ADH1A_SAAHA
ID ADH1A_SAAHA Reviewed; 375 AA.
AC P25405;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alcohol dehydrogenase 1A;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase I-A;
DE Short=ADH IA;
OS Saara hardwickii (Indian spiny-tailed lizard) (Uromastyx hardwickii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Acrodonta; Agamidae; Uromastycinae; Saara.
OX NCBI_TaxID=40250;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT GLY-1.
RX PubMed=8612630; DOI=10.1111/j.1432-1033.1996.00563.x;
RA Hjelmqvist L., Shafqat J., Siddiqi A.R., Joernvall H.;
RT "Linking of isozyme and class variability patterns in the emergence of
RT novel alcohol dehydrogenase functions. Characterization of isozymes in
RT Uromastix hardwickii.";
RL Eur. J. Biochem. 236:563-570(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-18.
RC TISSUE=Liver;
RX PubMed=1544464; DOI=10.1016/0014-5793(92)80080-z;
RA Hjelmqvist L., Ericsson M., Shafqat J., Carlquist M., Siddiqi A.R.,
RA Hoeoeg J.-O., Joernvall H.;
RT "Reptilian alcohol dehydrogenase. Heterogeneity relevant to class
RT multiplicity of the mammalian enzyme.";
RL FEBS Lett. 298:297-300(1992).
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: Multimeric (with different ratios of monomers).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In U.hardwickii there are two isozymes of alcohol
CC dehydrogenase I.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-I subfamily. {ECO:0000305}.
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DR PIR; S62638; S62638.
DR AlphaFoldDB; P25405; -.
DR SMR; P25405; -.
DR iPTMnet; P25405; -.
DR PRIDE; P25405; -.
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 1A"
FT /id="PRO_0000160677"
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 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-acetylglycine"
FT /evidence="ECO:0000269|PubMed:8612630"
SQ SEQUENCE 375 AA; 39663 MW; F315BB777996D906 CRC64;
GTAGKVIKCK AAIAWEIKKP LSIEQIEVAP PKAHEVRIKI LATGICRSDD HVISGAFKMP
LPMVLGHEAA GVVESVGEGV TCVKPGDKVI PLFVPQCGKC SSCRSTRGNL CTSNDLSAAT
GLMPDGTSRF TCKGKSLHHF ISTSSFTEYT VVHENSVVKI DAAAPLEKVC LIGCGFSTGY
GAAVETAKVE PGSTCAVFGL GGVGLSAVMG CKAAGASRII GVDINKDKFP KAKEMGATEC
VNPLDYKKPI NEVLFDLTGG EGVDYSFEVI GRTDTMTAAL ASCHMDYGTS IIVGLPPSAS
EITFSPGLIF TGRTWKGSVF GGWKSKDSVP RLVSDFMQKK FSLDPLITHT MPFDKINEGF
ELLRAGKSIR SVLLF
