ADH1A_MACMU
ID ADH1A_MACMU Reviewed; 375 AA.
AC P28469;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Alcohol dehydrogenase 1A;
DE EC=1.1.1.1 {ECO:0000269|PubMed:1618764};
DE AltName: Full=Alcohol dehydrogenase subunit alpha;
GN Name=ADH1A; Synonyms=ADH1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=1618764; DOI=10.1016/s0021-9258(18)42318-6;
RA Light D.R., Dennis M.S., Forsythe I.J., Liu C.C., Green D.W., Kratzer D.,
RA Plapp B.V.;
RT "Alpha-isoenzyme of alcohol dehydrogenase from monkey liver. Cloning,
RT expression, mechanism, coenzyme, and substrate specificity.";
RL J. Biol. Chem. 267:12592-12599(1992).
CC -!- FUNCTION: Alcohol dehydrogenase. Oxidizes primary as well as secondary
CC alcohols. Ethanol is a very poor substrate.
CC {ECO:0000269|PubMed:1618764}.
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:0000269|PubMed:1618764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10737;
CC Evidence={ECO:0000305|PubMed:1618764};
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:0000269|PubMed:1618764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10741;
CC Evidence={ECO:0000305|PubMed:1618764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butan-1-ol + NAD(+) = butanal + H(+) + NADH;
CC Xref=Rhea:RHEA:33199, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:1618764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33200;
CC Evidence={ECO:0000305|PubMed:1618764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-propanol + NAD(+) = H(+) + NADH + propanal;
CC Xref=Rhea:RHEA:50704, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:28831, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:1618764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50705;
CC Evidence={ECO:0000305|PubMed:1618764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + propan-2-ol = acetone + H(+) + NADH;
CC Xref=Rhea:RHEA:41984, ChEBI:CHEBI:15347, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17824, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:1618764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41985;
CC Evidence={ECO:0000305|PubMed:1618764};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07327};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P07327};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 mM for ethanol {ECO:0000269|PubMed:1618764};
CC KM=2.0 mM for 1-propanol {ECO:0000269|PubMed:1618764};
CC KM=0.19 mM for butan-1-ol {ECO:0000269|PubMed:1618764};
CC KM=0.024 mM for cyclohexanol {ECO:0000269|PubMed:1618764};
CC KM=1.4 mM for (S)-2-butanol {ECO:0000269|PubMed:1618764};
CC KM=0.42 mM for (R)-2-butanol {ECO:0000269|PubMed:1618764};
CC KM=3.5 mM for propan-2-ol {ECO:0000269|PubMed:1618764};
CC -!- SUBUNIT: Dimer of identical or heterodimer of closely related subunits
CC alpha, beta, or gamma that are encoded by genes ADH1A, ADH1B, and
CC ADH1C, respectively. {ECO:0000250|UniProtKB:P07327}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M81807; AAA36830.1; -; mRNA.
DR PIR; I55359; I55359.
DR RefSeq; NP_001036230.1; NM_001042765.1.
DR AlphaFoldDB; P28469; -.
DR SMR; P28469; -.
DR STRING; 9544.ENSMMUP00000024652; -.
DR GeneID; 707682; -.
DR KEGG; mcc:707682; -.
DR CTD; 124; -.
DR eggNOG; KOG0022; Eukaryota.
DR InParanoid; P28469; -.
DR OrthoDB; 664798at2759; -.
DR SABIO-RK; P28469; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:1990362; F:butanol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:UniProtKB.
DR GO; GO:0006069; P:ethanol oxidation; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR GO; GO:1902652; P:secondary alcohol metabolic process; IDA:UniProtKB.
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; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase 1A"
FT /id="PRO_0000160659"
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|UniProtKB:P07327"
FT BINDING 48..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
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|UniProtKB:P07327"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07327"
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|UniProtKB:P07327"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 318..320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P07327"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
SQ SEQUENCE 375 AA; 39913 MW; 8B0DDC03673AA8DA CRC64;
MSTAGKVIKC KAAVLWEVMK PFSIEDVEVA PPKAYEVRIK MVTVGICGTD DHVVSGTMVT
PLPVILGHEA AGIVESVGEG VTTVEPGDKV IPLALPQCGK CRICKTPERN YCLKNDVSNP
RGTLQDGTSR FTCRGKPIHH FLGVSTFSQY TVVDENAVAK IDAASPMEKV CLIGCGFSTG
YGSAVKVAKV TPGSTCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
NLSINPMLLL TGRTWKGAVY GGFKSKEDIP KLVADFMAKK FSLDALITHV LPFEKINEGF
DLLRSGKSIR TILTF
