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Database: UniProt
Entry: A0A132NEY0_HYDSH
LinkDB: A0A132NEY0_HYDSH
Original site: A0A132NEY0_HYDSH 
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
//
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