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Database: UniProt
Entry: P9WNX3
LinkDB: P9WNX3
Original site: P9WNX3 
ID   SERA_MYCTU              Reviewed;         528 AA.
AC   P9WNX3; L0TBH1; O53243; P0A544;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   13-FEB-2019, entry version 34.
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=Rv2996c; ORFNames=MTV012.10;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium
RT   tuberculosis through an interactome, reactome and genome-scale
RT   structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AL123456; CCP45801.1; -; Genomic_DNA.
DR   PIR; G70854; G70854.
DR   RefSeq; WP_003899578.1; NZ_NVQJ01000041.1.
DR   RefSeq; YP_177916.1; NC_000962.3.
DR   PDB; 1YGY; X-ray; 2.30 A; A/B=2-528.
DR   PDB; 3DC2; X-ray; 2.70 A; A/B=2-528.
DR   PDB; 3DDN; X-ray; 2.40 A; A/B=2-528.
DR   PDBsum; 1YGY; -.
DR   PDBsum; 3DC2; -.
DR   PDBsum; 3DDN; -.
DR   ProteinModelPortal; P9WNX3; -.
DR   SMR; P9WNX3; -.
DR   IntAct; P9WNX3; 1.
DR   STRING; 83332.Rv2996c; -.
DR   PaxDb; P9WNX3; -.
DR   PRIDE; P9WNX3; -.
DR   EnsemblBacteria; CCP45801; CCP45801; Rv2996c.
DR   GeneID; 887154; -.
DR   KEGG; mtu:Rv2996c; -.
DR   TubercuList; Rv2996c; -.
DR   eggNOG; ENOG4108JQ1; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   PhylomeDB; P9WNX3; -.
DR   BioCyc; MTBH37RV:G185E-7253-MONOMER; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005618; C:cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IDA:MTBBASE.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IDA:MTBBASE.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Complete proteome; NAD;
KW   Oxidoreductase; Reference proteome; Serine biosynthesis.
FT   CHAIN         1    528       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076005.
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}.
FT   STRAND        5      8       {ECO:0000244|PDB:1YGY}.
FT   HELIX        14     17       {ECO:0000244|PDB:1YGY}.
FT   STRAND       22     28       {ECO:0000244|PDB:1YGY}.
FT   HELIX        34     40       {ECO:0000244|PDB:1YGY}.
FT   HELIX        41     43       {ECO:0000244|PDB:1YGY}.
FT   STRAND       45     49       {ECO:0000244|PDB:1YGY}.
FT   STRAND       51     53       {ECO:0000244|PDB:1YGY}.
FT   HELIX        57     61       {ECO:0000244|PDB:1YGY}.
FT   STRAND       68     74       {ECO:0000244|PDB:1YGY}.
FT   HELIX        81     86       {ECO:0000244|PDB:1YGY}.
FT   STRAND       90     92       {ECO:0000244|PDB:1YGY}.
FT   TURN         95     98       {ECO:0000244|PDB:3DDN}.
FT   HELIX        99    114       {ECO:0000244|PDB:1YGY}.
FT   HELIX       117    125       {ECO:0000244|PDB:1YGY}.
FT   HELIX       131    133       {ECO:0000244|PDB:1YGY}.
FT   STRAND      143    147       {ECO:0000244|PDB:1YGY}.
FT   HELIX       151    161       {ECO:0000244|PDB:1YGY}.
FT   TURN        162    164       {ECO:0000244|PDB:1YGY}.
FT   STRAND      166    170       {ECO:0000244|PDB:1YGY}.
FT   HELIX       176    182       {ECO:0000244|PDB:1YGY}.
FT   HELIX       189    195       {ECO:0000244|PDB:1YGY}.
FT   STRAND      197    201       {ECO:0000244|PDB:1YGY}.
FT   TURN        207    211       {ECO:0000244|PDB:1YGY}.
FT   HELIX       215    218       {ECO:0000244|PDB:1YGY}.
FT   STRAND      226    229       {ECO:0000244|PDB:1YGY}.
FT   HELIX       238    246       {ECO:0000244|PDB:1YGY}.
FT   STRAND      248    250       {ECO:0000244|PDB:1YGY}.
FT   STRAND      252    257       {ECO:0000244|PDB:1YGY}.
FT   STRAND      259    262       {ECO:0000244|PDB:1YGY}.
FT   HELIX       267    270       {ECO:0000244|PDB:1YGY}.
FT   STRAND      274    276       {ECO:0000244|PDB:1YGY}.
FT   HELIX       285    303       {ECO:0000244|PDB:1YGY}.
FT   TURN        321    325       {ECO:0000244|PDB:1YGY}.
FT   HELIX       326    339       {ECO:0000244|PDB:1YGY}.
FT   STRAND      341    343       {ECO:0000244|PDB:1YGY}.
FT   STRAND      346    354       {ECO:0000244|PDB:1YGY}.
FT   HELIX       355    358       {ECO:0000244|PDB:1YGY}.
FT   HELIX       362    372       {ECO:0000244|PDB:1YGY}.
FT   HELIX       374    376       {ECO:0000244|PDB:1YGY}.
FT   HELIX       386    393       {ECO:0000244|PDB:1YGY}.
FT   STRAND      396    403       {ECO:0000244|PDB:1YGY}.
FT   STRAND      406    417       {ECO:0000244|PDB:1YGY}.
FT   STRAND      423    431       {ECO:0000244|PDB:1YGY}.
FT   TURN        432    435       {ECO:0000244|PDB:1YGY}.
FT   STRAND      436    442       {ECO:0000244|PDB:1YGY}.
FT   STRAND      445    451       {ECO:0000244|PDB:1YGY}.
FT   STRAND      453    461       {ECO:0000244|PDB:1YGY}.
FT   HELIX       466    476       {ECO:0000244|PDB:1YGY}.
FT   STRAND      481    488       {ECO:0000244|PDB:1YGY}.
FT   STRAND      490    493       {ECO:0000244|PDB:1YGY}.
FT   STRAND      495    503       {ECO:0000244|PDB:1YGY}.
FT   HELIX       507    517       {ECO:0000244|PDB:1YGY}.
FT   STRAND      519    526       {ECO:0000244|PDB:1YGY}.
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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