ID   A0A5M9ZNU8_9BIFI        Unreviewed;       381 AA.
AC   A0A5M9ZNU8;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   17-JUN-2020, entry version 3.
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   ORFNames=EMO89_08135 {ECO:0000313|EMBL:KAA8829311.1};
OS   Bifidobacterium tissieri.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1630162 {ECO:0000313|EMBL:KAA8829311.1, ECO:0000313|Proteomes:UP000412028};
RN   [1] {ECO:0000313|EMBL:KAA8829311.1, ECO:0000313|Proteomes:UP000412028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RST7 {ECO:0000313|EMBL:KAA8829311.1,
RC   ECO:0000313|Proteomes:UP000412028};
RX   PubMed=31585749;
RA   Modesto M., Satti M., Watanabe K., Puglisi E., Morelli L., Huang C.-H.,
RA   Liou J.-S., Miyashita M., Tamura T., Saito S., Mori K., Huang L.,
RA   Sciavilla P., Sandri C., Spiezio C., Vitali F., Cavalieri D.,
RA   Perpetuini G., Tofalo R., Bonetti A., Arita M., Mattarelli P.;
RT   "Characterization of Bifidobacterium species in feaces of the Egyptian
RT   fruit bat: Description of B. vespertilionis sp. nov. and B. rousetti sp.
RT   nov.";
RL   Syst. Appl. Microbiol. 42:126017-126017(2019).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|SAAS:SAAS00347519}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC         oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC         ChEBI:CHEBI:58538; EC=2.6.1.52; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00160, ECO:0000256|SAAS:SAAS01118610};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC         L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00160,
CC         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 from
CC       3-phospho-D-glycerate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00160,
CC       ECO:0000256|SAAS:SAAS00182464}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC       {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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAA8829311.1}.
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DR   EMBL; RZUI01000010; KAA8829311.1; -; Genomic_DNA.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000412028; Unassembled WGS sequence.
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;
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:KAA8829311.1};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160, 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   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:KAA8829311.1}.
FT   DOMAIN          137..348
FT                   /note="Aminotran_5"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          80..81
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   REGION          255..256
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         46
FT                   /note="L-glutamate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         104
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         150
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         174
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         197
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
SQ   SEQUENCE   381 AA;  41350 MW;  5EE7D36AF2B5D252 CRC64;
     MIEPVKIPMS MLPEDGRFGC GPSKIRHKQV KALTEAGYNL LGTSHRQAPV KHVVASIREG
     LSDYFSIPEG WQIALGNGGA SAFWEVACAS LISRRAAFGT YGSFSGKFAT SAAKAPFLEE
     PVIYKAEYGS CAIPQYTDDV DAYCWAQNET STGVMAPVHR VPGSVEQGAL TLIDATSGAG
     GLPIDISQTD AYYFSPQKVF GSDGGLWFAI LSPDAIKRAE DVEKSAELEG ARRWVPPFLS
     LTQALANSRK DQTLNTPAIS TLVLMDEQVR WLNEHGGLTW AQERCAKSAD ILYTWAEKSD
     YATPFVSDPS LRSNVVVTID LDDSIKAAAV VAVLRDNGIV DTSGYRKLGR NQLRIGVFPS
     VKPSDVEALT YCIDYVVEHL Q
//