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Database: UniProt
Entry: A0A261DB77_9RICK
LinkDB: A0A261DB77_9RICK
Original site: A0A261DB77_9RICK 
ID   A0A261DB77_9RICK        Unreviewed;       276 AA.
AC   A0A261DB77;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=3-oxoacyl-ACP reductase {ECO:0000313|EMBL:OZG31775.1};
GN   ORFNames=RiCNE_08350 {ECO:0000313|EMBL:OZG31775.1};
OS   Rickettsia endosymbiont of Culicoides newsteadi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=1961830 {ECO:0000313|EMBL:OZG31775.1, ECO:0000313|Proteomes:UP000216097};
RN   [1] {ECO:0000313|EMBL:OZG31775.1, ECO:0000313|Proteomes:UP000216097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RiCNE {ECO:0000313|EMBL:OZG31775.1,
RC   ECO:0000313|Proteomes:UP000216097};
RX   PubMed=28805302;
RA   Pilgrim J., Ander M., Garros C., Baylis M., Hurst G.D.D., Siozios S.;
RT   "Torix group Rickettsia are widespread in Culicoides biting midges
RT   (Diptera: Ceratopogonidae), reach high frequency and carry unique genomic
RT   features.";
RL   Environ. Microbiol. 19:4238-4255(2017).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZG31775.1}.
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DR   EMBL; MWZE01000044; OZG31775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261DB77; -.
DR   OrthoDB; 9810734at2; -.
DR   Proteomes; UP000216097; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43477; DIHYDROANTICAPSIN 7-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43477:SF1; DIHYDROANTICAPSIN 7-DEHYDROGENASE; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216097};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..276
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012175786"
SQ   SEQUENCE   276 AA;  30413 MW;  75A8179D0905384F CRC64;
     MRIFITIFTL IFCFSTYTIA DSSSSAVLVT GSTGAFGEAI CLSLASEGYN LLITGRNEKK
     LKSLKNKLQT KYPSTKVETL KIDFSDFKTI KAAANKTDGV SLKAVVLIGP RPSLRKNGFP
     STQEWSEEFQ KTFIAPLEVV RIFGEKIENN GSIVIISGSS SKNYLPNYQN TNVLRLAWIG
     EVKNLVQFFA VRKIRVNAVS PGIILTEYHK KRIEEKAKLN NTTFQAQLSL DTAAIPLRSY
     GHTDDVANLI SFLISDKSVH LNGSNIVLDG GESTAY
//
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