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Database: UniProt
Entry: R7XYF3_9ACTN
LinkDB: R7XYF3_9ACTN
Original site: R7XYF3_9ACTN 
ID   R7XYF3_9ACTN            Unreviewed;       382 AA.
AC   R7XYF3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EON24040.1};
GN   ORFNames=CF8_1958 {ECO:0000313|EMBL:EON24040.1};
OS   Nocardioides sp. CF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=110319 {ECO:0000313|EMBL:EON24040.1, ECO:0000313|Proteomes:UP000015971};
RN   [1] {ECO:0000313|EMBL:EON24040.1, ECO:0000313|Proteomes:UP000015971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF8 {ECO:0000313|EMBL:EON24040.1,
RC   ECO:0000313|Proteomes:UP000015971};
RX   PubMed=23833136;
RA   Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT   "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT   of Its Metabolic Capabilities.";
RL   Genome Announc. 1:e00439-e00439(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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:EON24040.1}.
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DR   EMBL; ASEP01000064; EON24040.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7XYF3; -.
DR   STRING; 110319.CF8_1958; -.
DR   PATRIC; fig|110319.3.peg.2573; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_11; -.
DR   Proteomes; UP000015971; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015971};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          14..130
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          178..246
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   382 AA;  41040 MW;  84535E5E7247ECFA CRC64;
     MQVREVPDPE IQEPTDVVID VTSTGLCGSD LHLYDPLTPF MTPGDIVGHE AMGVVREVGA
     AVTRLEVGDR VVVPFNISCG ACWMCERGLF SQCETTQNRE HGTGASLFGY SKLYGQVPGG
     QAEALRVPFG DTLPIKVSHG PVDDRFVFLS DVLPTAWQAV EYADADPDAT LLVIGAGPIG
     DMASRIAIHR GLRVISVDSV PERLGRAHAI GAEPIDMSEV EDVPARVREL TDGRGADAVI
     DAVGMEAHGS PVAETAQKAL GLLPKKVQEK VMLTAGSDRL AALHTAIDAV RRGGTISISG
     VYGGATDPLP MFQLFDKQVQ LRMGQANVRR WSDDILSLLE EDQDHLGVED FATHHLPLSD
     APEAYRSFRD KEGGMVKVVF TP
//
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