(data stored in ACNUC16935 zone)

SWISSPROT: 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   05-JUL-2017, entry version 123.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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
RT   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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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   ProteinModelPortal; P08843; -.
DR   SMR; P08843; -.
DR   STRING; 162425.CADANIAP00007876; -.
DR   EnsemblFungi; CADANIAT00007876; CADANIAP00007876; CADANIAG00007876.
DR   EnsemblFungi; EAA64311; EAA64311; AN8979.2.
DR   GeneID; 2868277; -.
DR   KEGG; ani:AN8979.2; -.
DR   HOGENOM; HOG000294685; -.
DR   InParanoid; P08843; -.
DR   KO; K13953; -.
DR   OMA; RKGAFPH; -.
DR   OrthoDB; EOG092C2Q8E; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006116; P:NADH oxidation; IBA:GO_Central.
DR   GO; GO:0006567; P:threonine catabolic process; IMP:AspGD.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020843; PKS_ER.
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;
DR   PRODOM; P08843.
DR   SWISS-2DPAGE; P08843.
KW   Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN         1    350       Alcohol dehydrogenase 1.
FT                                /FTId=PRO_0000160719.
FT   NP_BIND     178    184       NAD. {ECO:0000250}.
FT   NP_BIND     271    273       NAD. {ECO:0000250}.
FT   METAL        44     44       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        67     67       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        98     98       Zinc 2. {ECO:0000250}.
FT   METAL       101    101       Zinc 2. {ECO:0000250}.
FT   METAL       104    104       Zinc 2. {ECO:0000250}.
FT   METAL       112    112       Zinc 2. {ECO:0000250}.
FT   METAL       154    154       Zinc 1; catalytic. {ECO:0000250}.
FT   BINDING     202    202       NAD. {ECO:0000250}.
FT   BINDING     207    207       NAD. {ECO:0000250}.
FT   BINDING     343    343       NAD. {ECO:0000250}.
FT   CONFLICT      2      2       S -> C (in Ref. 1; AAA33291).
FT                                {ECO:0000305}.
FT   CONFLICT    146    146       L -> V (in Ref. 1; AAA33291).
FT                                {ECO:0000305}.
FT   CONFLICT    233    239       KAATPDG -> RHGRGC (in Ref. 1; AAA33291).
FT                                {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
//

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