ADH1_APTAU
ID ADH1_APTAU Reviewed; 375 AA.
AC P49645;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase I;
GN Name=ADH1;
OS Apteryx australis (Southern brown kiwi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Apterygiformes; Apterygidae; Apteryx.
OX NCBI_TaxID=8822;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7541757; DOI=10.1016/0014-5793(95)00554-m;
RA Hjelmqvist L., Metsis M., Persson H., Hoeoeg J.-O., McLennan J.,
RA Joernvall H.;
RT "Alcohol dehydrogenase of class I: kiwi liver enzyme, parallel evolution in
RT separate vertebrate lines, and correlation with 12S rRNA patterns.";
RL FEBS Lett. 367:306-310(1995).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-2.
RX PubMed=7607314; DOI=10.1016/0014-5793(95)00572-q;
RA Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J.,
RA Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Joernvall H.;
RT "Multiplicity of N-terminal structures of medium-chain alcohol
RT dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and
RT higher vertebrate class I, II, and III forms of the enzyme.";
RL FEBS Lett. 367:237-240(1995).
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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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DR EMBL; S78778; AAC60755.2; -; mRNA.
DR PIR; S66272; S66272.
DR AlphaFoldDB; P49645; -.
DR SMR; P49645; -.
DR iPTMnet; P49645; -.
DR PRIDE; P49645; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160671"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:7607314"
SQ SEQUENCE 375 AA; 39631 MW; A6EBC1BEB0D66E02 CRC64;
MSTAGKVIKC KAAVLWEPKK PFSIEEVEVA PPKAHEVRIK ILATGICRSD DHVITGALVR
PFPIILGHEA AGVVESVGEG VTSVKPGDKV IPLFVPQCGE CSACLSTKGN LCSKNDIGSA
SGLMPDGTTR FTCKGKAIHH FIGTSTFTEY TVVHETAVAK IAAAAPLEKV CLIGCGFSTG
YGAAVQTAKV EPGSTCAVFG LGGVGLSVVM GCKAAGASRI IAIDINKDKF AKAKELGATD
CVNPKDFTKP IHEVLMEMTG LGVDYSFEVI GHTETMAAAL ASCHFNYGVS VILGVPPAAE
KISFDPMLLF SGRTWKGSVF GGWKSKDAVP KLVADYMEKK FVLEPLITHT LPFIKINEGF
DLLRKGKSIR SVLVF
