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Database: UniProt
Entry: P35136
LinkDB: P35136
Original site: P35136 
ID   SERA_BACSU              Reviewed;         525 AA.
AC   P35136; O32011;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   13-NOV-2013, entry version 117.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=PGDH;
DE            EC=1.1.1.95;
GN   Name=serA; OrderedLocusNames=BSU23070;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / VKM B-501;
RX   PubMed=8760912;
RA   Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA   Serror P.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between
RT   the serA and kdg loci cloned in a yeast artificial chromosome.";
RL   Microbiology 142:2005-2016(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 157-158.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-525.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / VKM B-501;
RX   PubMed=7934829;
RA   Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT   "The organization of the Bacillus subtilis 168 chromosome region
RT   between the spoVA and serA genetic loci, based on sequence data.";
RL   Mol. Microbiol. 10:385-395(1993).
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3-
CC       phosphonooxypyruvate + NADH.
CC   -!- CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate +
CC       NADH.
CC   -!- ENZYME REGULATION: In bacteria displays feedback inhibition by L-
CC       serine.
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.
CC   -!- SIMILARITY: Contains 1 ACT domain.
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DR   EMBL; L47648; AAC83943.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14239.2; -; Genomic_DNA.
DR   EMBL; L09228; AAA67502.1; -; Genomic_DNA.
DR   PIR; C69705; C69705.
DR   RefSeq; NP_390188.2; NC_000964.3.
DR   ProteinModelPortal; P35136; -.
DR   SMR; P35136; 1-524.
DR   STRING; 224308.BSU23070; -.
DR   PaxDb; P35136; -.
DR   EnsemblBacteria; CAB14239; CAB14239; BSU23070.
DR   GeneID; 938964; -.
DR   KEGG; bsu:BSU23070; -.
DR   PATRIC; 18976431; VBIBacSub10457_2406.
DR   GenoList; BSU23070; -.
DR   eggNOG; COG0111; -.
DR   HOGENOM; HOG000136693; -.
DR   KO; K00058; -.
DR   OrthoDB; EOG6VXFC3; -.
DR   ProtClustDB; PRK13581; -.
DR   BioCyc; BSUB:BSU23070-MONOMER; -.
DR   UniPathway; UPA00135; UER00196.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
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; 3.40.50.720; -; 2.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR006236; D-3-Phosphoglycerate_DH.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR10996:SF20; PTHR10996:SF20; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 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   Reference proteome; Serine biosynthesis.
FT   CHAIN         1    525       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000075998.
FT   DOMAIN      452    524       ACT.
FT   NP_BIND     148    149       NAD (By similarity).
FT   NP_BIND     227    229       NAD (By similarity).
FT   NP_BIND     276    279       NAD (By similarity).
FT   ACT_SITE    229    229       By similarity.
FT   ACT_SITE    258    258       By similarity.
FT   ACT_SITE    276    276       Proton donor (By similarity).
FT   BINDING     168    168       NAD (By similarity).
FT   BINDING     200    200       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     253    253       NAD (By similarity).
FT   CONFLICT    157    158       AR -> RG (in Ref. 1; AAC83943 and 4;
FT                                AAA67502).
SQ   SEQUENCE   525 AA;  57129 MW;  9B026BF481FBC1D2 CRC64;
     MFRVLVSDKM SNDGLQPLIE SDFIEIVQKN VADAEDELHT FDALLVRSAT KVTEDLFNKM
     TSLKIVGRAG VGVDNIDIDE ATKHGVIVIN APNGNTISTA EHTFAMISSL MRHIPQANIS
     VKSREWNRTA YVGSELYGKT LGIVGLGRIG SEIAQRARAF GMTVHVFDPF LTEERAKKIG
     VNSRTFEEVL ESADIITVHT PLTKETKGLL NKETIAKTKK GVRLINCARG GIIDEAALLE
     ALENGHVAGA ALDVFEVEPP VDNKLVDHPL VIATPHLGAS TKEAQLNVAA QVSEEVLQFA
     KGLPVMSAIN LPAMTKDEFA KIKPYHQIAG KIGSLVSQCM KEPVQDVAIQ YEGTIAKLET
     SFITKALLSG FLKPRVDSTV NEVNAGGVAK ERGISFSEKI SSSESGYDNC ISVKVTGDRS
     TFTVTATYIP HFGERIVEIN GFNIDFYPTG HLVYIQHQDT TGVIGRVGRI LGDNDINIAT
     MQVGRKEKGG EAIMMLSFDR HLEDKIVKEL TNVPDIVSVK LIDLP
//
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