ADH1_PELPE
ID ADH1_PELPE Reviewed; 375 AA.
AC P22797;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase, major;
OS Pelophylax perezi (Perez's frog) (Rana perezi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=8403;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RC TISSUE=Liver;
RX PubMed=2007119; DOI=10.1021/bi00225a011;
RA Cederlund E., Peralba J.M., Pares X., Joernvall H.;
RT "Amphibian alcohol dehydrogenase, the major frog liver enzyme.
RT Relationships to other forms and assessment of an early gene duplication
RT separating vertebrate class I and class III alcohol dehydrogenases.";
RL Biochemistry 30:2811-2816(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-5.
RX PubMed=2387402; DOI=10.1016/0014-5793(90)81152-e;
RA Egestad B., Estonius M., Danielsson O., Persson B., Cederlund E.,
RA Kaiser R., Holmquist B., Vallee B., Pares X., Jefferey J., Joernvall H.;
RT "Fast atom bombardment mass spectrometry and chemical analysis in
RT determinations of acyl-blocked protein structures.";
RL FEBS Lett. 269:194-196(1990).
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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DR PIR; A38405; A38405.
DR PIR; S11075; S11075.
DR AlphaFoldDB; P22797; -.
DR SMR; P22797; -.
DR iPTMnet; P22797; -.
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 CHAIN 1..375
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160680"
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"
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 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2007119"
SQ SEQUENCE 375 AA; 40185 MW; 283E0A60E3339195 CRC64;
ATAGKVIKCK AAVCWGPKQP LSIEEIEVAP PKRHEVRVKI VATGICRSDD HVISGALSDM
KFPVILGHEA AGVVESVGEG VTKFKPGDKV IPLFVPQCGE CRCCKNPESN LCYKNDIGKY
DGVLLDKTSR FTCKGKSIHN FISTSTFTEY TVLDEIAVAK IHEDAPLEKV CLIGCGFSTG
YGSAVNTGKV KPGSTCAVFG LGGVGLSVII GCKVAGASRI IGVDLNSDKF TTAKECGATE
CINPKDYNIP IHEVLAKMTD DGVDYAFEVI GNTTVMTSAL SSSHFGCGKT VIVGLAPSSA
VMSFDPLLIL TGRILTGAVF GGWKSKDDVP KLVRDYLNKK FDFDPLITHY MPFEKINEGF
ELLRNGKSIR TILTF
