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Database: UniProt
Entry: P0A545
LinkDB: P0A545
Original site: P0A545 
ID   SERA_MYCBO              Reviewed;         528 AA.
AC   P0A545; A0A1R3Y2U1; O53243; X2BME8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   05-DEC-2018, entry version 97.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=PGDH;
DE            EC=1.1.1.95 {ECO:0000250|UniProtKB:P0A9T0};
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000250|UniProtKB:P0A9T0};
DE            EC=1.1.1.399 {ECO:0000250|UniProtKB:P0A9T0};
GN   Name=serA; OrderedLocusNames=BQ2027_MB3020C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomeA.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium
RT   bovis AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-
CC       glycerate to 3-phosphonooxypyruvate, the first step of the
CC       phosphorylated L-serine biosynthesis pathway. Also catalyzes the
CC       reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
CC       {ECO:0000250|UniProtKB:P0A9T0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + 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:0000250|UniProtKB:P0A9T0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.399;
CC         Evidence={ECO:0000250|UniProtKB:P0A9T0};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; LT708304; SIU01644.1; -; Genomic_DNA.
DR   RefSeq; NP_856665.1; NC_002945.3.
DR   RefSeq; WP_003899578.1; NC_002945.4.
DR   ProteinModelPortal; P0A545; -.
DR   SMR; P0A545; -.
DR   EnsemblBacteria; CDO44288; CDO44288; Mb3020c.
DR   PATRIC; fig|233413.5.peg.3319; -.
DR   HOGENOM; HOG000136693; -.
DR   OMA; NIAGMQV; -.
DR   BioCyc; MBOV233413:G1GT4-3173-MONOMER; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001419; Chromosome.
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: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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; NAD; Oxidoreductase;
KW   Serine biosynthesis.
FT   CHAIN         1    528       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076003.
FT   DOMAIN      455    527       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     151    152       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     230    232       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     279    282       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    232    232       {ECO:0000250}.
FT   ACT_SITE    261    261       {ECO:0000250}.
FT   ACT_SITE    279    279       Proton donor. {ECO:0000250}.
FT   BINDING     171    171       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     256    256       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
SQ   SEQUENCE   528 AA;  54554 MW;  3B5696AAFD82A901 CRC64;
     MSLPVVLIAD KLAPSTVAAL GDQVEVRWVD GPDRDKLLAA VPEADALLVR SATTVDAEVL
     AAAPKLKIVA RAGVGLDNVD VDAATARGVL VVNAPTSNIH SAAEHALALL LAASRQIPAA
     DASLREHTWK RSSFSGTEIF GKTVGVVGLG RIGQLVAQRI AAFGAYVVAY DPYVSPARAA
     QLGIELLSLD DLLARADFIS VHLPKTPETA GLIDKEALAK TKPGVIIVNA ARGGLVDEAA
     LADAITGGHV RAAGLDVFAT EPCTDSPLFE LAQVVVTPHL GASTAEAQDR AGTDVAESVR
     LALAGEFVPD AVNVGGGVVN EEVAPWLDLV RKLGVLAGVL SDELPVSLSV QVRGELAAEE
     VEVLRLSALR GLFSAVIEDA VTFVNAPALA AERGVTAEIC KASESPNHRS VVDVRAVGAD
     GSVVTVSGTL YGPQLSQKIV QINGRHFDLR AQGINLIIHY VDRPGALGKI GTLLGTAGVN
     IQAAQLSEDA EGPGATILLR LDQDVPDDVR TAIAAAVDAY KLEVVDLS
//
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