SERC_NEIMA
ID SERC_NEIMA Reviewed; 368 AA.
AC O34370; A1IT98; O33382; O33383; O33384; O33386;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=NMA1894;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Various strains;
RX PubMed=9350862; DOI=10.1046/j.1365-2958.1997.5211882.x;
RA Morelli G., Malorny B., Mueller K., Seiler A., Wang J.-F., del Valle J.,
RA Achtman M.;
RT "Clonal descent and microevolution of Neisseria meningitidis during 30
RT years of epidemic spread.";
RL Mol. Microbiol. 25:1047-1064(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(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; AF004820; AAC32675.1; -; Genomic_DNA.
DR EMBL; AF004821; AAC32679.1; -; Genomic_DNA.
DR EMBL; AF004822; AAC32683.1; -; Genomic_DNA.
DR EMBL; AF004823; AAC32687.1; -; Genomic_DNA.
DR EMBL; AF004824; AAC32691.1; -; Genomic_DNA.
DR EMBL; AF004825; AAC32695.1; -; Genomic_DNA.
DR EMBL; AF004826; AAC32699.1; -; Genomic_DNA.
DR EMBL; AL157959; CAM09011.1; -; Genomic_DNA.
DR PIR; F81816; F81816.
DR RefSeq; WP_002249856.1; NC_003116.1.
DR AlphaFoldDB; O34370; -.
DR SMR; O34370; -.
DR EnsemblBacteria; CAM09011; CAM09011; NMA1894.
DR KEGG; nma:NMA1894; -.
DR HOGENOM; CLU_034866_0_2_4; -.
DR OMA; GYRASMY; -.
DR BioCyc; NMEN122587:NMA_RS09570-MON; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000000626; 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; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Pyridoxine biosynthesis; Serine biosynthesis; Transferase.
FT CHAIN 1..368
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150191"
FT BINDING 44
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 78..79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 104
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 157
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 179
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 202
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 244..245
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT VARIANT 168
FT /note="R -> C (in strain: B293, Z3910 and Z3918)"
FT VARIANT 192
FT /note="A -> S (in strain: Z3524)"
FT VARIANT 237
FT /note="I -> L (in strain: B293, Z3524, Z3910, Z3915 and
FT Z3918)"
FT VARIANT 240
FT /note="D -> E (in strain: Z3915 and Z3524)"
FT VARIANT 289
FT /note="G -> D (in strain: B293, Z3910 and Z3918)"
FT VARIANT 336
FT /note="T -> S (in strain: Z4296)"
SQ SEQUENCE 368 AA; 41388 MW; 3D3E305853698537 CRC64;
MSLYPIYNFS AGPAVLPEAV LETARQEMLD YNGTGFPVMA MSHRSEMFLS ILHHAEQDLR
QLLKVPDNYK ILFLQGGATT QFNMAAMNLA HGFRTADAVV TGNWSRIAYE QMSRLTDTEI
RLAAHGGEQF DYLDLPPVET WDVAPDSAFV HFAVNETVNG LQYREVPRLS EGMPPLVCDM
SSEILSREFD VADYGLIYAG AQKNIGPAGV TVVIVREDLL ERCPNDIPDV FNYRSHINRD
GMYNTPSTYA IYMSGLVFRW LQAQGGVKKI EAVNRLKAQT LYETIDGSGG FYINRIRPNA
RSKMNVVFQT GDEELDRRFV LEAELQGLCL LKGYKTVGGM RASIYNAMPL EGVRALADFM
RDFQRRYG
