ID   A0A5M9ZNU8_9BIFI        Unreviewed;       381 AA.
AC   A0A5M9ZNU8;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-NOV-2024, entry version 21.
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; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; 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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(phosphooxy)-L-threonine + 2-oxoglutarate = (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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001607, ECO:0000256|HAMAP-
CC         Rule:MF_00160};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-serine + 2-oxoglutarate = 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|ARBA:ARBA00001871, ECO:0000256|HAMAP-
CC         Rule:MF_00160};
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|ARBA:ARBA00005099,
CC       ECO:0000256|HAMAP-Rule:MF_00160}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006904, ECO:0000256|HAMAP-Rule:MF_00160}.
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   AlphaFoldDB; A0A5M9ZNU8; -.
DR   OrthoDB; 975012at2; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000412028; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:TreeGrafter.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:TreeGrafter.
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:0004760; F:serine-pyruvate transaminase activity; IEA:TreeGrafter.
DR   GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IEA:TreeGrafter.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01366; serC_3; 1.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00160};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00160}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00160};
KW   Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW   Rule:MF_00160};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299, ECO:0000256|HAMAP-
KW   Rule:MF_00160};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000313|EMBL:KAA8829311.1}.
FT   DOMAIN          139..345
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         46
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         80..81
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         104
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         150
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         174
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         197
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         255..256
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
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
//