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 01-MAY-2013, entry version 114.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 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: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; 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 451 522 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
//
