ID A0A2I2G7F6_9EURO Unreviewed; 747 AA.
AC A0A2I2G7F6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=P170DRAFT_494323 {ECO:0000313|EMBL:PLB48812.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB48812.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB48812.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB48812.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, 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:PLB48812.1}.
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DR EMBL; MSFO01000004; PLB48812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2G7F6; -.
DR STRING; 1392250.A0A2I2G7F6; -.
DR VEuPathDB; FungiDB:P170DRAFT_494323; -.
DR OrthoDB; 178754at2759; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd08297; CAD3; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 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 Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF3; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000234275};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 23..352
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 747 AA; 80619 MW; 6405E4A3087E0FC8 CRC64;
MPESIFPKVN GNSLPTTQWA QVSTGKTIEL KKTPVPQPGP DEVLVKIEYS GVCHTDLHSW
KGDWPVTPKD LCVGGHEGAG LVAALGSRVH NLRIGDAVGI QWLNNTCGTC EYCSVGNQPL
CPSLQLSGCT VDGTFQQYCI CKADNAVRIP PNIPLETAAP ILCAGITVYK AILEANVQPG
QTIAIVGGGG GLGSLACQYA KACRYKVLAL SSGSSKRNMC LNDLGADVYV DYKSSNVVDE
VKSTTNGGPH AAVIVSSVEE PFHQALQYIR PGGTVVAVGL PPGKMSTDIF AMVTQKVNIK
GSYVGNRLET EEALNILARA RFEVQSRVVD FSELPRVFDM MEKGSMHGRA VLKVGDHLSK
YPGRFKSLKG SAGPDDVYQS QDSSPTSFVS PTLQRAIKKA GRDFRSDTVT VPTGPVMQAI
VNASTFGDNI YDEGGDSSVN ALQEKIVQLT GKEAALFVPS GTMGNQICLR THLHQPPHTI
LLDYRAHVQC WETGAIPVLS QATVTGVEPK NGVHLTLDDV KDRIVQEDNF HFPPTRIVSL
ENTLSGSILP LKDAREISNY VRSVPVPANR TPIAMHLDGA RLFDGITAEG IDIKDYLACF
DTASLCLSKG IGAPMGSVIV GPKEFIQRAI WFRKMFGGAT RQMGMMAAAA EAALDHNLPQ
LPRVHALARR VAEFFRGIGY ELLLPVSTNM IVLDLKKMSI DGEVVAGYCR RHGLAVFPNG
RLVFHHQTSE DGVSRLQEAL FELIDRH
//
