ADHX_SCYCA
ID ADHX_SCYCA Reviewed; 376 AA.
AC P86884;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Alcohol dehydrogenase class-3 {ECO:0000250|UniProtKB:P11766};
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P11766};
DE AltName: Full=Alcohol dehydrogenase class-III {ECO:0000250|UniProtKB:P11766};
DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000250|UniProtKB:P11766};
DE Short=FALDH {ECO:0000250|UniProtKB:P11766};
DE Short=FDH {ECO:0000250|UniProtKB:P11766};
DE Short=GSH-FDH {ECO:0000250|UniProtKB:P11766};
DE EC=1.1.1.-;
DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000250|UniProtKB:P11766};
DE EC=1.1.1.284 {ECO:0000250|UniProtKB:P11766};
OS Scyliorhinus canicula (Small-spotted catshark) (Squalus canicula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=7830;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RA Cederlund E., Hedlund J., Hjelmqvist L., Jonsson A., Shafqat J.;
RL Submitted (DEC-2010) to UniProtKB.
CC -!- FUNCTION: Class-III ADH is remarkably ineffective in oxidizing ethanol,
CC but it readily catalyzes the oxidation of long-chain primary alcohols
CC and the oxidation of S-(hydroxymethyl) glutathione.
CC {ECO:0000250|UniProtKB:P11766}.
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:P11766};
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:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11766}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000255}.
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DR AlphaFoldDB; P86884; -.
DR SMR; P86884; -.
DR BRENDA; 1.1.1.1; 5640.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR CDD; cd08300; alcohol_DH_class_III; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014183; ADH_3.
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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 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..376
FT /note="Alcohol dehydrogenase class-3"
FT /id="PRO_0000405312"
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:P11766"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT SITE 117
FT /note="Important for FDH activity and activation by fatty
FT acids"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P81600"
SQ SEQUENCE 376 AA; 39937 MW; 36D56CECA4B3BA12 CRC64;
AGTVGKVIKC KAAVAWEAGK PLCIEEIEVA PPKAHEVRIK IIATAVCHSD SYTLSGSDSE
GLFPVILGHE GAGIVESVGE GVTCVKAGDR VIPLYIPQCG DCNFCLNPKT NLCQKIRVTQ
GQGLMPDKTS RFTCKGQLLY HYMGTSTFSE YTVVADISVA KIDEAAPLDK VCLLGCGIST
GYGAAVNTAK VEPGSTCAVF GLGGVGLAGI MGCKAAGATR IIGVDLNKDK FTKAKEFGAT
EYINPKDYDK PIQEVLVGLT DGGVDYSFEC IGNVKTMRAA LEACHKGWGT SVIVGVAPAG
HEIATRPFQL VTGRTWKGTA FGGWKSVESV PKLVKEYMAK KLKVDEFVTH TLPFNQINES
FELMHAGKSI RCVLSF
