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Database: UniProt
Entry: A0A1N7INF8_9CORY
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Original site: A0A1N7INF8_9CORY 
ID   A0A1N7INF8_9CORY        Unreviewed;       371 AA.
AC   A0A1N7INF8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=S-(Hydroxymethyl)mycothiol dehydrogenase {ECO:0000313|EMBL:SIS38609.1};
GN   ORFNames=SAMN05444817_101112 {ECO:0000313|EMBL:SIS38609.1};
OS   Corynebacterium appendicis CIP 107643.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1161099 {ECO:0000313|EMBL:SIS38609.1, ECO:0000313|Proteomes:UP000186292};
RN   [1] {ECO:0000313|Proteomes:UP000186292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44531 {ECO:0000313|Proteomes:UP000186292};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) 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|RuleBase:RU361277}.
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DR   EMBL; FTOF01000001; SIS38609.1; -; Genomic_DNA.
DR   RefSeq; WP_076598116.1; NZ_FTOF01000001.1.
DR   AlphaFoldDB; A0A1N7INF8; -.
DR   STRING; 1161099.SAMN05444817_101112; -.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000186292; Unassembled WGS sequence.
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; 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   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          21..369
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   371 AA;  39125 MW;  4C1464FD39CDC745 CRC64;
     MTNNEQQTEQ TVKGVIAREK GADVEIADIV IPAPGPNDVV VKVQATGVCH TDLAYRDGDI
     EDAYPFLLGH ETAGVVETVG ADVTHVEPGD FVVLNWRAVC GECRACRKGD TKNCFNTHNA
     SKGMTLTDGT ELTPALGIGS FAEKTLVHEM QCTKVNPDED PAAAGLLGCG IMAGLGAAVN
     TGEVQRGETV AVFGLGGVGL AAVAGAALAG AVKVIAVDVD KRKCDAAAKF GATDAICSKD
     MSEGEVIDRV RELTGGFGPD VTIDAVGIQP TWRQAFYSRD LAGRMVMVGV PNQTDHVDIP
     AIDLYARGGS IKPAWYGDCL PERDFPTYVD LHLDGRFPLG EFVSERIGLG DIEGAFTKMK
     QGDVLRSVVE F
//
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