ID A0A132NEY0_HYDSH Unreviewed; 419 AA.
AC A0A132NEY0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 33.
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 ORFNames=HSCHL_0133 {ECO:0000313|EMBL:PTQ54554.1}, KM312_05890
GN {ECO:0000313|EMBL:MBT9282173.1}, SA87_07045
GN {ECO:0000313|EMBL:OAR04199.1};
OS Hydrogenibacillus schlegelii (Bacillus schlegelii).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family X. Incertae Sedis; Hydrogenibacillus.
OX NCBI_TaxID=1484 {ECO:0000313|EMBL:OAR04199.1, ECO:0000313|Proteomes:UP000243024};
RN [1] {ECO:0000313|EMBL:OAR04199.1, ECO:0000313|Proteomes:UP000243024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA 48 {ECO:0000313|EMBL:OAR04199.1,
RC ECO:0000313|Proteomes:UP000243024};
RA Hemp J.;
RT "Draft genome sequence of Hydrogenibacillus schlegelii DSM 2000.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PTQ54554.1, ECO:0000313|Proteomes:UP000244180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL33 {ECO:0000313|EMBL:PTQ54554.1};
RA Kadnikov V.V., Mardanov A.V., Ivasenko D., Beletsky A.V., Karnachuk O.V.,
RA Ravin N.V.;
RT "Burning lignite coal seam in the remote Altai Mountains harbors a
RT hydrogen-driven thermophilic microbial community.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MBT9282173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RBS10-49 {ECO:0000313|EMBL:MBT9282173.1};
RA Kadnikov V., Mardanov A.V., Beletsky A.V., Karnachuk O.V., Ravin N.V.;
RT "Metagenomic Analysis of the Microbial Community in the Underground Coal
RT Fire Area (Kemerovo Region, Russia) Revealed Predominance of Thermophilic
RT Members of the Phyla Deinococcus-thermus, Aquificae, and Firmicutes.";
RL Microbiology 0:0-0(2021).
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 -!- 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:OAR04199.1}.
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DR EMBL; JAHHQF010000050; MBT9282173.1; -; Genomic_DNA.
DR EMBL; JXBB01000023; OAR04199.1; -; Genomic_DNA.
DR EMBL; PEBV01000003; PTQ54554.1; -; Genomic_DNA.
DR RefSeq; WP_066201520.1; NZ_PEBV01000003.1.
DR AlphaFoldDB; A0A132NEY0; -.
DR STRING; 1484.SA87_07045; -.
DR OrthoDB; 9803846at2; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000243024; Unassembled WGS sequence.
DR Proteomes; UP000244180; Unassembled WGS sequence.
DR Proteomes; UP000748108; 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, MITOCHONDRIAL; 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|HAMAP-Rule:MF_00051};
KW Methyltransferase {ECO:0000313|EMBL:OAR04199.1};
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:UP000243024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00051}.
FT DOMAIN 5..378
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT BINDING 117
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 121..123
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 240
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT SITE 225
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 419 AA; 45754 MW; 7D4ABD93BAAD2DB4 CRC64;
MEQLRAQDPD VFRAIQRELE RQRSHLELIA SENFVSPAVL EAMGTVLTNK YAEGYPGRRY
YGGCTYVDVV EDLARERAKA LFGAEHANVQ PHSGAQANMA VYHALLEPGD TVLGMDLAHG
GHLTHGSPVN FSGKLYRFVA YGVDPETETI DYDAVYRLAE EHRPKLIVAG ASAYPRIIDF
ARFREIADAV GALFMVDMAH IAGLVAAGLH PSPVPYADAV TTTTHKTLRG PRGGLILSRE
RYAKAIDKAL FPGIQGGPLM HVIAAKAVAL GEALQPAFKR YSEQVVKNAR RLAEALRARG
FRLVSGGTDN HLILIDLRNR GLTGREAEAR LDAVGITTNK NAIPFDPEKP NTTSGLRVGT
AAVTTRGMDE AAMDEIAELF DLVLTPNPRP GAEEEARRRV QALVERFPLY DALVPGYRL
//