ID A0A045J6N7_MYCTX Unreviewed; 426 AA.
AC A0A045J6N7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00051};
DE Short=SHMT {ECO:0000256|HAMAP-Rule:MF_00051};
DE Short=Serine methylase {ECO:0000256|HAMAP-Rule:MF_00051};
DE EC=2.1.2.1 {ECO:0000256|HAMAP-Rule:MF_00051};
GN Name=glyA1 {ECO:0000313|EMBL:COV82080.1};
GN Synonyms=glyA {ECO:0000256|HAMAP-Rule:MF_00051,
GN ECO:0000313|EMBL:SGI02832.1};
GN ORFNames=A4S10_01165 {ECO:0000313|EMBL:OMH59002.1}, ERS007665_01009
GN {ECO:0000313|EMBL:CNU39335.1}, ERS007679_02519
GN {ECO:0000313|EMBL:COV82080.1}, ERS007681_02302
GN {ECO:0000313|EMBL:CFE39912.1}, ERS007741_03610
GN {ECO:0000313|EMBL:COX00484.1}, ERS053720_03144
GN {ECO:0000313|EMBL:CFH91679.1}, GJE03_05810
GN {ECO:0000313|EMBL:QGK78359.1}, SAMEA2683035_02641
GN {ECO:0000313|EMBL:SGI02832.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:COV82080.1, ECO:0000313|Proteomes:UP000045842};
RN [1] {ECO:0000313|EMBL:CFH91679.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH91679.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000045274, ECO:0000313|Proteomes:UP000045842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGI02832.1,
RC ECO:0000313|Proteomes:UP000182946}, D00700688
RC {ECO:0000313|EMBL:CNU39335.1, ECO:0000313|Proteomes:UP000045274},
RC G09801536 {ECO:0000313|EMBL:COV82080.1,
RC ECO:0000313|Proteomes:UP000045842}, G09901357
RC {ECO:0000313|EMBL:CFE39912.1, ECO:0000313|Proteomes:UP000048289}, and
RC P00601463 {ECO:0000313|EMBL:COX00484.1,
RC ECO:0000313|Proteomes:UP000048600};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OMH59002.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH59002.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH59002.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH59002.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QGK78359.1, ECO:0000313|Proteomes:UP000388593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUSMDU00018547 {ECO:0000313|EMBL:QGK78359.1,
RC ECO:0000313|Proteomes:UP000388593};
RA Baines S.L., Goncalves da Silva A., Carter G.P., Jennison A.V.,
RA Rathnayake I.U., Graham R.M.A., Sintchenko V., Wang Q., Rockett R.J.,
RA Timms V.J., Martinez E., Ballard S., Tomita T., Isles N., Horan K.A.,
RA Pitchers W., Stinear T.P., Williamson D.A., Howden B.P., Seemann T.;
RT "Complete microbial genomes for public health in Australia and Southwest
RT Pacific.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC glycine with tetrahydrofolate (THF) serving as the one-carbon carrier.
CC This reaction serves as the major source of one-carbon groups required
CC for the biosynthesis of purines, thymidylate, methionine, and other
CC important biomolecules. Also exhibits THF-independent aldolase activity
CC toward beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC retro-aldol mechanism. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00051};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00051, ECO:0000256|PIRSR:PIRSR000412-50};
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC serine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|HAMAP-Rule:MF_00051}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC ECO:0000256|HAMAP-Rule:MF_00051}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00051}.
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DR EMBL; CFOE01000290; CFE39912.1; -; Genomic_DNA.
DR EMBL; CFSW01000022; CFH91679.1; -; Genomic_DNA.
DR EMBL; CQPW01000138; CNU39335.1; -; Genomic_DNA.
DR EMBL; CSAD01000355; COV82080.1; -; Genomic_DNA.
DR EMBL; CHKL01000570; COX00484.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH59002.1; -; Genomic_DNA.
DR EMBL; CP045962; QGK78359.1; -; Genomic_DNA.
DR EMBL; FPTZ01000018; SGI02832.1; -; Genomic_DNA.
DR RefSeq; WP_003405797.1; NZ_WUCS01000016.1.
DR PATRIC; fig|1773.211.peg.1970; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000045274; Unassembled WGS sequence.
DR Proteomes; UP000045842; Unassembled WGS sequence.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000048289; Unassembled WGS sequence.
DR Proteomes; UP000048600; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; Chromosome.
DR Proteomes; UP000388593; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00378; SHMT; 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_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00051};
KW Methyltransferase {ECO:0000313|EMBL:COV82080.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_00051};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00051};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00051}.
FT DOMAIN 5..386
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT BINDING 118
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 122..124
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT SITE 226
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT MOD_RES 227
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 426 AA; 45001 MW; 9256AAEB7C1F9BA6 CRC64;
MSAPLAEVDP DIAELLAKEL GRQRDTLEMI ASENFAPRAV LQAQGSVLTN KYAEGLPGRR
YYGGCEHVDV VENLARDRAK ALFGAEFANV QPHSGAQANA AVLHALMSPG ERLLGLDLAN
GGHLTHGMRL NFSGKLYENG FYGVDPATHL IDMDAVRATA LEFRPKVIIA GWSAYPRVLD
FAAFRSIADE VGAKLLVDMA HFAGLVAAGL HPSPVPHADV VSTTVHKTLG GGRSGLIVGK
QQYAKAINSA VFPGQQGGPL MHVIAGKAVA LKIAATPEFA DRQRRTLSGA RIIADRLMAP
DVAKAGVSVV SGGTDVHLVL VDLRDSPLDG QAAEDLLHEV GITVNRNAVP NDPRPPMVTS
GLRIGTPALA TRGFGDTEFT EVADIIATAL ATGSSVDVSA LKDRATRLAR AFPLYDGLEE
WSLVGR
//
