ID K0KPD6_WICCF Unreviewed; 421 AA.
AC K0KPD6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Alcohol dehydrogenase, putative {ECO:0000313|EMBL:CCH47130.1};
DE EC=1.1.1.284 {ECO:0000313|EMBL:CCH47130.1};
GN ORFNames=BN7_6741 {ECO:0000313|EMBL:CCH47130.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH47130.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH47130.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(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}.
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:CCH47130.1}.
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DR EMBL; CAIF01000330; CCH47130.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KPD6; -.
DR STRING; 1206466.K0KPD6; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_3_1; -.
DR InParanoid; K0KPD6; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 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 PANTHER; PTHR42813:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G03930)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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 ECO:0000313|EMBL:CCH47130.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 40..162
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 210..278
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 421 AA; 46180 MW; D0DB091CCCEA399A CRC64;
MTEVTPIHKE SSSIKCLALQ WMGKDNVEVN EVPKPQITEP EDALIKVTGS TVCGSDLHLY
HGEILDLRKG DILGHEYCGI VEEIGSNVKD LKPGDRIVAS FQIACGHCRY CKQKLTSGCD
NTSDSPIQKE MYGDNFAGIY GYAHFTGGFA GGQAEYVRAP KADFNLMKIP DNVPDEKALY
ISDIIPTSYH SVVSAEVKSG DIVAIWGLGP IGILAANFAK LKGAKQIIGI DNVKERLDKV
QKVVPGTKVI NFDEQKDVVS AIREIAPGGV DASIDAAAFR YAKSFTDKIQ RTLGLETDTS
ELINEQIKAT KKFGTISLVA DYVGLANQFL IGALMEKGIT LRGCGQAPVQ KYWKELMSRI
QSGEFDPSFI LTHRFDFKEF KELYKAFDEK KGGIEKVFVQ TKFSKPPAPG TPKLTKVSDL
K
//
