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Database: UniProt
Entry: I4F2K5_9ACTN
LinkDB: I4F2K5_9ACTN
Original site: I4F2K5_9ACTN 
ID   I4F2K5_9ACTN            Unreviewed;       320 AA.
AC   I4F2K5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   20-JUN-2018, entry version 30.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CCH89868.1};
DE            EC=1.1.1.95 {ECO:0000313|EMBL:CCH89868.1};
GN   Name=serA {ECO:0000313|EMBL:CCH89868.1};
GN   OrderedLocusNames=MODMU_4485 {ECO:0000313|EMBL:CCH89868.1};
OS   Modestobacter marinus.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Modestobacter.
OX   NCBI_TaxID=477641 {ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH89868.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC501 {ECO:0000313|EMBL:CCH89868.1,
RC   ECO:0000313|Proteomes:UP000006461};
RX   PubMed=22887672; DOI=10.1128/JB.01029-12;
RA   Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA   Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA   Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I.,
RA   Gtari M.;
RT   "Genome sequence of radiation-resistant Modestobacter marinus strain
RT   BC501, a representative Actinobacterium that thrives on calcareous
RT   stone surfaces.";
RL   J. Bacteriol. 194:4773-4774(2012).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FO203431; CCH89868.1; -; Genomic_DNA.
DR   RefSeq; WP_014742432.1; NC_017955.1.
DR   ProteinModelPortal; I4F2K5; -.
DR   EnsemblBacteria; CCH89868; CCH89868; MODMU_4485.
DR   KEGG; mmar:MODMU_4485; -.
DR   PATRIC; fig|477641.3.peg.4194; -.
DR   OrthoDB; POG091H068U; -.
DR   BioCyc; MMAR477641:MODMU_RS21185-MONOMER; -.
DR   Proteomes; UP000006461; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 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   Complete proteome {ECO:0000313|Proteomes:UP000006461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW   ECO:0000313|EMBL:CCH89868.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT   DOMAIN       54    317       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      120    286       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
SQ   SEQUENCE   320 AA;  33605 MW;  E37088A562A4628A CRC64;
     MPDTAPAAPV LDLGADETLH VLVPSRALAE AVEAVSPRIR AHRFDPADGV PTGEAAEARV
     MVPRGGGELT AEVWDALPRL RLVQLMSAGA EKFVGRLPER VVLCNARGAH TPATAEWAVA
     ATLAAQRGLP HFTRLQEAGR WEMRTDHSLV GAKVLIVGAG DIGRTIGRMM AGFDVDVTWV
     ARTAREGVHA FGDLPDLLPD ADVVVLIVPV TPETTGMVDA GFLAAMKDDA LLVNAARGVV
     VDTDALLAEL TAGRLRAALD VTEPEPLPEG HPLWSAPGLL LTPHVAGAVP DTNARATAAV
     VEQLQRVLAG QPLENVVADY
//
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