ID A0A0D2AZ31_9EURO Unreviewed; 385 AA.
AC A0A0D2AZ31;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Alcohol dehydrogenase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_09221 {ECO:0000313|EMBL:KIW11948.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW11948.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW11948.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW11948.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847498; KIW11948.1; -; Genomic_DNA.
DR RefSeq; XP_016232164.1; XM_016383541.1.
DR AlphaFoldDB; A0A0D2AZ31; -.
DR STRING; 91928.A0A0D2AZ31; -.
DR GeneID; 27336304; -.
DR VEuPathDB; FungiDB:PV08_09221; -.
DR HOGENOM; CLU_026673_11_3_1; -.
DR OrthoDB; 21669at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08282; PFDH_like; 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:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 31..140
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 191..259
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 385 AA; 41061 MW; 1580F3456F10DAD2 CRC64;
MSSTQTMKAV NYQGPFSVKV EDVPKAKIEH PDDVVVKITT TAICGSDLHM YEGRTSAKPG
ITFGHENMGI VEEVGPGVTT LHKGDRVVLP FNVADGRCRN CEEGKTGFCE GVNPGFSGGA
YGYVAMGPYR GGQAQYLRVP FADFNALKLP PGKEHESDFI LVADVFPTGW HGVTISGFKP
GETIAVWGAG PVGLMAAYSA VLRGASKVFS VDRVPERLAA AKKIGCIPID FSKGDAADQI
IEQNGGMVDR TVDAVGYQAI DTGGKERPNI VLEDMIKATR PCGGLGIPGL YVPTDPGAPD
EASGKGMLSL SFGKLFEKGL SLATGQCNVK QYNRYLRDLI ISGKAKPSFV VSHEIGIEDA
ETAYEKFDKR IDGYTKVLIH PNGPL
//
