(data stored in ACNUC7421 zone)

SWISSPROT: D6ZAC7_SEGRD

ID   D6ZAC7_SEGRD            Unreviewed;       372 AA.
AC   D6ZAC7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
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=Srot_0180 {ECO:0000313|EMBL:ADG96669.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96669.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96669.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96669.1; -; Genomic_DNA.
DR   RefSeq; WP_013137125.1; NC_014168.1.
DR   STRING; 640132.Srot_0180; -.
DR   EnsemblBacteria; ADG96669; ADG96669; Srot_0180.
DR   KEGG; srt:Srot_0180; -.
DR   eggNOG; ENOG4107R8H; Bacteria.
DR   eggNOG; COG1932; LUCA.
DR   HOGENOM; HOG000239573; -.
DR   KO; K00831; -.
DR   OMA; ETDVYYF; -.
DR   OrthoDB; 996960at2; -.
DR   BioCyc; SROT640132:G1GLH-184-MONOMER; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000002247; 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; D6ZAC7.
DR   SWISS-2DPAGE; D6ZAC7.
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:ADG96669.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:UP000002247};
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:ADG96669.1}.
FT   DOMAIN       19    331       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION       79     80       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
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     152    152       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     174    174       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     197    197       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   MOD_RES     198    198       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
SQ   SEQUENCE   372 AA;  39938 MW;  246C4A10EC4BAAAC CRC64;
     MTALEIPSGL KPKDGRFGSG PSKVRPEQIQ AIAASAATVL GTSHRQAPVK NVVKRVRAGL
     KELYSLPDGY EVLLGNGGAT FFWDAAAFGL IRERSLHLSF GEFSAKFASV VAKHPDRKEP
     VVVQSDPGSA PAVPDSAPAE PVDVLAWAHN ETSTGVTVPV ARPSWAKDEL VVIDGTSAAA
     GVPLDVTQTD VYYFSPQKGF ASDGGLWLAL LSPAAIERVN ELSGRWAPES ISLPTALENS
     TKDQTYNTPA VATLVLLAEQ IEWINGQGGL AWSTARTKDS SSRLYDWAEQ SEFATPFVTD
     PALRSPVVAT IDFHEEVDAA KVAKTLRENG IVDTEPYRKL GRNQLRLGVF PAVDPEDVTA
     LTKAIDWVVE RL
//

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