ADH1G_PAPHA
ID ADH1G_PAPHA Reviewed; 375 AA.
AC O97959;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Alcohol dehydrogenase 1C;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P00326};
DE AltName: Full=Alcohol dehydrogenase subunit gamma;
GN Name=ADH1C; Synonyms=ADH3;
OS Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10331249; DOI=10.1093/oxfordjournals.molbev.a026035;
RA Cheung B., Holmes R.S., Easteal S., Beacham I.R.;
RT "Evolution of class I alcohol dehydrogenase genes in catarrhine primates:
RT gene conversion, substitution rates, and gene regulation.";
RL Mol. Biol. Evol. 16:23-36(1999).
CC -!- FUNCTION: Alcohol dehydrogenase. Exhibits high activity for ethanol
CC oxidation and plays a major role in ethanol catabolism.
CC {ECO:0000250|UniProtKB:P00326}.
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:P00326};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:P00326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25291;
CC Evidence={ECO:0000250|UniProtKB:P00326};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00326};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00326};
CC -!- SUBUNIT: Dimer of identical or non-identical chains of class I alcohol
CC dehydrogenase: ADH1A, ADH1B, and ADH1C. {ECO:0000250|UniProtKB:P00326}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:10331249}.
CC -!- MISCELLANEOUS: There are 7 different ADH's isozymes in human: three
CC belongs to class-I: ADH1A, ADH1B, and ADH1C, one to class-II: ADH4, one
CC to class-III: ADH5, one to class-IV: ADH7 and one to class-V: ADH6.
CC {ECO:0000250|UniProtKB:P00326}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L30113; AAD09950.1; -; mRNA.
DR AlphaFoldDB; O97959; -.
DR SMR; O97959; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; ISS: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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase 1C"
FT /id="PRO_0000160665"
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:P00326"
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:P00326"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00326"
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:P00326"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 318..320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00326"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
SQ SEQUENCE 375 AA; 39841 MW; BBB215BCD5FDB9EA CRC64;
MSTAGKVIKC KAAVLWEVKK PFSIEEVEVA PPKAHEVRIK MVAVGICRSD DHVVSGTLVT
PLPAILGHEA AGIVEGVGEG VTTVKPGDKV IPLFTPQCGK CRVCKNPESN YCFKNDLSNP
RGTMQDGTRR FTCGGKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
YGPAVKVAKV TPGSTCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTIMASL LCCHEACGTS VIVGVPPDSQ
NLSINPVLLL TGRTWKGAIF GGFKSKESVP KLVSDFMAKK FSLDALITNV LPFEKINEGF
DLLRSGKSIR TILMF
