ID Q3BZQ9_XANC5 Unreviewed; 330 AA.
AC Q3BZQ9;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CAJ21654.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:CAJ21654.1};
GN Name=serA {ECO:0000313|EMBL:CAJ21654.1};
GN OrderedLocusNames=XCV0023 {ECO:0000313|EMBL:CAJ21654.1};
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN [1] {ECO:0000313|EMBL:CAJ21654.1, ECO:0000313|Proteomes:UP000007069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10 {ECO:0000313|EMBL:CAJ21654.1,
RC ECO:0000313|Proteomes:UP000007069};
RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneicker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ21654.1; -; Genomic_DNA.
DR RefSeq; WP_011345784.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BZQ9; -.
DR STRING; 456327.BJD11_22830; -.
DR GeneID; 63989250; -.
DR KEGG; xcv:XCV0023; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_6; -.
DR Proteomes; UP000007069; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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}.
FT DOMAIN 38..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 35324 MW; 132F24211FB81F3E CRC64;
MRIVVPDDYQ GAVAQLPCLQ QMQGHPVQVL GALGAELDAR AASLADADAL VLIRERTRVD
AALLQRLPRL KLISQTGRVG AHVDVAACTA SGVAVAEGVG SPVAPAELTW ALILSASRRL
TDYQHALQQG RWQALGDPGL GRVLHGRTLG IWSYGRIGQR VASFGRAFGM QVLVWGGPAS
CAQAARDGFA VAGSREELFE RSDVLSLHRR LTAQTRHDIT AQDLARMRAD ALLVNTSRAE
LIAPGALLAA LDAGRPAQAA LDVFEHEPVL DPRDPLLRHA RVLATPHLGY VERDSYALYF
AAAFDNVLAF AAGTPRNLVN PEVLATTQRV
//
