SERC_SALTY
ID SERC_SALTY Reviewed; 362 AA.
AC P55900;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
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=STM0977;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Mouslim C., Flores A., Cano D.A., Casadesus J.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y10355; CAA71381.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19911.1; -; Genomic_DNA.
DR RefSeq; NP_459952.1; NC_003197.2.
DR RefSeq; WP_000079584.1; NC_003197.2.
DR PDB; 3QM2; X-ray; 2.25 A; A/B=1-362.
DR PDBsum; 3QM2; -.
DR AlphaFoldDB; P55900; -.
DR SMR; P55900; -.
DR STRING; 99287.STM0977; -.
DR PaxDb; P55900; -.
DR EnsemblBacteria; AAL19911; AAL19911; STM0977.
DR GeneID; 1252495; -.
DR KEGG; stm:STM0977; -.
DR PATRIC; fig|99287.12.peg.1030; -.
DR HOGENOM; CLU_034866_0_2_6; -.
DR OMA; GYRASMY; -.
DR PhylomeDB; P55900; -.
DR BioCyc; SENT99287:STM0977-MON; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR EvolutionaryTrace; P55900; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
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; 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 Pyridoxal phosphate; Pyridoxine biosynthesis; Reference proteome;
KW Serine biosynthesis; Transferase.
FT CHAIN 1..362
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150207"
FT BINDING 9
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 42
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 76..77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 102
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 153
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 174
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 197
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 239..240
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT CONFLICT 47
FT /note="I -> M (in Ref. 1; CAA71381)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="Q -> T (in Ref. 1; CAA71381)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3QM2"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3QM2"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3QM2"
FT TURN 176..180
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3QM2"
FT TURN 196..200
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 261..281
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:3QM2"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:3QM2"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:3QM2"
FT HELIX 344..361
FT /evidence="ECO:0007829|PDB:3QM2"
SQ SEQUENCE 362 AA; 39832 MW; 802C026A8B4CE2C3 CRC64;
MAQVFNFSSG PAMLPAEVLK LAQQELCDWH GLGTSVMEIS HRGKEFIQVA EEAEQDFRDL
LNIPSNYKVL FCHGGGRGQF AGVPLNLLGD KTTADYVDAG YWAASAIKEA KKYCAPQIID
AKITVDGKRA VKPMREWQLS DNAAYLHYCP NETIDGIAID ETPDFGPEVV VTADFSSTIL
SAPLDVSRYG VIYAGAQKNI GPAGLTLVIV REDLLGKAHE SCPSILDYTV LNDNDSMFNT
PPTFAWYLSG LVFKWLKAQG GVAAMHKINQ QKAELLYGVI DNSDFYRNDV AQANRSRMNV
PFQLADNTLD KVFLEESFAA GLHALKGHRV VGGMRASIYN AMPIEGVKAL TDFMIDFERR
HG
