ID A3JQU0_9RHOB Unreviewed; 371 AA.
AC A3JQU0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:EBA04130.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:EBA04130.1};
GN ORFNames=RB2150_06503 {ECO:0000313|EMBL:EBA04130.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA04130.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA04130.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA04130.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
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:EBA04130.1}.
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DR EMBL; AAXZ01000002; EBA04130.1; -; Genomic_DNA.
DR AlphaFoldDB; A3JQU0; -.
DR eggNOG; COG1052; Bacteria.
DR Proteomes; UP000004731; Unassembled WGS sequence.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05301; GDH; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000004731};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..371
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002654930"
FT DOMAIN 50..365
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 155..334
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 371 AA; 40944 MW; A42B28C4DF1CBD03 CRC64;
MRPIFVVIFV SARFFLTSAC SMLRLGAVCQ KERTEKSDPS MNKPHKQLSV VVTRRLPEPI
ERRLAELFDV NLRESDAPMT RDELVSAMKT ADILVPTITD TIDAEMLAQA GDQLKLLANY
GAGIDHINVD AARARGVLVS NTPGVLTEDT ADMTMALILA VTRRIPDGLA LMQTGQWEGW
SPTALMGGRI AGRNLGILGM GRIGQAVARR ASAFGMNVHY HNRHRLRTET EAALNATYWD
SLDQMVARTD VLSVNCPHTP ATFHLMNARR LKLMKETAVI VNTSRGEVID ENALTRMLRS
GEISGAGLDV YEKGREVNPR LRELKNVVLL PHMGSATVEA RMEMGEKVLI NIKTFDDGHR
PPDLVLPGMD D
//
