMAIN      123    355       Enoyl_reductase. {ECO:0000259|Pfam:
FT                                PF12241}.
FT   DOMAIN      363    425       Eno-Rase_FAD_bd. {ECO:0000259|Pfam:
FT                                PF07055}.
FT   NP_BIND      87     92       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     113    114       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     150    151       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     178    179       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   NP_BIND     311    313       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   ACT_SITE    273    273       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     263    263       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01838}.
FT   BINDING     282    282       NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
FT   SITE        114    114       Plays an important role in discriminating
FT                                NADH against NADPH. {ECO:0000256|HAMAP-
FT                                Rule:MF_01838}.
SQ   SEQUENCE   435 AA;  46723 MW;  590DF2DE9D5B5382 CRC64;
     MGSLALPLVF LPPYCPYPAR HQGNPQLLGY AVASSFGDPV MIIHPQIQGC VARNCHPIGC
     RAAVLQQISS VKAAGSFNGP KRVLVLGASS GFGLASRIAL TFGAGADTVG VSFERGPSDK
     GLGSAGWYNN IWFRQAAEQE GRVAVNLIGD AFSDAMRQQA IDSIRQQLGQ VDLVIYSLAS
     GIRVLPDGRQ VRSALKTTGQ PFSGWGLDLE QDKLVQQSLA PATPEEIRDT VTVMGGEDWQ
     LWMLALQQAD CLAPGARTVA YSYIGPESTY PLYRDGTIGY AKEHLHATAE AINLQLAELG
     GHAWVSVCKA LVTKASAYIP VLPVYLGLLM GVMKERGVHE GCIEQMQRLF ASKMYGPQGV
     VADGNRLIRM DDHELDPAIQ AAVSTLWSKV TPDNFHTLGD FAGLRQDFMQ LNGFELPGVD
     YGAPVDVASL TELVP
//
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