GenomeNet

Database: UniProt
Entry: E9CWY2_COCPS
LinkDB: E9CWY2_COCPS
Original site: E9CWY2_COCPS 
ID   E9CWY2_COCPS            Unreviewed;       589 AA.
AC   E9CWY2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   07-NOV-2018, entry version 32.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   ORFNames=CPSG_01965 {ECO:0000313|EMBL:EFW21808.1};
OS   Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN   [1] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
RN   [2] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J.,
RA   Gardner M.J., Kirkland T.N., Taylor J.W., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA   Mehta T., Neiman D., Park D., Pearson M., Richards J., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Coccidioides posadasii strain Silveira.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3-
CC       phosphonooxypyruvate + NADH. {ECO:0000256|RuleBase:RU363003}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000256|RuleBase:RU363003}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU363003}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; GL636487; EFW21808.1; -; Genomic_DNA.
DR   ProteinModelPortal; E9CWY2; -.
DR   EnsemblFungi; EFW21808; EFW21808; CPSG_01965.
DR   OrthoDB; EOG092C11JF; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000002497; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002497};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002497};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN       38    225       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   589 AA;  61739 MW;  EF1AAF703A3985C4 CRC64;
     MPLLSSEGPR PKVLVPEKLS PDGLALLRAS TDVHEKMGLT PEELLTIISD YDALVVRSET
     KVTDEVLQTA KNLKVVARAG VGVDNVDVDT ATKLGIVVVN SPAGNVGAAA EHTIALMLAT
     ARKISHACSS LKGDKWERSK FVGVEVKGKT LGIIGLGKVG MIVARLAKGL GMNVNAMDPY
     ASEAVASSAS ITLVSSLSEL LPTVDFLTIH TPLIASTKGM ISTAELAKMK PGARILNVAR
     GGTIDEIALL DALESGHIAG AGIDVFTSEP PKPGSSASRL IAHPNVVATP HLGASTVEAQ
     ENVSIDVCEQ VLQILGGALP RSAVNAPLIL PEEYKKLQPF VRLVEKMGSL YTQHYSSSTS
     FDANRSTFDL IYEGDIAGIN NTKPLFAAFI KGLMATISST NVSIVNAELV ARERGIVVNE
     QRSRDPSTHS YSSLVTLVAR PPSRAPSRAP GVAETQRPLQ NPHQQIISGT CSGSQIIISR
     LGRFATSFVP EGRLLICHNY DSPGKIGVVG SILGKQDVNI NFMSVAPISK QLLEEDAAKG
     QSQKGYGGNG NGIHTEALML LGVDGPVSQD VVTALVDSGG VLSASLVSL
//
DBGET integrated database retrieval system