ID SERC_ECOLI Reviewed; 362 AA.
AC P23721; P78266;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 27-MAR-2024, entry version 201.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC; Synonyms=pdxC, pdxF; OrderedLocusNames=b0907, JW0890;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3518706; DOI=10.1042/bj2340049;
RA Duncan K., Coggins J.R.;
RT "The serC-aro A operon of Escherichia coli. A mixed function operon
RT encoding enzymes from two different amino acid biosynthetic pathways.";
RL Biochem. J. 234:49-57(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP SIMILARITY TO RABBIT EPIP.
RX PubMed=2682527; DOI=10.1093/nar/17.20.8379;
RA van der Zel A., Lam H.-M., Winkler M.E.;
RT "Extensive homology between the Escherichia coli K-12 SerC(PdxF)
RT aminotransferase and a protein encoded by a progesterone-induced mRNA in
RT rabbit and human endometria.";
RL Nucleic Acids Res. 17:8379-8379(1989).
RN [7]
RP FUNCTION, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=2121717; DOI=10.1128/jb.172.11.6518-6528.1990;
RA Lam H.-M., Winkler M.E.;
RT "Metabolic relationships between pyridoxine (vitamin B6) and serine
RT biosynthesis in Escherichia coli K-12.";
RL J. Bacteriol. 172:6518-6528(1990).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=8706854; DOI=10.1016/0014-5793(96)00652-7;
RA Drewke C., Klein M., Clade D., Arenz A., Mueller R., Leistner E.;
RT "4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product
RT involved in vitamin B6 biosynthesis.";
RL FEBS Lett. 390:179-182(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-362 IN COMPLEX WITH PLP AND
RP SUBSTRATE ANALOG, SUBUNIT, CATALYTIC MECHANISM, AND PYRIDOXAL PHOSPHATE AT
RP LYS-198.
RX PubMed=10024454; DOI=10.1006/jmbi.1998.2506;
RA Hester G., Stark W., Moser M., Kallen J., Markovic-Housley Z.,
RA Jansonius J.N.;
RT "Crystal structure of phosphoserine aminotransferase from Escherichia coli
RT at 2.3-A resolution: comparison of the unligated enzyme and a complex with
RT alpha-methyl-L-glutamate.";
RL J. Mol. Biol. 286:829-850(1999).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both
CC pyridoxine and serine biosynthesis. {ECO:0000269|PubMed:2121717,
CC ECO:0000269|PubMed:8706854}.
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:8706854};
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:8706854};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:8706854};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:8706854};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for 3-phosphonooxypyruvate {ECO:0000269|PubMed:8706854};
CC KM=17 uM for O(3)-phospho-L-serine {ECO:0000269|PubMed:8706854};
CC KM=110 uM for 4-phosphonooxy-L-threonine
CC {ECO:0000269|PubMed:8706854};
CC Vmax=45 nmol/sec/mg enzyme with 3-phosphonooxypyruvate as substrate
CC {ECO:0000269|PubMed:8706854};
CC Vmax=9.9 nmol/sec/mg enzyme with O(3)-phospho-L-serine as substrate
CC {ECO:0000269|PubMed:8706854};
CC Vmax=3.8 nmol/sec/mg enzyme with 4-phosphonooxy-L-threonine as
CC substrate {ECO:0000269|PubMed:8706854};
CC Note=No activity could be observed with non-phosphorylated
CC substrates.;
CC pH dependence:
CC Optimum pH is 7.5-8.8. {ECO:0000269|PubMed:8706854};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000269|PubMed:2121717}.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC {ECO:0000269|PubMed:2121717}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10024454}.
CC -!- INTERACTION:
CC P23721; P0A6Y8: dnaK; NbExp=2; IntAct=EBI-557952, EBI-542092;
CC P23721; P14081: selB; NbExp=3; IntAct=EBI-557952, EBI-551705;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC73993.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35642.1; -; Genomic_DNA.
DR PIR; B64830; B64830.
DR RefSeq; NP_415427.1; NC_000913.3.
DR RefSeq; WP_000057138.1; NZ_SSZK01000002.1.
DR PDB; 1BJN; X-ray; 2.30 A; A/B=3-362.
DR PDB; 1BJO; X-ray; 2.80 A; A/B=3-362.
DR PDBsum; 1BJN; -.
DR PDBsum; 1BJO; -.
DR AlphaFoldDB; P23721; -.
DR SMR; P23721; -.
DR BioGRID; 4260006; 30.
DR DIP; DIP-2896N; -.
DR IntAct; P23721; 9.
DR STRING; 511145.b0907; -.
DR SWISS-2DPAGE; P23721; -.
DR jPOST; P23721; -.
DR PaxDb; 511145-b0907; -.
DR EnsemblBacteria; AAC73993; AAC73993; b0907.
DR GeneID; 945527; -.
DR KEGG; ecj:JW0890; -.
DR KEGG; eco:b0907; -.
DR PATRIC; fig|1411691.4.peg.1369; -.
DR EchoBASE; EB0939; -.
DR eggNOG; COG1932; Bacteria.
DR HOGENOM; CLU_034866_0_2_6; -.
DR InParanoid; P23721; -.
DR OMA; AFVYFCD; -.
DR OrthoDB; 9809412at2; -.
DR PhylomeDB; P23721; -.
DR BioCyc; EcoCyc:PSERTRANSAM-MONOMER; -.
DR BioCyc; MetaCyc:PSERTRANSAM-MONOMER; -.
DR BRENDA; 2.6.1.52; 2026.
DR SABIO-RK; P23721; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR EvolutionaryTrace; P23721; -.
DR PRO; PR:P23721; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0006564; P:L-serine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006563; P:L-serine metabolic process; IGI:UniProtKB.
DR GO; GO:0033359; P:lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate; IGI:EcoCyc.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IMP:EcoCyc.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00611; PSAT_like; 1.
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; 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 NCBIfam; TIGR01364; serC_1; 1.
DR PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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; Pyridoxine biosynthesis;
KW Reference proteome; Serine biosynthesis; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..362
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150167"
FT BINDING 9
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 42
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 76..77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 102
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 174
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 197
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 239..240
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 293
FT /note="A -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1BJN"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1BJN"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1BJN"
FT TURN 176..180
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1BJN"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:1BJO"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:1BJN"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 261..282
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:1BJN"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:1BJN"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:1BJN"
FT HELIX 344..361
FT /evidence="ECO:0007829|PDB:1BJN"
SQ SEQUENCE 362 AA; 39783 MW; F6A58CBF9FA22BC9 CRC64;
MAQIFNFSSG PAMLPAEVLK QAQQELRDWN GLGTSVMEVS HRGKEFIQVA EEAEKDFRDL
LNVPSNYKVL FCHGGGRGQF AAVPLNILGD KTTADYVDAG YWAASAIKEA KKYCTPNVFD
AKVTVDGLRA VKPMREWQLS DNAAYMHYCP NETIDGIAID ETPDFGADVV VAADFSSTIL
SRPIDVSRYG VIYAGAQKNI GPAGLTIVIV REDLLGKANI ACPSILDYSI LNDNGSMFNT
PPTFAWYLSG LVFKWLKANG GVAEMDKINQ QKAELLYGVI DNSDFYRNDV AKANRSRMNV
PFQLADSALD KLFLEESFAA GLHALKGHRV VGGMRASIYN AMPLEGVKAL TDFMVEFERR
HG
//
