(data stored in ACNUC7421 zone)

SWISSPROT: Q47TD3_THEFY

ID   Q47TD3_THEFY            Unreviewed;       373 AA.
AC   Q47TD3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 113.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE            EC=2.6.1.52 {ECO:0000256|HAMAP-Rule:MF_00160};
DE   AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE            Short=PSAT {ECO:0000256|HAMAP-Rule:MF_00160};
GN   Name=serC {ECO:0000256|HAMAP-Rule:MF_00160};
GN   OrderedLocusNames=Tfu_0246 {ECO:0000313|EMBL:AAZ54284.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54284.1, 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   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine.
CC       {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00347519}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-
CC         hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate;
CC         Xref=Rhea:RHEA:16573, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58452, ChEBI:CHEBI:58538; EC=2.6.1.52;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00160,
CC         ECO:0000256|SAAS:SAAS01118610};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-
CC         phosphooxypyruvate + L-glutamate; Xref=Rhea:RHEA:14329,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:18110, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57524; EC=2.6.1.52; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00160, ECO:0000256|SAAS:SAAS01118608};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00160};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00160};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 2/3. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|SAAS:SAAS00182464}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160,
CC       ECO:0000256|SAAS:SAAS00347516}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160,
CC       ECO:0000256|SAAS:SAAS00019491}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|SAAS:SAAS00542307}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
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DR   EMBL; CP000088; AAZ54284.1; -; Genomic_DNA.
DR   RefSeq; WP_011290693.1; NC_007333.1.
DR   STRING; 269800.Tfu_0246; -.
DR   EnsemblBacteria; AAZ54284; AAZ54284; Tfu_0246.
DR   KEGG; tfu:Tfu_0246; -.
DR   eggNOG; ENOG4107R8H; Bacteria.
DR   eggNOG; COG1932; LUCA.
DR   HOGENOM; HOG000239573; -.
DR   KO; K00831; -.
DR   OMA; ETDVYYF; -.
DR   OrthoDB; 996960at2; -.
DR   BioCyc; TFUS269800:G1G4Q-251-MONOMER; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR006272; Pser_aminoTfrase_mycobac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01366; serC_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TD3.
DR   SWISS-2DPAGE; Q47TD3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00182425};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00182445, ECO:0000313|EMBL:AAZ54284.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00425508};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00182424};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Serine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00182451};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00182455, ECO:0000313|EMBL:AAZ54284.1}.
FT   DOMAIN      139    331       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      247    248       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
FT   BINDING      45     45       L-glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00160}.
FT   BINDING     103    103       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     149    149       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     172    172       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     195    195       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   MOD_RES     196    196       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
SQ   SEQUENCE   373 AA;  40147 MW;  7ECCA963DB7DBF1E CRC64;
     MTEIHIPENL LPGDGRFGCG PSKVRPEQVT ALASSGATYL GTSHRQKPVK SLVGRVRSGL
     AELFSLPDGY EVVLGNGGTT AFWDIAAHTL VRRKSQHVSF GEFSSKFAKV TQGAPWLDEP
     TVITAEPGSY APPRAEAGVD VYALTHNETS TGVATPIERI AGADEDALVL VDATSGAGGL
     PVDITQTDVY YFAPQKCFAA DGGLWIAIMS PRALERMAEI AATDRYIPAF FSLTTAVDNS
     RKDQTYNTPA VSTLLLFAEQ IEWLNKQGGL EWAARRTAES SSILYSWAEK SEYATPFVAD
     PALRSQVVGT IDFSDEVDAA KVAAVLRANG VVDTEPYRKL GRNQLRIGMF PAVEPEDVRA
     LTECIDYVVG KLG
//

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