ID SERC_MYCTU Reviewed; 376 AA.
AC P9WQ73; L0T803; P63514; Q10534;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC; OrderedLocusNames=Rv0884c; ORFNames=MTCY31.12c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-18.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, AND SUBUNIT.
RX PubMed=22525753; DOI=10.1107/s0907444912004829;
RA Coulibaly F., Lassalle E., Baker H.M., Baker E.N.;
RT "Structure of phosphoserine aminotransferase from Mycobacterium
RT tuberculosis.";
RL Acta Crystallogr. D 68:553-563(2012).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:22525753};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:22525753};
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:22525753}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP43632.1; -; Genomic_DNA.
DR PIR; A70781; A70781.
DR RefSeq; NP_215399.1; NC_000962.3.
DR RefSeq; WP_003404623.1; NZ_NVQJ01000001.1.
DR PDB; 2FYF; X-ray; 1.50 A; A/B=1-376.
DR PDB; 3VOM; X-ray; 2.10 A; A/B=1-376.
DR PDBsum; 2FYF; -.
DR PDBsum; 3VOM; -.
DR AlphaFoldDB; P9WQ73; -.
DR SMR; P9WQ73; -.
DR STRING; 83332.Rv0884c; -.
DR iPTMnet; P9WQ73; -.
DR PaxDb; 83332-Rv0884c; -.
DR DNASU; 885140; -.
DR GeneID; 885140; -.
DR KEGG; mtu:Rv0884c; -.
DR TubercuList; Rv0884c; -.
DR eggNOG; COG1932; Bacteria.
DR InParanoid; P9WQ73; -.
DR OrthoDB; 975012at2; -.
DR PhylomeDB; P9WQ73; -.
DR BRENDA; 2.6.1.52; 3445.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
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:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR006272; Pser_aminoTfrase_mycobac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01366; serC_3; 1.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Cytoplasm; Direct protein sequencing; Pyridoxal phosphate;
KW Pyridoxine biosynthesis; Reference proteome; Serine biosynthesis;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127,
FT ECO:0007744|PubMed:21969609"
FT CHAIN 2..376
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150188"
FT BINDING 50
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 84..85
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 108
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22525753"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22525753"
FT BINDING 199
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22525753"
FT BINDING 251..252
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:2FYF"
FT TURN 39..46
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 52..68
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:2FYF"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2FYF"
FT TURN 178..183
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:2FYF"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 274..294
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2FYF"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:2FYF"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:3VOM"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:2FYF"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:2FYF"
SQ SEQUENCE 376 AA; 40233 MW; 32677398E8967D1E CRC64;
MADQLTPHLE IPTAIKPRDG RFGSGPSKVR LEQLQTLTTT AAALFGTSHR QAPVKNLVGR
VRSGLAELFS LPDGYEVILG NGGATAFWDA AAFGLIDKRS LHLTYGEFSA KFASAVSKNP
FVGEPIIITS DPGSAPEPQT DPSVDVIAWA HNETSTGVAV AVRRPEGSDD ALVVIDATSG
AGGLPVDIAE TDAYYFAPQK NFASDGGLWL AIMSPAALSR IEAIAATGRW VPDFLSLPIA
VENSLKNQTY NTPAIATLAL LAEQIDWLVG NGGLDWAVKR TADSSQRLYS WAQERPYTTP
FVTDPGLRSQ VVGTIDFVDD VDAGTVAKIL RANGIVDTEP YRKLGRNQLR VAMFPAVEPD
DVSALTECVD WVVERL
//
