(data stored in SCRATCH zone)

SWISSPROT: Q47SB5_THEFY

ID   Q47SB5_THEFY            Unreviewed;       528 AA.
AC   Q47SB5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 105.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   OrderedLocusNames=Tfu_0614 {ECO:0000313|EMBL:AAZ54652.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54652.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={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}.
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DR   EMBL; CP000088; AAZ54652.1; -; Genomic_DNA.
DR   RefSeq; WP_011291061.1; NC_007333.1.
DR   STRING; 269800.Tfu_0614; -.
DR   EnsemblBacteria; AAZ54652; AAZ54652; Tfu_0614.
DR   KEGG; tfu:Tfu_0614; -.
DR   eggNOG; ENOG4108JQ1; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136693; -.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; TFUS269800:G1G4Q-625-MONOMER; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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; 3.30.1330.90; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
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   Pfam; PF01842; ACT; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 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;
DR   PRODOM; Q47SB5.
DR   SWISS-2DPAGE; Q47SB5.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363003,
KW   ECO:0000313|EMBL:AAZ54652.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN      455    528       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   528 AA;  55854 MW;  4EF36A20F43142D6 CRC64;
     MPKPVVLVAE ELSPAGIALL EEDFEVRHVN GADRSQLLPA LAGVDALIVR SATKVDAEVL
     AAAPSLKVVA RAGVGLDNVD VEAATKAGVL VVNAPTSNII SAAEQAINLL LATARNTAAA
     HAALVRGEWK RSKYTGVELY DKTVGIVGLG RIGVLVAQRL QAFGTKLIAY DPFVQPARAA
     QLGVELVELD ELLERSDFIT IHLPKTKDTI GLIGEEELRK VKPTVRIINA ARGGIVDETA
     LYHALKEGRV AGAGLDVFAK EPCTDSPLFE LENVVVAPHL GASTHEAQEK AGTQVARSVK
     LALAGEFVPD AVNIQGKGVA EDIKPGLPLT EKLGRILAAL ADGAITRVEV EVRGEIVAHD
     VKVIELAALK GLFTDIVEEA VTYVNAPLVA KERGIEVSLT TEEESPDWRN VITVRAILSD
     GQRVSVSGTL TGPRQLEKLV EVNGYTMEIA PSEHMAFFSY HDRPGVVGVV GQLLGQAQVN
     IAGMQVSRDK EGGAALIALT VDSAIPDETL ETISKEIGAE ISRVDLVD
//

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