ID A5EJ40_BRASB Unreviewed; 332 AA.
AC A5EJ40;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Putative phosphoglycerate dehydrogenase {ECO:0000313|EMBL:ABQ36184.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:ABQ36184.1};
GN OrderedLocusNames=BBta_4121 {ECO:0000313|EMBL:ABQ36184.1};
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ36184.1, ECO:0000313|Proteomes:UP000000246};
RN [1] {ECO:0000313|EMBL:ABQ36184.1, ECO:0000313|Proteomes:UP000000246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000494; ABQ36184.1; -; Genomic_DNA.
DR RefSeq; WP_012044185.1; NC_009485.1.
DR AlphaFoldDB; A5EJ40; -.
DR STRING; 288000.BBta_4121; -.
DR KEGG; bbt:BBta_4121; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_5; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000000246; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR029753; D-isomer_DH_CS.
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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 12..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 119..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 35576 MW; 1E2AA5C2505CE2AA CRC64;
MTTRTATNKN KILVTESFSA KGRALLTARD DVEMIEFPNM ISAADFSALL KSHAPVHGVA
LGATRFGEPE LLAAGDMKVV TRIGVGFDAV DVPALSKHKV PLMVAGTANS PSVAEQALFM
MLTLAKRANE MHAMVRDGTW GSRLGVLPFD LYGKTVLIIG FGRIGTRTAK RCQAMEMQVL
VYDPYKPAAD ITAAGCEPVA DLDAALPRAD FVSIHCPKTP ETIGLFNAAR LRLMKPTAYL
INTARGGLID EAALYDALSS RRLAGAGLDV FEQEPPPVGH ALHALPNVIM APHVAGVTRE
AVDRMSEQTA RNILSVLDGD PIRQNVINQD VL
//
