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Database: UniProt
Entry: I8UIA9_9BACI
LinkDB: I8UIA9_9BACI
Original site: I8UIA9_9BACI 
ID   I8UIA9_9BACI            Unreviewed;       521 AA.
AC   I8UIA9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   18-SEP-2019, entry version 36.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   ORFNames=A374_03244 {ECO:0000313|EMBL:EIT86553.1};
OS   Fictibacillus macauensis ZFHKF-1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT86553.1, ECO:0000313|Proteomes:UP000004080};
RN   [1] {ECO:0000313|EMBL:EIT86553.1, ECO:0000313|Proteomes:UP000004080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT86553.1,
RC   ECO:0000313|Proteomes:UP000004080};
RX   PubMed=22887677; DOI=10.1128/JB.01049-12;
RA   Cai L., Zhang T.;
RT   "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming
RT   Bacterium.";
RL   J. Bacteriol. 194:4780-4780(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000256|RuleBase:RU363003};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000256|RuleBase:RU363003}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU363003}.
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:EIT86553.1}.
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DR   EMBL; AKKV01000020; EIT86553.1; -; Genomic_DNA.
DR   RefSeq; WP_007200748.1; NZ_AKKV01000020.1.
DR   STRING; 1196324.A374_03244; -.
DR   EnsemblBacteria; EIT86553; EIT86553; A374_03244.
DR   PATRIC; fig|1196324.3.peg.657; -.
DR   OrthoDB; 1638924at2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000004080; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR029009; ASB_dom_sf.
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; IPR006236; PGDH.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004080};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004080};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN      449    521       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   521 AA;  56445 MW;  08C37F318A6C2014 CRC64;
     MFQVLATDSI AKEGLTVLEN DSNVSVIYGS VDEAPTTIDA LIVRSATQVT AELLAQFPSL
     KIVARAGVGT DNIDIDAASK RGVLVINAPD GNTISTAEHT FAMMMSLLRR IPQANHSILE
     GKWNRSSFKG SELLGKVVGI IGLGRIGTEL AKRLKAFQTD VIVFDPFLTE ERAKSLHVQS
     VSLDALLTTS DIITVHTPLT KETKNLLSKE NLAKTKKGVY FINCARGGIY DEEALYDCLK
     SGHAAGCALD VFIEEPATNN KLVHLPNVVA TPHIAASTTE AQLNVAVGVA QEIHGFFNGK
     TVKNAINLPS VPGEELQKIM PFHELAKLSG QILSQVFTSG VKEIRLSFSG TITDHDTGLV
     TRGLLSGFLM QRVDRYVNDI NAPLIAKEQG FTISETSRSE TYGYENCLQV EVIGEHDSFS
     LQSTYIPGYG PRIVNMNGYV TDFMPEGAMI YIEHVDKPGV IGNVGKLLGD LDINIASMQV
     GRKKAGGEAI MLLTFDHELT KETEMKIRQL KDVVSAKSLA L
//
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