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Database: UniProt
Entry: A0A176Q973_9MICO
LinkDB: A0A176Q973_9MICO
Original site: A0A176Q973_9MICO 
ID   A0A176Q973_9MICO        Unreviewed;       425 AA.
AC   A0A176Q973; A0A5P8FM03;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=AWH69_15050 {ECO:0000313|EMBL:OAB86212.1}, EEW87_010610
GN   {ECO:0000313|EMBL:QFQ30639.2};
OS   Janibacter melonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB86212.1, ECO:0000313|Proteomes:UP000076976};
RN   [1] {ECO:0000313|EMBL:OAB86212.1, ECO:0000313|Proteomes:UP000076976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD11-4 {ECO:0000313|EMBL:OAB86212.1,
RC   ECO:0000313|Proteomes:UP000076976};
RA   Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT   "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QFQ30639.2, ECO:0000313|Proteomes:UP000271708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M714 {ECO:0000313|EMBL:QFQ30639.2,
RC   ECO:0000313|Proteomes:UP000271708};
RA   Jin M., Zhao Q.R.;
RT   "Complete Genome Sequence of Janibacter melonis M714 with both human health
RT   impact and industrial applications.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QFQ30639.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M714 {ECO:0000313|EMBL:QFQ30639.2};
RA   Zhao Q.;
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|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}.
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DR   EMBL; LQZG01000005; OAB86212.1; -; Genomic_DNA.
DR   EMBL; CP044548; QFQ30639.2; -; Genomic_DNA.
DR   RefSeq; WP_068277860.1; NZ_QSNP01000002.1.
DR   AlphaFoldDB; A0A176Q973; -.
DR   STRING; 262209.AWH69_15050; -.
DR   GeneID; 59161621; -.
DR   KEGG; jme:EEW87_010610; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000076976; Unassembled WGS sequence.
DR   Proteomes; UP000271708; 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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Aminotransferase {ECO:0000313|EMBL:QFQ30639.2};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:OAB86212.1};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00051}; Reference proteome {ECO:0000313|Proteomes:UP000076976};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00051}.
FT   DOMAIN          15..390
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   BINDING         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         131..133
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         251
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   SITE            235
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT                   ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   425 AA;  45053 MW;  C26E5D5A64D97FA2 CRC64;
     MTDDTFYGSD FGGLRAFDPE IADVLLSELG RIRSGLQLIA SENLSSPEVL TALGSTLSNK
     YAEGYPGRRY YGGCSEVDKA EQLAIDRCKA LFDADHANVQ AHSGASANQA VYGAFLKPGE
     KILAMSLPHG GHLTHGTKVS FSGKWFDAVH YGVHPETEDV DYDEMERLAK EHRPKVICAG
     GSAIPRLIDF ERIRAIADEV GAIFWVDAAH FIGLVAGKAI PSPVPFADVV TFTTHKVLRG
     PRSGALVCKA EHAAALDKAI FPMMQGGPQM HTIAAKAVNF KECASPEYAD YTRRVITNSQ
     ALAAGLAERG IRPTTGGTDT HLALLDLQGV GVTGKDAEAR ADAAGIVLNK NAIPNDPQKP
     GIASGVRVGT PCVTTQGMGE AEMATIAELI HVAVTQGDAD PEHAVSQQVR AGVDELVTAF
     PAYPR
//
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