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Database: UniProt
Entry: W4HGK7_9RHOB
LinkDB: W4HGK7_9RHOB
Original site: W4HGK7_9RHOB 
ID   W4HGK7_9RHOB            Unreviewed;       324 AA.
AC   W4HGK7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:ETW11528.1};
GN   ORFNames=ATO8_16475 {ECO:0000313|EMBL:ETW11528.1};
OS   Roseivivax marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1379903 {ECO:0000313|EMBL:ETW11528.1, ECO:0000313|Proteomes:UP000019063};
RN   [1] {ECO:0000313|EMBL:ETW11528.1, ECO:0000313|Proteomes:UP000019063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s10s {ECO:0000313|EMBL:ETW11528.1,
RC   ECO:0000313|Proteomes:UP000019063};
RX   PubMed=24567080; DOI=10.1007/s10482-014-0140-5;
RA   Li G., Lai Q., Liu X., Sun F., Shao Z.;
RT   "Roseivivax atlanticus sp. nov., isolated from surface seawater of the
RT   Atlantic Ocean.";
RL   Antonie Van Leeuwenhoek 105:863-869(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:ETW11528.1}.
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DR   EMBL; AQQW01000011; ETW11528.1; -; Genomic_DNA.
DR   RefSeq; WP_043846084.1; NZ_AQQW01000011.1.
DR   AlphaFoldDB; W4HGK7; -.
DR   STRING; 1379903.ATO8_16475; -.
DR   PATRIC; fig|1317118.6.peg.3389; -.
DR   eggNOG; COG0111; Bacteria.
DR   Proteomes; UP000019063; 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; cd12169; PGDH_like_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; 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:UP000019063}.
FT   DOMAIN          22..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   324 AA;  34654 MW;  97F615E0478AEA75 CRC64;
     MKVHILDDYF DTLRGLPSFA ALADHDVTVW TDKPATEAEL AERLQDADVL ILFRDRTEIT
     ESLVSRLPNL KLVAMRSAYP HVDVDALTRA GVLFCSNMHA GSPSTAAAEL TFLLILAAAR
     RLPEQVASIR AGHWQAGVGR SLSGRTLGLY GYGRLGKAVA GYARAFGMNV VWWASEEGRA
     RAAADGETVA TSRDAFFAEP DVISIHKRLN AATRGEITAD DLAAMRADAI FVNTSRAGLV
     APGALVAALD AGRPGLAAVD VFDTEPVTDP DDPVVSHPRV LPTPHIGFVT EDELDTQFAD
     IYAIVTAYAD GDPVHVINPE ARAS
//
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