SERC_CAMJE
ID SERC_CAMJE Reviewed; 358 AA.
AC Q9PIH3; Q0PBI3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE EC=2.6.1.52 {ECO:0000255|HAMAP-Rule:MF_00160};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE Short=PSAT {ECO:0000255|HAMAP-Rule:MF_00160};
GN Name=serC {ECO:0000255|HAMAP-Rule:MF_00160}; OrderedLocusNames=Cj0326;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000255|HAMAP-
CC Rule:MF_00160}.
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:0000255|HAMAP-Rule:MF_00160};
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:0000255|HAMAP-
CC Rule:MF_00160};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00160};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00160}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00160}.
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DR EMBL; AL111168; CAL34477.1; -; Genomic_DNA.
DR PIR; B81452; B81452.
DR RefSeq; WP_002858670.1; NC_002163.1.
DR RefSeq; YP_002343764.1; NC_002163.1.
DR PDB; 3M5U; X-ray; 2.15 A; A/B=1-358.
DR PDBsum; 3M5U; -.
DR AlphaFoldDB; Q9PIH3; -.
DR SMR; Q9PIH3; -.
DR IntAct; Q9PIH3; 19.
DR STRING; 192222.Cj0326; -.
DR PaxDb; Q9PIH3; -.
DR PRIDE; Q9PIH3; -.
DR EnsemblBacteria; CAL34477; CAL34477; Cj0326.
DR GeneID; 904650; -.
DR KEGG; cje:Cj0326; -.
DR PATRIC; fig|192222.6.peg.318; -.
DR eggNOG; COG1932; Bacteria.
DR HOGENOM; CLU_034866_0_2_7; -.
DR OMA; GYRASMY; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000000799; 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 CDD; cd00611; PSAT_like; 1.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PTHR43247; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Pyridoxal phosphate; Pyridoxine biosynthesis; Reference proteome;
KW Serine biosynthesis; Transferase.
FT CHAIN 1..358
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150161"
FT BINDING 41
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 75..76
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 100
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 167
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 190
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 233..234
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3M5U"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:3M5U"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3M5U"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:3M5U"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:3M5U"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 256..275
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:3M5U"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:3M5U"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:3M5U"
FT HELIX 340..357
FT /evidence="ECO:0007829|PDB:3M5U"
SQ SEQUENCE 358 AA; 40486 MW; F280E35A5ABB5445 CRC64;
MRKINFSAGP STLPLEILEQ AQKELCDYQG RGYSIMEISH RTKVFEEVHF GAQEKAKKLY
ELNDDYEVLF LQGGASLQFA MIPMNLALNG VCEYANTGVW TKKAIKEAQI LGVNVKTVAS
SEESNFDHIP RVEFSDNADY AYICSNNTIY GTQYQNYPKT KTPLIVDASS DFFSRKVDFS
NIALFYGGVQ KNAGISGLSC IFIRKDMLER SKNKQIPSML NYLTHAENQS LFNTPPTFAI
YMFNLEMDWL LNQGGLDKVH EKNSQKATML YECIDLSNGF YKGHADKKDR SLMNVSFNIA
KNKDLEPLFV KEAEEAGMIG LKGHRILGGI RASIYNALNL DQVKTLCEFM KEFQGKYA
