ID Q0EDS3_PSESH Unreviewed; 417 AA.
AC Q0EDS3;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=PHA45 {ECO:0000313|EMBL:BAF32911.1};
GN Synonyms=glyA {ECO:0000256|HAMAP-Rule:MF_00051};
OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS phaseolicola).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=319 {ECO:0000313|EMBL:BAF32911.1};
RN [1] {ECO:0000313|EMBL:BAF32911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 302282 {ECO:0000313|EMBL:BAF32911.1};
RX PubMed=8979356;
RA Sawada H., Takeuchi T., Matsuda I.;
RT "Comparative analysis of Pseudomonas syringae pv. actinidiae and pv.
RT phaseolicola based on phaseolotoxin-resistant ornithine
RT carbamoyltransferase gene (argK) and 16S-23S rRNA intergenic spacer
RT sequences.";
RL Appl. Environ. Microbiol. 63:282-288(1997).
RN [2] {ECO:0000313|EMBL:BAF32911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 302282 {ECO:0000313|EMBL:BAF32911.1};
RX PubMed=10552044; DOI=.1007/PL00006584;
RA Sawada H., Suzuki F., Matsuda I., Saitou N.;
RT "Phylogenetic analysis of Pseudomonas syringae pathovars suggests the
RT horizontal gene transfer of argK and the evolutionary stability of hrp gene
RT cluster.";
RL J. Mol. Evol. 49:627-644(1999).
RN [3] {ECO:0000313|EMBL:BAF32911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 302282 {ECO:0000313|EMBL:BAF32911.1};
RX PubMed=11956683; DOI=.1007/s00239-001-0032-y;
RA Sawada H., Kanaya S., Tsuda M., Suzuki F., Azegami K., Saitou N.;
RT "A phylogenomic study of the OCTase genes in Pseudomonas syringae
RT pathovars: the horizontal transfer of the argK-tox cluster and the
RT evolutionary history of OCTase genes on their genomes.";
RL J. Mol. Evol. 54:437-457(2002).
RN [4] {ECO:0000313|EMBL:BAF32911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 302282 {ECO:0000313|EMBL:BAF32911.1};
RX PubMed=16927007; DOI=.1007/s00239-005-0271-4;
RA Genka H., Baba T., Tsuda M., Kanaya S., Mori H., Yoshida T., Noguchi M.T.,
RA Tsuchiya K., Sawada H.;
RT "Comparative analysis of argK-tox clusters and their flanking regions in
RT phaseolotoxin-producing Pseudomonas syringae pathovars.";
RL J. Mol. Evol. 63:401-414(2006).
RN [5] {ECO:0000313|EMBL:BAF32911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 302282 {ECO:0000313|EMBL:BAF32911.1};
RA Sawada H., Fujikawa T.;
RT "Genetic diversity of Pseudomonas syringae pv. actinidiae, pathogen of
RT kiwifruit bacterial canker.";
RL Plant Pathol. 68:1235-1248(2019).
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|HAMAP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB237164; BAF32911.1; -; Genomic_DNA.
DR RefSeq; WP_003340745.1; NZ_RBUR01000291.1.
DR AlphaFoldDB; Q0EDS3; -.
DR SMR; Q0EDS3; -.
DR GeneID; 69861339; -.
DR PATRIC; fig|319.14.peg.5230; -.
DR OMA; SRQKHFI; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
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:SF50; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00051}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW Methyltransferase {ECO:0000313|EMBL:BAF32911.1};
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 9..385
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT BINDING 121
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 125..127
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 354..356
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT SITE 228
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT MOD_RES 229
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 417 AA; 44844 MW; 5C1C1960BF14A789 CRC64;
MFSRDLTIAK YDADLFAAME QEALRQEEHI ELIASENYTS PAVMEAQGSA LTNKYAEGYP
GKRYYGGCEY VDVIEQLAID RAKELFGADY ANVQPHAGSQ ANSAVYLALL QGGDTILGMS
LAHGGHLTHG ASVSSSGKLY NAVQYGIDAN GMIDYDEVER LAVEHKPKMI VAGFSAYSQI
LDFPRFRAIA DKVGAYLFVD MAHVAGLVAA GVYPNPVPFA DVVTTTTHKT LRGPRGGLIL
ARANAEIEKK LNSAVFPGSQ GGPLEHVIAA KAVCFKEALQ PEFKTYQQQV VKNAKAMAGV
FIERGFDVVS GGTENHLFLL SLIKQDISGK DADAALGRAF ITVNKNSVPN DPRSPFVTSG
LRFGTPAVTT RGFKEAECKE LAGWICDILA DLNNEAVIDA VREKVKAICA KLPVYGA
//
