ID SERA_MYCLE Reviewed; 528 AA.
AC O33116;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 01-MAY-2013, entry version 103.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE Short=PGDH;
DE EC=1.1.1.95;
GN Name=serA; OrderedLocusNames=ML1692; ORFNames=MLCB637.25;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3-
CC phosphonooxypyruvate + NADH.
CC -!- CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate +
CC NADH.
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; Z99263; CAB16440.1; -; Genomic_DNA.
DR EMBL; AL583923; CAC30645.1; -; Genomic_DNA.
DR PIR; T45418; T45418.
DR RefSeq; NP_302163.1; NC_002677.1.
DR ProteinModelPortal; O33116; -.
DR SMR; O33116; 3-528.
DR STRING; 272631.ML1692; -.
DR EnsemblBacteria; CAC30645; CAC30645; CAC30645.
DR GeneID; 910062; -.
DR KEGG; mle:ML1692; -.
DR PATRIC; 18056520; VBIMycLep78757_3189.
DR Leproma; ML1692; -.
DR eggNOG; COG0111; -.
DR HOGENOM; HOG000136693; -.
DR KO; K00058; -.
DR OMA; SKEPCTD; -.
DR ProtClustDB; PRK13581; -.
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 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 Serine biosynthesis.
FT CHAIN 1 528 D-3-phosphoglycerate dehydrogenase.
FT /FTId=PRO_0000076004.
FT DOMAIN 454 525 ACT.
FT NP_BIND 151 152 NAD (By similarity).
FT NP_BIND 230 232 NAD (By similarity).
FT NP_BIND 279 282 NAD (By similarity).
FT ACT_SITE 232 232 By similarity.
FT ACT_SITE 261 261 By similarity.
FT ACT_SITE 279 279 Proton donor (By similarity).
FT BINDING 171 171 NAD (By similarity).
FT BINDING 256 256 NAD (By similarity).
SQ SEQUENCE 528 AA; 54469 MW; 1A6DC60F9FB71222 CRC64;
MDLPVVLIAD KLAQSTVAAL GDQVEVRWVD GPDRTKLLAA VPEADALLVR SATTVDAEVL
AAAPKLKIVA RAGVGLDNVD VDAATARGVL VVNAPTSNIH SAAEHALALL LAASRQIAEA
DASLRAHIWK RSSFSGTEIF GKTVGVVGLG RIGQLVAARI AAFGAHVIAY DPYVAPARAA
QLGIELMSFD DLLARADFIS VHLPKTPETA GLIDKEALAK TKPGVIIVNA ARGGLVDEVA
LADAVRSGHV RAAGLDVFAT EPCTDSPLFE LSQVVVTPHL GASTAEAQDR AGTDVAESVR
LALAGEFVPD AVNVDGGVVN EEVAPWLDLV CKLGVLVAAL SDELPASLSV HVRGELASED
VEILRLSALR GLFSTVIEDA VTFVNAPALA AERGVSAEIT TGSESPNHRS VVDVRAVASD
GSVVNIAGTL SGPQLVQKIV QVNGRNFDLR AQGMNLVIRY VDQPGALGKI GTLLGAAGVN
IQAAQLSEDT EGPGATILLR LDQDVPGDVR SAIVAAVSAN KLEVVNLS
//
