ID M0NTP5_9EURY Unreviewed; 346 AA.
AC M0NTP5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:EMA61131.1};
GN ORFNames=C469_07667 {ECO:0000313|EMBL:EMA61131.1};
OS Halorubrum lipolyticum DSM 21995.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227482 {ECO:0000313|EMBL:EMA61131.1, ECO:0000313|Proteomes:UP000011650};
RN [1] {ECO:0000313|EMBL:EMA61131.1, ECO:0000313|Proteomes:UP000011650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21995 {ECO:0000313|EMBL:EMA61131.1,
RC ECO:0000313|Proteomes:UP000011650};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:EMA61131.1}.
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DR EMBL; AOJG01000018; EMA61131.1; -; Genomic_DNA.
DR RefSeq; WP_008005308.1; NZ_AOJG01000018.1.
DR AlphaFoldDB; M0NTP5; -.
DR STRING; 1227482.C469_07667; -.
DR PATRIC; fig|1227482.3.peg.1547; -.
DR OrthoDB; 9358at2157; -.
DR Proteomes; UP000011650; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08287; FDH_like_ADH3; 1.
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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..124
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 179..296
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 346 AA; 36343 MW; 3C7C0928C052627D CRC64;
MRAAIFNGPG DIGVEERPRP DIEAPTDAII RVTHTAVCGS DLWFYRGDSD RDEGSPVGHE
PMGIVEAVGD DVTSVAPGDR VLAPFTISCG ECEFCRKGLH TSCENGDSWG GDNGGGQGEY
VRSTRADGTL VRVPDRFADD EDTLRSLLPL TDVMGTGHHA AVSAGVEAGA TVVVIGDGAV
GLCGVLAARR LGAERIVAVG HHEDRLELAA EFGATETVSE RGEAAVERVR ELTHGGPNHV
MECVGAASAM NTAIDIVRPG GTIGYVGVPY GVEEEGLDVF GMFGRNVTLA GGVAPVRAYA
EELMADVLQG TLDPAPIFTE TVGLDEVDEG YRMMDEREAI KVLVKP
//
