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Database: UniProt
Entry: A0A085HQH3_9GAMM
LinkDB: A0A085HQH3_9GAMM
Original site: A0A085HQH3_9GAMM 
ID   A0A085HQH3_9GAMM        Unreviewed;       410 AA.
AC   A0A085HQH3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 19.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KFC98218.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:KFC98218.1};
DE            EC=1.1.1.95 {ECO:0000313|EMBL:KFC98218.1};
GN   ORFNames=GLGR_0110 {ECO:0000313|EMBL:KFC98218.1};
OS   Leminorella grimontii ATCC 33999 = DSM 5078.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Leminorella.
OX   NCBI_TaxID=1005999 {ECO:0000313|EMBL:KFC98218.1, ECO:0000313|Proteomes:UP000028624};
RN   [1] {ECO:0000313|EMBL:KFC98218.1, ECO:0000313|Proteomes:UP000028624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33999 {ECO:0000313|EMBL:KFC98218.1,
RC   ECO:0000313|Proteomes:UP000028624};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction
RT   of the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFC98218.1}.
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DR   EMBL; JMPN01000002; KFC98218.1; -; Genomic_DNA.
DR   RefSeq; WP_027275582.1; NZ_JMPN01000002.1.
DR   ProteinModelPortal; A0A085HQH3; -.
DR   EnsemblBacteria; KFC98218; KFC98218; GLGR_0110.
DR   PATRIC; fig|1005999.4.peg.111; -.
DR   Proteomes; UP000028624; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR002912; ACT_dom.
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   InterPro; IPR029015; PGDH_2.
DR   PANTHER; PTHR10996:SF165; PTHR10996:SF165; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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   Complete proteome {ECO:0000313|Proteomes:UP000028624};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW   ECO:0000313|EMBL:KFC98218.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028624}.
FT   DOMAIN      341    410       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   410 AA;  44531 MW;  796739C0678792D4 CRC64;
     MVKVSLEKER IKFLLVEGVH QSAVDSLRAA GYHNIEYHKG ALSDDELKEA IRDAHFVGIR
     SRTHLSEDIL SAAEKLVAIG CFCIGTNQVD LAAAAKRGVP VFNAPFSNTR SVAEMVLGEI
     LLLLRRIPEA NAKAHRNEWC KLAVGCFEAR GKNLGIIGYG HIGTQLGILA ESIGMNVMFY
     DIENKLPLGN AQQVHHLSDL LNRSDVVSLH VPETASTKNM MGTKELAMMK PGSILINASR
     GTVVDIPALC DVLESKHLAG AALDVFPVEP ATNTDPFESP LCAFDNVLLT PHIGGSTQEA
     QANIGMEVAG KLTKYSDNGS TLSAVNFPEV SLPAPQEHVS RLLHIHENRP GVLNQINQIF
     AEEGINIAAQ FLQTNNEIGY VVIDVETDRA DEALEHMKSI QGTVRARLLF
//
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