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Database: UniProt/TrEMBL
Entry: A7HZ99_PARL1
LinkDB: A7HZ99_PARL1
Original site: A7HZ99_PARL1 
ID   A7HZ99_PARL1            Unreviewed;       288 AA.
AC   A7HZ99;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   25-APR-2018, entry version 69.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094};
DE            EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094};
GN   OrderedLocusNames=Plav_3634 {ECO:0000313|EMBL:ABS65232.1};
OS   Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhodobiaceae; Parvibaculum.
OX   NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS65232.1, ECO:0000313|Proteomes:UP000006377};
RN   [1] {ECO:0000313|EMBL:ABS65232.1, ECO:0000313|Proteomes:UP000006377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC   {ECO:0000313|Proteomes:UP000006377};
RX   PubMed=22675581; DOI=10.4056/sigs.2215005;
RA   Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA   Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T.,
RA   Goodwin L., Pennacchio L., Nolan M., Cook A.M., Kjelleberg S.,
RA   Thomas T.;
RT   "Complete genome sequence of Parvibaculum lavamentivorans type strain
RT   (DS-1(T)).";
RL   Stand. Genomic Sci. 5:298-310(2011).
CC   -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a
CC       trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
CC       {ECO:0000256|PIRNR:PIRNR000094}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. FabI subfamily. {ECO:0000256|PIRNR:PIRNR000094}.
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DR   EMBL; CP000774; ABS65232.1; -; Genomic_DNA.
DR   ProteinModelPortal; A7HZ99; -.
DR   STRING; 402881.Plav_3634; -.
DR   EnsemblBacteria; ABS65232; ABS65232; Plav_3634.
DR   KEGG; pla:Plav_3634; -.
DR   eggNOG; ENOG4105CSJ; Bacteria.
DR   eggNOG; COG0623; LUCA.
DR   KO; K00208; -.
DR   OMA; NHSIAWG; -.
DR   OrthoDB; POG091H06HU; -.
DR   Proteomes; UP000006377; Chromosome.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43159:SF2; PTHR43159:SF2; 1.
DR   PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006377};
KW   Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW   Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000094};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000094};
KW   NAD {ECO:0000256|PIRNR:PIRNR000094, ECO:0000256|PIRSR:PIRSR000094-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006377}.
FT   NP_BIND      36     37       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   NP_BIND      81     82       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   ACT_SITE    162    162       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000094-1}.
FT   ACT_SITE    172    172       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000094-1}.
FT   BINDING      30     30       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING      57     57       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING     109    109       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000094-3}.
FT   BINDING     179    179       NAD. {ECO:0000256|PIRSR:PIRSR000094-3}.
SQ   SEQUENCE   288 AA;  30562 MW;  E22AF3A1B610481F CRC64;
     MHGSGGEKAG EGALVLTGPL MKGRRGLIMG VANDHSIAWG IARALAAHGA ELAFTYQGES
     FGRRVKPLAA SAGSKLLLPC DVTDPASLDA AFETLEKEWG VLDFVVHAIA HSDKNELKGR
     YVDTTRENFL RTMDISCFSF TDVARRAAKL MTRGGSMVTL TYGGSTRVMP NYNVMGVAKA
     ALEASVRYLA VDLGRHGIRV NAISAGPMRT LAGSAVGDAR FVFKWNKTHA PIKESIELDH
     VGGAGLYLLS DLSARVSGEV HHVDGGYNII GLPRAEELKA SQPEGGEG
//
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