ADH1_STRCA
ID ADH1_STRCA Reviewed; 374 AA.
AC P80338;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase I;
GN Name=ADH1;
OS Struthio camelus (Common ostrich).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=8801;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=7925350; DOI=10.1111/j.1432-1033.1994.00373.x;
RA Estonius M., Hjelmqvist L., Joernvall H.;
RT "Diversity of vertebrate class I alcohol dehydrogenase. Mammalian and non-
RT mammalian enzyme functions correlated through the structure of a ratite
RT enzyme.";
RL Eur. J. Biochem. 224:373-378(1994).
RN [2]
RP PROTEIN SEQUENCE OF 1-13, AND ACETYLATION AT SER-1.
RX PubMed=8706859; DOI=10.1016/0014-5793(96)00657-6;
RA Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.;
RT "Alcoholytic deblocking of N-terminally acetylated peptides and proteins
RT for sequence analysis.";
RL FEBS Lett. 390:199-202(1996).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
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 PIR; S48157; S48157.
DR AlphaFoldDB; P80338; -.
DR SMR; P80338; -.
DR iPTMnet; P80338; -.
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..374
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160674"
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 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 199..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 292..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:7607314,
FT ECO:0000269|PubMed:8706859"
FT VARIANT 112
FT /note="R -> C"
SQ SEQUENCE 374 AA; 39583 MW; 3ACC5386332EEC3C CRC64;
STAGKVIKCK AAVLWEPKKP FSIEEVEVAP PKAHEVRVKI IATGICRSDD HVISGVLVMP
FPIILGHEAA GVVESVGEGV TSVKPGDKVI PLFVPQCGEC SVCLSTKGNL CRKNDIGPAS
ALMPDGTSRF TCKGKAIHHF AGTSTFTEYT VLHETAVAKI DAAAPLEKVC LIGCGFSTGY
GAALQTAKVE PGSTCAVFGL GGVGLSVVMG CKAAGASRII GVDINKDKFA KAKELGATDC
VNPKDFTKPI HEVLMEMTGL GVDYSFEVIG HTETMAAALA SCHFNYGVSV IVGVPPAAEK
LSFDPMLLFS GRTWKGSVFG GWKSKDSVPK LVADYMEKKF VLDPLITHTL PFHKINEGFD
LLRTGKSIRS VLLF
