SERC_NIACI
ID SERC_NIACI Reviewed; 362 AA.
AC Q59196;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21783 / subsp. Alkalophilus;
RA Battchikova N., Holopainen M., Himanen J.-P., Korpela T.;
RT "Phosphoserine aminotransferase from Bacillus circulans var. alkalophilus:
RT purification, gene cloning and sequencing.";
RL (In) Sannia G. (eds.);
RL Proceedings of 9th meeting on vitamin B6 and carbonyl catalysis,
RL pp.207-207, Dipt. Chimica Organica e Biologica, Napoli (1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, SUBUNIT, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 21783 / subsp. Alkalophilus;
RX PubMed=8695645; DOI=10.1016/0167-4838(96)00039-8;
RA Battchikova N., Himanen J.-P., Ahjolahti M., Korpela T.;
RT "Phosphoserine aminotransferase from Bacillus circulans subsp.
RT alkalophilus: purification, gene cloning and sequencing.";
RL Biochim. Biophys. Acta 1295:187-194(1996).
RN [3]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 21783 / subsp. Alkalophilus;
RX PubMed=8819175; DOI=10.1002/pro.5560050721;
RA Moser M., Mueller R., Battchikova N., Koivulehto M., Korpela T.,
RA Jansonius J.N.;
RT "Crystallization and preliminary X-ray analysis of phosphoserine
RT aminotransferase from Bacillus circulans subsp. alkalophilus.";
RL Protein Sci. 5:1426-1428(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLU-3 IN COMPLEX WITH PLP,
RP AND COFACTOR.
RC STRAIN=ATCC 21783 / subsp. Alkalophilus;
RA Hester G., Luong T.N., Moser M., Jansonius J.N.;
RL Submitted (SEP-1998) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF MUTANT GLU-3 IN COMPLEX WITH PLP,
RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=ATCC 21783 / subsp. Alkalophilus;
RX PubMed=16532449; DOI=10.1002/prot.20935;
RA Kapetaniou E.G., Thanassoulas A., Dubnovitsky A.P., Nounesis G.,
RA Papageorgiou A.C.;
RT "Effect of pH on the structure and stability of Bacillus circulans ssp.
RT alkalophilus phosphoserine aminotransferase: thermodynamic and
RT crystallographic studies.";
RL Proteins 63:742-753(2006).
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:0000269|PubMed:16532449}.
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:0000269|PubMed:8695645};
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;
CC Evidence={ECO:0000269|PubMed:8695645};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:16532449, ECO:0000269|Ref.4};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:16532449, ECO:0000269|Ref.4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for glutamate (at pH 7) {ECO:0000269|PubMed:16532449};
CC KM=0.2 mM for glutamate (at pH 9) {ECO:0000269|PubMed:16532449};
CC KM=0.1 mM for phosphohydroxypyruvate (at pH 7)
CC {ECO:0000269|PubMed:16532449};
CC KM=0.09 mM for phosphohydroxypyruvate (at pH 9)
CC {ECO:0000269|PubMed:16532449};
CC Vmax=6 nmol/min/mg enzyme for the reaction forming phosphoserine (at
CC pH 7) {ECO:0000269|PubMed:16532449};
CC Vmax=10 nmol/min/mg enzyme for the reaction forming phosphoserine (at
CC pH 9) {ECO:0000269|PubMed:16532449};
CC pH dependence:
CC Optimum pH is 9.0. At pH 9.5, retains more 60% of its maximum
CC activity. Inactive below pH 6. {ECO:0000269|PubMed:16532449};
CC Temperature dependence:
CC Thermal denaturation midpoint (Tm) is 71 degrees Celsius at pH 6 and
CC is lowered around 58 degrees Celsius at pH 8.5 and 10.
CC {ECO:0000269|PubMed:16532449};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16532449,
CC ECO:0000269|PubMed:8695645, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Significant conformational rearrangements are involved
CC in response to pH changes.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; Z46432; CAA86558.2; -; Genomic_DNA.
DR PIR; S71439; S71439.
DR PDB; 1BT4; X-ray; 2.30 A; A=4-362.
DR PDB; 1W3U; X-ray; 1.50 A; A=1-362.
DR PDB; 2C0R; X-ray; 1.20 A; A/B=2-362.
DR PDBsum; 1BT4; -.
DR PDBsum; 1W3U; -.
DR PDBsum; 2C0R; -.
DR AlphaFoldDB; Q59196; -.
DR SMR; Q59196; -.
DR PRIDE; Q59196; -.
DR BRENDA; 2.6.1.52; 649.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR EvolutionaryTrace; Q59196; -.
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 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Direct protein sequencing; Pyridoxal phosphate; Serine biosynthesis;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8695645"
FT CHAIN 2..362
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150147"
FT BINDING 43
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 77..78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 103
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 153
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 173
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 196
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 238..239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:2C0R"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2C0R"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2C0R"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:2C0R"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 260..280
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2C0R"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:2C0R"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:2C0R"
FT HELIX 344..361
FT /evidence="ECO:0007829|PDB:2C0R"
SQ SEQUENCE 362 AA; 39924 MW; 2D63C629C8DD269B CRC64;
MSKRAYNFNA GPAALPLEVL ERAQAEFVDY QHTGMSIMEM SHRGAVYEAV HNEAQARLLA
LLGNPTGYKV LFIQGGASTQ FAMIPMNFLK EGQTANYVMT GSWASKALKE AKLIGDTHVA
ASSEASNYMT LPKLQEIQLQ DNAAYLHLTS NETIEGAQFK AFPDTGSVPL IGDMSSDILS
RPFDLNQFGL VYAGAQKNLG PSGVTVVIVR EDLVAESPKH LPTMLRYDTY VKNNSLYNTP
PSFGIYMVNE VLKWIEERGG LEGVQQANRK KASLIYDAID QSGGFYRGCV DVDSRSDMNI
TFRLASEELE KEFVKASEQE GFVGLKGHRS VGGLRASIYN AVPYESCEAL VQFMEHFKRS
RG
