ID L9W6K9_9EURY Unreviewed; 355 AA.
AC L9W6K9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=2,3-butanediol dehydrogenase {ECO:0000313|EMBL:ELY43968.1};
GN ORFNames=C494_17783 {ECO:0000313|EMBL:ELY43968.1};
OS Natronorubrum bangense JCM 10635.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1227500 {ECO:0000313|EMBL:ELY43968.1, ECO:0000313|Proteomes:UP000011690};
RN [1] {ECO:0000313|EMBL:ELY43968.1, ECO:0000313|Proteomes:UP000011690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10635 {ECO:0000313|EMBL:ELY43968.1,
RC ECO:0000313|Proteomes:UP000011690};
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|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:ELY43968.1}.
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DR EMBL; AOHY01000054; ELY43968.1; -; Genomic_DNA.
DR AlphaFoldDB; L9W6K9; -.
DR STRING; 1227500.C494_17783; -.
DR PATRIC; fig|1227500.6.peg.3584; -.
DR eggNOG; arCOG01459; Archaea.
DR OrthoDB; 73567at2157; -.
DR Proteomes; UP000011690; 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; cd08233; butanediol_DH_like; 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; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..142
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 183..302
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 355 AA; 37133 MW; 43DE0CA6FF3E77F0 CRC64;
MRSAVFHGRE NIQVDEIAEP VVERDSVLID VIAAGICGSD LHEYAAGPIF IPGDAPHPVT
GETAPVSMGH EFGGEVIEIG DDVEDIAVGD TVTVNPILYC GECRYCEDGS YHLCESGGFI
GLSGGGGGFS EQIAVSSEQA IPVPDDVPAE YAALVEPFSV GLHAVRNAEF SAGDSVAVYG
TGPIGLTVIQ AAKAAGANPV YAIEPQDARR ELAAEVGADM TFNPIDTDAP EAIIEQSDGG
VDATFEVAGI EQTVRDAIRS VKNDGSVTIV SIFEESVEIE PNEIVLGERT VSGTLAYEGG
PNSDVEFGAV IDMFADETLD PEPLITSRIG LEEIVDGFDT LLGGEHDEIK IIVEP
//