ID A0A218V2G6_9PASE Unreviewed; 1202 AA.
AC A0A218V2G6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alcohol dehydrogenase class-3 {ECO:0000256|ARBA:ARBA00020108};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.284 {ECO:0000256|ARBA:ARBA00012309};
DE AltName: Full=Alcohol dehydrogenase class-III {ECO:0000256|ARBA:ARBA00033399};
DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00032767};
GN Name=ADHX {ECO:0000313|EMBL:OWK60078.1};
GN ORFNames=RLOC_00002079 {ECO:0000313|EMBL:OWK60078.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK60078.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK60078.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK60078.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001030};
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:0000256|ARBA:ARBA00001646};
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:0000256|ARBA:ARBA00001146};
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:0000256|ARBA:ARBA00000781};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000256|ARBA:ARBA00010902}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK60078.1}.
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DR EMBL; MUZQ01000066; OWK60078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218V2G6; -.
DR STRING; 299123.ENSLSDP00000013800; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
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; cd08299; alcohol_DH_class_I_II_IV; 1.
DR CDD; cd08300; alcohol_DH_class_III; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR014183; ADH_3.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF4; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR Pfam; PF08240; ADH_N; 3.
DR Pfam; PF00107; ADH_zinc_N; 3.
DR SUPFAM; SSF50129; GroES-like; 5.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR PROSITE; PS00059; ADH_ZINC; 3.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 2..87
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 162..285
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT DOMAIN 398..524
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 567..672
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT DOMAIN 882..934
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 1037..1166
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT REGION 723..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 127910 MW; B2E2C3F2A97B6341 CRC64;
MATGICRSDD HVITGALVMP FPIILGHEAA GVVESVGQGV TSVKPGDKVI PLFVPQCGEC
KSCLNTKGNL CSKTDLATGA GLMPDGTTRF TCKGKAIYHF IGTSTFTEYT VLHESAVAKI
DSAAPLEKVC LIGCGFSTGY GAALQTAKVE PGSTCAVFGL GGVGLSVIMG CKAAGAARII
AVDINSDKFA KAKELGATDC VNPKDFNKPI HQVLMDMTGE GVDYSFEVIG RTDTMTAALA
CCQCNYGVSV IVGVPPAAQN ITFDPMLLFT GRSWKGSVFG GWKSKDAVPK LVADYMKKKF
VLDPLITHTL TLAKINEGFD LLRTGKRPHG HCGKSKDNAF PILLSEVSCP GLLSKVNLPL
QCIPLGCFQV IRCKAAVAWA PGKPLSVEEV EVAPPKAGEV RIKIVATGIC HTDDHILKGS
LPNVEFPVIP GHEGAGIVES IGQGVTSVKP GDKVIPLCLP QCGECSFCQN PESNYCQKTH
FSEPQNLLPD KTSRFSCKGK QIHHFLWVST FAEYTVVPEY AVAKIDAAAP LDKVCLIGCG
FSTGYGAALN TAKVKPGSTC AVFGLGGVGL SVVMGCKAAG AARIIAVDIN SNKFAKAKEL
GATDCINPRD FKKPIQEVLT EMTGQGVDYS FEAIGHTDTM IAALASCNTN TGVCVMVGVL
DSEISIDPVL LLTGRWKTRE CIPKLVSSYL EGKFNSDLLI THTLPFAKYP HCPALLKDTA
KEAEQRDQRS RCSPGPGPSQ PAPLLVGHQE KRMRNSPVLE SLLVLLCLDK IQTDDFPRKI
LLLIKAGFVV ALRAVNEDLL TVIPVATAEV LEPYSKVPLV PLHHWAPLHV SCISLLESYL
KTILIRNRKF NLDVIKCKAA VAWEAGKPLS IEEVEVAPPK AHEVRIKIVA TAVCHTDAYT
LSGADPEGCF PVILGHEGAG IVESVGEGVT KVKKEYLLLK TLHFPVFASR VTQGKGVMPD
GTSRFTCKGK QIYHFMGTST FSEYTVVADI SVAKIDAAAP LDKVCLLGCG ISTGYGAAVN
TAKVEPGSTC AVFGLGGVGL AVIMGCKIAG ASRIIGIDIN KDKYAKAKEF GATECISPQD
SKKPIQEVLV EMTDGGVDYS FECIGNVGVM RAALEACHKG WGVSVIVGVA AAGQEISTRP
FQLVTGRTWK GTAFGGWKSV DNVPKLVTEY MSKKIKVDEF VTHTLPFDKI NEAFELMHSG
KR
//
