ADH1_EMENI
ID ADH1_EMENI Reviewed; 350 AA.
AC P08843; C8VL73; Q5ARV1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P06525};
DE AltName: Full=Alcohol dehydrogenase I;
DE Short=ADH I;
GN Name=alcA; ORFNames=AN8979;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3297923; DOI=10.1016/0378-1119(87)90309-x;
RA Gwynne D.I., Buxton F.P., Sibley S., Davies R.W., Lockington R.A.,
RA Scazzocchio C., Sealy-Lewis H.M.;
RT "Comparison of the cis-acting control regions of two coordinately
RT controlled genes involved in ethanol utilization in Aspergillus nidulans.";
RL Gene 51:205-216(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:P06525};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:P06525};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}.
CC Secreted {ECO:0000269|PubMed:19146970}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M16196; AAA33291.1; -; Genomic_DNA.
DR EMBL; AACD01000168; EAA64311.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF84526.1; -; Genomic_DNA.
DR PIR; A29054; A29054.
DR RefSeq; XP_682248.1; XM_677156.1.
DR AlphaFoldDB; P08843; -.
DR SMR; P08843; -.
DR STRING; 162425.CADANIAP00007876; -.
DR PRIDE; P08843; -.
DR EnsemblFungi; CBF84526; CBF84526; ANIA_08979.
DR EnsemblFungi; EAA64311; EAA64311; AN8979.2.
DR GeneID; 2868277; -.
DR KEGG; ani:AN8979.2; -.
DR VEuPathDB; FungiDB:AN8979; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; P08843; -.
DR OMA; QYAHNVF; -.
DR OrthoDB; 771875at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:AspGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046187; P:acetaldehyde catabolic process; IEP:AspGD.
DR GO; GO:0097308; P:cellular response to farnesol; IEP:AspGD.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:AspGD.
DR GO; GO:0006567; P:threonine catabolic process; IMP:AspGD.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 InterPro; IPR001763; Rhodanese-like_dom.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome;
KW Secreted; Zinc.
FT CHAIN 1..350
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160719"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 178..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 271..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT CONFLICT 2
FT /note="S -> C (in Ref. 1; AAA33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="L -> V (in Ref. 1; AAA33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..239
FT /note="KAATPDG -> RHGRGC (in Ref. 1; AAA33291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 37153 MW; 730F216F16217AC4 CRC64;
MSIPTMQWAQ VAEKVGGPLV YKQIPVPKPG PDQILVKIRY SGVCHTDLHA MMGHWPIPVK
MPLVGGHEGA GIVVAKGELV HEFEIGDQAG IKWLNGSCGE CEFCRQSDDP LCARAQLSGY
TVDGTFQQYA LGKASHASKI PAGVPLDAAA PVLCAGITVY KGLKEAGVRP GQTVAIVGAG
GGLGSLAQQY AKAMGIRVVA VDGGDEKRAM CESLGTETYV DFTKSKDLVA DVKAATPDGL
GAHAVILLAV SEKPFQQATE YVRSRGTIVA IGLPPDAYLK APVINTVVRM ITIKGSYVGN
RQDGVEALDF FARGLIKAPF KTAPLKDLPK IYELMEQGRI AGRYVLEMPE
