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Database: UniProt
Entry: G7XW37_ASPKW
LinkDB: G7XW37_ASPKW
Original site: G7XW37_ASPKW 
ID   G7XW37_ASPKW            Unreviewed;       380 AA.
AC   G7XW37;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:GAA91146.1};
GN   ORFNames=AKAW_09260 {ECO:0000313|EMBL:GAA91146.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA91146.1};
RN   [1] {ECO:0000313|EMBL:GAA91146.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA91146.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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; DF126478; GAA91146.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XW37; -.
DR   STRING; 1033177.G7XW37; -.
DR   VEuPathDB; FungiDB:AKAW_09260; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   InParanoid; G7XW37; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF3; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01980)-RELATED; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          32..160
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          209..336
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   380 AA;  41545 MW;  51A207BC1BACC1A6 CRC64;
     MPPPEHFHGY LSHSPTTPLT YAPYTPKPFT PTDIEINITH CGICGTDLHT LRSGWGPNTT
     TYPCIVGHEI IGIVTRIGSS IPTYPNTTPL RIGDRVGIGA QTHSCLQPSC EECVAGKENY
     CPRITGTYNS RYWDNETGKR SDVIAYGGFA RKWRGPAAFA FRIPERLESE VAAPLLCAGT
     TVFAPLRKYL GDGTDSGKGK TVAVVGIGGL GHLGIMFAKA LGCERVIGIS RSNGKREDAV
     KGLGADEFIA TGEEKGWEKK WSRTVDLILC TVDGDDMPLG KYLRLLKAGG TFVLVGAPEK
     PLPRMRAFEL IGKGVNVTGS NIGSREDIRC MLEVAAEKGV RPWVETRRME EVNETLRDME
     AGRARFRYVL VNGEERESRL
//
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