ID A0A2A2FHF7_9EURY Unreviewed; 346 AA.
AC A0A2A2FHF7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=D-arabinose dehydrogenase {ECO:0000313|EMBL:PAU84107.1};
GN ORFNames=CK500_06635 {ECO:0000313|EMBL:PAU84107.1};
OS Halorubrum salipaludis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=2032630 {ECO:0000313|EMBL:PAU84107.1, ECO:0000313|Proteomes:UP000218083};
RN [1] {ECO:0000313|EMBL:PAU84107.1, ECO:0000313|Proteomes:UP000218083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN019 {ECO:0000313|EMBL:PAU84107.1,
RC ECO:0000313|Proteomes:UP000218083};
RA Liu D., Zhang G.;
RT "The strain WRN001 was isolated from Binhai saline alkaline soil, Tianjin,
RT China.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PAU84107.1}.
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DR EMBL; NSKC01000003; PAU84107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2FHF7; -.
DR OrthoDB; 75495at2157; -.
DR Proteomes; UP000218083; 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; cd05284; arabinose_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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 31..140
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 183..310
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 36580 MW; FC2EC02F9327FB5B CRC64;
MQAARLHEYT DDMSEGLTID EVERPEATGA DDVIVEVEGA GWCQTDNHII EGMWAEYVPQ
ELPMTLGHEN AGTVVETGED VELVSPGDPV ICHPVQTCGT CRPCRLGETM YCENDAFNGL
TTDGGFAEYL HTSERSVIPL PSGVEPIDIA PHADAGITAY HAAKKAVADL NPGDHAVVIG
VGGLGHIGLQ CLDAMSAARI TAVDLKESAL DLAAGYGADH LVNPGESDVP DEIEAITDGT
GAAQVLDFVG EDVTTAYAPD ITAAGGDHHI IGYGGHVHEP AQALVNGEFS FVGNIVGRYA
ELQELVALVE QGDVDLHTSR YDLGEVNEVA EKLEHREIDG RAVIMP
//
