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Database: UniProt
Entry: H8IIE0_MYCIA
LinkDB: H8IIE0_MYCIA
Original site: H8IIE0_MYCIA 
ID   H8IIE0_MYCIA            Unreviewed;       370 AA.
AC   H8IIE0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Oxidoreductase, zinc-binding dehydrogenase family protein {ECO:0000313|EMBL:AFC46153.1};
GN   OrderedLocusNames=OCU_49340 {ECO:0000313|EMBL:AFC46153.1};
OS   Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS   NCTC 13025 / 3600).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC46153.1, ECO:0000313|Proteomes:UP000008004};
RN   [1] {ECO:0000313|EMBL:AFC46153.1, ECO:0000313|Proteomes:UP000008004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC   {ECO:0000313|Proteomes:UP000008004};
RX   PubMed=22535933; DOI=10.1128/JB.00295-12;
RA   Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA   Kim B.J.;
RT   "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT   13950T.";
RL   J. Bacteriol. 194:2750-2750(2012).
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}.
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DR   EMBL; CP003322; AFC46153.1; -; Genomic_DNA.
DR   RefSeq; WP_009957284.1; NZ_CP076382.1.
DR   AlphaFoldDB; H8IIE0; -.
DR   KEGG; mia:OCU_49340; -.
DR   PATRIC; fig|487521.10.peg.4941; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_11; -.
DR   OMA; RVKMIAT; -.
DR   Proteomes; UP000008004; 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   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43350:SF21; S-NITROSOMYCOTHIOL REDUCTASE MSCR; 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          19..366
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   370 AA;  37689 MW;  A91F3891663AA43E CRC64;
     MSGIRGAVLE HIGAPRPYAR SRPISIADVD LAPPGRDEVL VRIEAAGLCH SDLSVVDGNR
     VRPVPMLLGH EAAGIVERVG DGVGDVAVGQ RVVLVFLPRC GHCAACATEG LTPCEPGSAA
     NGAGTLLGGD IRLSRAGQPV FHHLGVSGFA THAVVNRASA VAVPPDVPAD VAALLGCAVL
     TGGGAVLNVG QPRPGQTVAV VGLGGVGMAA LLTALTYDDV RVVAVDQLPD KLAAARALGA
     HEAYTPQQAE DARVKAAVVV EAVGHPAALE TAIALTAPGG RTITVGLPPP DARITVSPLG
     FVAEGRSLIG SYLGSAVPSR DIPRFVELWR SGRLPVQSLV SSTIALDEIN EAMDHLADGT
     AVRQLIRFDA
//
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