ID O28179_ARCFU Unreviewed; 402 AA.
AC O28179;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE SubName: Full=Alcohol dehydrogenase, zinc-dependent {ECO:0000313|EMBL:AAB89145.1};
GN OrderedLocusNames=AF_2101 {ECO:0000313|EMBL:AAB89145.1};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325 {ECO:0000313|EMBL:AAB89145.1, ECO:0000313|Proteomes:UP000002199};
RN [1] {ECO:0000313|EMBL:AAB89145.1, ECO:0000313|Proteomes:UP000002199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16
RC {ECO:0000313|Proteomes:UP000002199};
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.P., Clayton R.A., Tomb J., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B., Peterson S.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L., Utterback T., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AE000782; AAB89145.1; -; Genomic_DNA.
DR PIR; E69512; E69512.
DR RefSeq; WP_010879592.1; NC_000917.1.
DR AlphaFoldDB; O28179; -.
DR STRING; 224325.AF_2101; -.
DR PaxDb; 224325-AF_2101; -.
DR EnsemblBacteria; AAB89145; AAB89145; AF_2101.
DR GeneID; 24795848; -.
DR KEGG; afu:AF_2101; -.
DR eggNOG; arCOG01459; Archaea.
DR HOGENOM; CLU_026673_11_0_2; -.
DR OrthoDB; 73567at2157; -.
DR PhylomeDB; O28179; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051262; P:protein tetramerization; IEA:UniProt.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 49..173
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 215..345
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 402 AA; 43837 MW; D53C08959B242983 CRC64;
MRALVVELRL WKAALSLLLG KVTKSVYYSP LSLLKYYKNY PEPALPDEDW VKVKTRLCGI
CGSDLRIITL QESFYLAPLT SFPFIPGHEV VGEVVEVGKE ADAQEGERVV INTALSCRVR
GFDDCDACRK GHFAACHNVD RGRISPGIFT GTCRDTGGGW AEYFVAHESQ LVRVPEGIRD
ENAVFAEPLT IGIHSALRSF PDDGEVVAIV GCGVIGICTI IALRHLGFRG EIIGIDISER
QAELARKFGA DGVVTENPVE RIAEMTGGRV YRPPRDKPMF IGGGVDVAFE CTGIPQTVDT
ALRITKPLGR VVIAGTVAKM GVDWAPVFAK ELSVLGTFGC GIEEVNGEKR DAFDIAFEIL
KKVDLSSLLT HRFTIEDYKK ALRAAIEKGK SGAVKVAFDF TL
//
