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Database: UniProt
Entry: Q5YR32_NOCFA
LinkDB: Q5YR32_NOCFA
Original site: Q5YR32_NOCFA 
ID   Q5YR32_NOCFA            Unreviewed;       347 AA.
AC   Q5YR32;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   OrderedLocusNames=NFA_45080 {ECO:0000313|EMBL:BAD59359.1};
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD59359.1, ECO:0000313|Proteomes:UP000006820};
RN   [1] {ECO:0000313|EMBL:BAD59359.1, ECO:0000313|Proteomes:UP000006820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD59359.1,
RC   ECO:0000313|Proteomes:UP000006820};
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; AP006618; BAD59359.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YR32; -.
DR   STRING; 247156.NFA_45080; -.
DR   KEGG; nfa:NFA_45080; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_11_2_11; -.
DR   OMA; TTAYHGI; -.
DR   Proteomes; UP000006820; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05284; arabinose_DH_like; 1.
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   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006820};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          11..345
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   347 AA;  35735 MW;  61D416C853ECA3A6 CRC64;
     MMHALQLTGP GRLELRTVPV PGIGPTDVLL RVGAAGICHS DLYVLGLPFP LREEPLTLGH
     EIAGTVEAVG AEVDGPRPGD RGVVYLCWSC GVCRECIRGN ENVCLAAGRS AMPPCPGLGP
     DGGMAEYVRV PARAFVPIGE LDFLQAAPLA DAALTSYHAI AGARDHLLPG ATAVVIGIGG
     LGHVAVQILA ATTAVRIIAV DVSEDKLFLA AHYGADEGLV IGADTAARIL ERTGGRGAEA
     VFDFVGVDET ARLAVETVAP NGAYRMVGLG GGAPELTAGP AGGPGWPWGA SVRKSYGGTR
     SDLVESIALA QAGKLRVEVE PYELADGREA LDRLDRGLVR GRAVLVP
//
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