ID D4GYW8_HALVD Unreviewed; 324 AA.
AC D4GYW8; L9UI72;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=D-2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:ADE03704.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ADE03704.1};
GN Name=serA1 {ECO:0000313|EMBL:ADE03704.1};
GN OrderedLocusNames=HVO_0122 {ECO:0000313|EMBL:ADE03704.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE03704.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE03704.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001956; ADE03704.1; -; Genomic_DNA.
DR RefSeq; WP_004045234.1; NZ_AOHU01000105.1.
DR AlphaFoldDB; D4GYW8; -.
DR STRING; 309800.HVO_0122; -.
DR PaxDb; 309800-C498_18848; -.
DR EnsemblBacteria; ADE03704; ADE03704; HVO_0122.
DR GeneID; 8926037; -.
DR KEGG; hvo:HVO_0122; -.
DR PATRIC; fig|309800.29.peg.3671; -.
DR eggNOG; arCOG01757; Archaea.
DR HOGENOM; CLU_019796_1_0_2; -.
DR OrthoDB; 168224at2157; -.
DR Proteomes; UP000008243; Chromosome.
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; cd05300; 2-Hacid_dh_1; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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:UP000008243}.
FT DOMAIN 21..303
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..282
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 324 AA; 35307 MW; 807C2E6F868C7DEA CRC64;
MTTILVLDRP THGIPASEYA AALRERLPDA TVRHPKTTAE TLDAATDATI ITSTSLPDEV
LDAADELRLF AGAAAGYDHL PLETLRERGV RVTNASGVHG PNIAEHVIGW LLMITRRLDE
GLRRQRRREW RRFQSYGELQ GSTATVVGLG AIGQAVVERL DAFGVETVGV RYTPEKGGPT
DEVLGFDDLE SALVRTDFLV VACPLTDETR DLIDRRALSA LPEHAILVNV ARGGIVDTDA
LVSHLRSNRL RAAALDVTDP EPLPEDHPLW GFENVYITPH VSGHTPHYWT RVADILAENV
GRLASASDGE TPTLRNQVVP SPNP
//
