ID A0A2A7NCE2_MYCAG Unreviewed; 491 AA.
AC A0A2A7NCE2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=glyA {ECO:0000256|HAMAP-Rule:MF_00051,
GN ECO:0000313|EMBL:GFG55458.1};
GN ORFNames=CQY20_05505 {ECO:0000313|EMBL:PEG41111.1}, MAGR_68990
GN {ECO:0000313|EMBL:GFG55458.1};
OS Mycolicibacterium agri (Mycobacterium agri).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=36811 {ECO:0000313|EMBL:PEG41111.1, ECO:0000313|Proteomes:UP000220914};
RN [1] {ECO:0000313|EMBL:PEG41111.1, ECO:0000313|Proteomes:UP000220914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG37673 {ECO:0000313|EMBL:PEG41111.1,
RC ECO:0000313|Proteomes:UP000220914};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GFG55458.1, ECO:0000313|Proteomes:UP000465302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG55458.1,
RC ECO:0000313|Proteomes:UP000465302};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:GFG55458.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG55458.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PEG41111.1}.
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DR EMBL; BLKS01000004; GFG55458.1; -; Genomic_DNA.
DR EMBL; PDCP01000007; PEG41111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A7NCE2; -.
DR OrthoDB; 9803846at2; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000220914; Unassembled WGS sequence.
DR Proteomes; UP000465302; Unassembled WGS sequence.
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; 2.
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:PEG41111.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000220914};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00051}.
FT DOMAIN 33..136
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT DOMAIN 169..441
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT BINDING 176
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 180..182
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT SITE 287
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT MOD_RES 288
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 491 AA; 51989 MW; E2C84BDD7C159B82 CRC64;
MAVDPVTTSA PAPGADYVET ASAAYRDILQ IIETVEPRIA AATRKEIADQ RDSLKLIASE
NYASPAVLLT MGTWLSDKYA EGTIGHRFYA GCQNVDTVET VAAEHARELF GAPYAYAQPH
SGIDANLVAY WAILATRVEA PGLADAGVKN VNDLSEEGWE KLRAQLGNQR LLGMSLDAGG
HLTHGFRPNI SGKMFHQRSY GTDPETGLLD YDALAKAARE FKPLILVGGY SAYPRRINFA
KMREIADEVG ATLMVDMAHF AGLVAGKVFT GDEDPVPHAH VTTTTTHKSL RGPRGGLVLA
TPEYSDAVDK GCPMVLGGPL SHVMAAKAVA LAEARQPAFQ AYAQRVADNA KALAEGFLKR
GARLVTGGTD NHIVLLDVQS FGVTGRQAES ALLDSGIVTN RNSIPADPNG AWYTSGIRLG
TPALTTRGFG PDEFDRVAEL IVDVLAKTEP AAAASGPSKA KYSLADGTAE RVHAAASELL
AANPLYPGLT L
//
