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Database: UniProt
Entry: B6BHF5_SULGG
LinkDB: B6BHF5_SULGG
Original site: B6BHF5_SULGG 
ID   B6BHF5_SULGG            Unreviewed;       270 AA.
AC   B6BHF5; H1FT32;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=NAD(P)-dependent oxidoreductase, short chain dehydrogenase/reductase family {ECO:0000313|EMBL:EHP29951.1};
GN   ORFNames=SMGD1_1427 {ECO:0000313|EMBL:EHP29951.1};
OS   Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP29951.1, ECO:0000313|Proteomes:UP000006431};
RN   [1] {ECO:0000313|EMBL:EHP29951.1, ECO:0000313|Proteomes:UP000006431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD1 {ECO:0000313|EMBL:EHP29951.1,
RC   ECO:0000313|Proteomes:UP000006431};
RX   PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA   Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA   Labrenz M., Jurgens K.;
RT   "Genome and physiology of a model Epsilonproteobacterium responsible for
RT   sulfide detoxification in marine oxygen depletion zones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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:EHP29951.1}.
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DR   EMBL; AFRZ01000001; EHP29951.1; -; Genomic_DNA.
DR   RefSeq; WP_008336324.1; NZ_DS995286.1.
DR   AlphaFoldDB; B6BHF5; -.
DR   STRING; 929558.SMGD1_1427; -.
DR   PATRIC; fig|929558.5.peg.1418; -.
DR   eggNOG; COG4221; Bacteria.
DR   HOGENOM; CLU_010194_2_9_7; -.
DR   OrthoDB; 5354363at2; -.
DR   Proteomes; UP000006431; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05374; 17beta-HSD-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43976:SF16; NAD(P)-BINDING PROTEIN; 1.
DR   PANTHER; PTHR43976; SHORT CHAIN DEHYDROGENASE; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006431}.
SQ   SEQUENCE   270 AA;  29296 MW;  4942BBB5F6D50ADD CRC64;
     MSKVVLITGA SSGMGKLTAE FLSDNGYTVY AGTRDADAIN FDSSLKSIYI DVTKSASIDH
     AVEMIMHKEG KIDVLVNNAG YGLLATVEDG TDEEMFNQFD VNVFGLLKVT RAVLPHMRKA
     KSGVIINISS FLGKMGLPLL AHYNASKYAV EGIVDSLRFE TLPFNIRVHS IQSGLFGTNF
     VKNGLVANAQ TTAEDSPYKE LVSHFVPIVA KAINEGPSPQ PIADAVKKII EDENSNIFIP
     VGGEAETFVP MRKELSDEAF ELKVKETFGL
//
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