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Database: UniProt
Entry: A0A1Q7WCQ8_9ACTN
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Original site: A0A1Q7WCQ8_9ACTN 
ID   A0A1Q7WCQ8_9ACTN        Unreviewed;       279 AA.
AC   A0A1Q7WCQ8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OLE28565.1};
GN   ORFNames=AUG49_02020 {ECO:0000313|EMBL:OLE28565.1};
OS   Catenulispora sp. 13_1_20CM_3_70_7.
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE28565.1, ECO:0000313|Proteomes:UP000186605};
RN   [1] {ECO:0000313|EMBL:OLE28565.1, ECO:0000313|Proteomes:UP000186605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLE28565.1}.
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DR   EMBL; MNJN01000034; OLE28565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7WCQ8; -.
DR   Proteomes; UP000186605; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05233; 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; IPR002347; SDR_fam.
DR   PANTHER; PTHR43391:SF14; DEHYDROGENASE_REDUCTASE SDR FAMILY PROTEIN 7-LIKE; 1.
DR   PANTHER; PTHR43391; RETINOL DEHYDROGENASE-RELATED; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   279 AA;  29859 MW;  BD893A4C04C0BE6E CRC64;
     MLTDLPGKTA VVTGAAGGIG LAMAKLFAAE GMNVVLADVE EPALAKAVEA VMRHRAGEAE
     AIGHVTDVSL PESVQALADR AFATFPSVDV LCNNAGVGSG AEGPMWQHER SDWQWAFAVN
     VWGVFHGVQA FLPRMIAQDT PGHVVNTSSP DGGIAPLPTA SVYAVTKAAI VTLTEALYAQ
     LKQADAKIGA SVLFPGPHMV RTGLWESYRN RPERFAKSRP RQTPYPEPEE VAAHALEGIR
     TGTFWILPKG GGSDDMIRRR SQSMLERSNP GYLETFILD
//
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