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Database: UniProt
Entry: G9XI42_DESHA
LinkDB: G9XI42_DESHA
Original site: G9XI42_DESHA 
ID   G9XI42_DESHA            Unreviewed;       289 AA.
AC   G9XI42;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Oxidoreductase, short chain dehydrogenase/reductase family protein {ECO:0000313|EMBL:EHL08686.1};
GN   ORFNames=HMPREF0322_00618 {ECO:0000313|EMBL:EHL08686.1};
OS   Desulfitobacterium hafniense DP7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=537010 {ECO:0000313|EMBL:EHL08686.1, ECO:0000313|Proteomes:UP000004416};
RN   [1] {ECO:0000313|EMBL:EHL08686.1, ECO:0000313|Proteomes:UP000004416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP7 {ECO:0000313|EMBL:EHL08686.1,
RC   ECO:0000313|Proteomes:UP000004416};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHL08686.1}.
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DR   EMBL; AFZX01000016; EHL08686.1; -; Genomic_DNA.
DR   RefSeq; WP_005808923.1; NZ_JH414447.1.
DR   AlphaFoldDB; G9XI42; -.
DR   PATRIC; fig|537010.4.peg.572; -.
DR   HOGENOM; CLU_010194_4_1_9; -.
DR   Proteomes; UP000004416; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05355; SDR_c1; 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; PTHR48107:SF16; NADPH-DEPENDENT ALDEHYDE REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48107; NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF13561; adh_short_C2; 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   Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   289 AA;  30857 MW;  5CE934381FE5D787 CRC64;
     MSETKIPQPT FPAQHQDKQP GLETLMNPSP IFEDLNYRPS GKLQGKVALI SGGDSGIGKA
     VAILYAKEGA DIAIVYLDEQ VDAQATKARI EQLGRRCLLI PGDIGEENFS NQAVQKTLDT
     LGGLDILVNN AAEQHPQNSL LDITAQQIEQ TFRTNIFGML YLTKAALPHL RYGSVIINTA
     SITAYKGDAK LIDYSASKGA VVAFTRSLSE SLIKQGIRVN GVAPGPIWTP LIPASFDANE
     VSTFGSTTPM QRAGQPVELA PAYLFLACEG SAYMSGQIVH VNGGTIVNG
//
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