ID M0AF55_NATA1 Unreviewed; 319 AA.
AC M0AF55;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:ELY97174.1};
GN ORFNames=C481_20666 {ECO:0000313|EMBL:ELY97174.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELY97174.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELY97174.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELY97174.1,
RC ECO:0000313|Proteomes:UP000011554};
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 -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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:ELY97174.1}.
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DR EMBL; AOIO01000048; ELY97174.1; -; Genomic_DNA.
DR RefSeq; WP_006111248.1; NZ_AOIO01000048.1.
DR AlphaFoldDB; M0AF55; -.
DR STRING; 29540.C481_20666; -.
DR PATRIC; fig|29540.5.peg.4182; -.
DR eggNOG; arCOG01754; Archaea.
DR OrthoDB; 34275at2157; -.
DR Proteomes; UP000011554; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000011554}.
FT DOMAIN 15..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 34732 MW; 714B9BBABD5324FE CRC64;
MTESEKWQLL IPEQIASEGP ESISDIVLSV ETYDDETIGD QLPDADAIIL RGVELDTDLI
ADAERLKVIS KHGVGLDSID IDAASDRGIV VCNTPQANSR TVAEHAITLI LTMRRNLLQA
DRAVRGGNWD ARSDWDRFSR QTITGDTLGL FGFGSIAREA ADLAVGMGMR CIVYDPYVSE
DKLPADVEKA SEKRALFEAA DTVSVHAPLT DETRRAIGRD ELREIDYIVN TARGEIIDES
ALERALAEDE LIAAGLDVLH DEPPAPDDPL LQRDDVILSP HMGTLSVEAT RRMSVGAAEN
VRTVYDGGVP ESTVNKDAL
//
