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Database: UniProt
Entry: C3JNC8_RHOER
LinkDB: C3JNC8_RHOER
Original site: C3JNC8_RHOER 
ID   C3JNC8_RHOER            Unreviewed;       362 AA.
AC   C3JNC8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=Mycothiol-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:EEN87392.1};
DE            EC=1.1.1.306 {ECO:0000313|EMBL:EEN87392.1};
GN   ORFNames=RHOER0001_2092 {ECO:0000313|EMBL:EEN87392.1};
OS   Rhodococcus erythropolis SK121.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN87392.1, ECO:0000313|Proteomes:UP000005836};
RN   [1] {ECO:0000313|EMBL:EEN87392.1, ECO:0000313|Proteomes:UP000005836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK121 {ECO:0000313|EMBL:EEN87392.1,
RC   ECO:0000313|Proteomes:UP000005836};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, 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:EEN87392.1}.
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DR   EMBL; ACNO01000046; EEN87392.1; -; Genomic_DNA.
DR   RefSeq; WP_003943254.1; NZ_ACNO01000046.1.
DR   AlphaFoldDB; C3JNC8; -.
DR   Proteomes; UP000005836; Unassembled WGS sequence.
DR   GO; GO:0050607; F:mycothiol-dependent formaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08279; Zn_ADH_class_III; 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; IPR017816; MycoS_dep_FDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR03451; mycoS_dep_FDH; 1.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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   ECO:0000313|EMBL:EEN87392.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          14..362
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  38373 MW;  14FEC45409A2C892 CRC64;
     MPQQVRGVIA RSKGAPVEIV PITIPDPGAN EVVVAIAACG VCHTDLTYRD GGINDEYPFL
     LGHEASGIVE SVGPGVTHVE VGDFVVLNWR AVCGQCRACK RGRPQYCFDT FNAEQKMTLE
     DGTELTPALG IGAFADKTLV HEGQCTKVDA SADPAVVGLL GCGVMAGMGA AMNTGNVGRG
     DSVAVIGCGG VGDAAIMGSR LAGANTIIAI DRDPRKLEWA TELGATHTIN ATEVDDVVEA
     VQELTGGFGA DVVVDAVGRP ETWKQAFYAR DLAGTVVLVG VPTPDMQLEM PLVDFFSRGG
     ALKSSWYGDC LPERDFPVLV DLYQQGRLPL EKFVSERIKL DEVEKAFETM HRGEVLRSVV
     VL
//
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