ADH1B_SAAHA
ID ADH1B_SAAHA Reviewed; 375 AA.
AC P25406;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Alcohol dehydrogenase 1B;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase I-B;
DE Short=ADH IB;
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.
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, AND ACETYLATION AT SER-1.
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; S62639; S62639.
DR AlphaFoldDB; P25406; -.
DR SMR; P25406; -.
DR iPTMnet; P25406; -.
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 1B"
FT /id="PRO_0000160678"
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-acetylserine"
FT /evidence="ECO:0000269|PubMed:1544464"
SQ SEQUENCE 375 AA; 40060 MW; 392071E594C32E0D CRC64;
STAGKVIKCK AAVVWEPKKP FSIVEIEVAP PKAHEVRIKI LASGICRSDD HVLSGALKVN
FPIILGHEAA GVVESVGEGV TSMKPGDKVI PIFLPQCGEC NSCRHPRGNV CKKSELGPFT
GLLYDGTSRF TYQGKPVYHF VRTGTFTEYT VAPEDSVVKI DASAPLEKVC LIGCGFSTGY
GAAINSAKVQ PGSTCAVFGL GGVGLSAVMG CKAAGASRII GIDINKEKFP KAKELGATEC
VNPLDYKKPI NEVLFDMTDG EGVEYSFEVI GRTDTMTAAL ASCHNNYGTS VIVGVPPSAS
QIAFDPLLLF TGRTWKGSVF GGWKSKDAVP RLVSDFMGKK FILDPLITHT MPFEKINEGF
ELLRSGKSIR TVLTF
