ID R9SNG4_9EURY Unreviewed; 422 AA.
AC R9SNG4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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.- {ECO:0000256|HAMAP-Rule:MF_00051};
GN Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051,
GN ECO:0000313|EMBL:AGN17546.1};
GN ORFNames=Abm4_1690 {ECO:0000313|EMBL:AGN17546.1};
OS Methanobrevibacter sp. AbM4.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=224719 {ECO:0000313|EMBL:AGN17546.1, ECO:0000313|Proteomes:UP000014066};
RN [1] {ECO:0000313|EMBL:AGN17546.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AbM4 {ECO:0000313|EMBL:AGN17546.1};
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGN17546.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abm4 {ECO:0000313|Proteomes:UP000014066};
RG Pastoral Greenhouse Gas Research Consortium;
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RT "The comlpete genome sequence of Methanobrevibacter sp. AbM4.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon
CC carrier. Also exhibits a pteridine-independent aldolase activity toward
CC beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-
CC aldol mechanism. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methylenetetrahydromethanopterin + glycine + H2O =
CC 5,6,7,8-tetrahydromethanopterin + L-serine; Xref=Rhea:RHEA:47104,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57818, ChEBI:CHEBI:58103; Evidence={ECO:0000256|HAMAP-
CC 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 -!- 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; CP004050; AGN17546.1; -; Genomic_DNA.
DR RefSeq; WP_016359243.1; NC_021355.1.
DR AlphaFoldDB; R9SNG4; -.
DR STRING; 224719.Abm4_1690; -.
DR GeneID; 15799178; -.
DR KEGG; meb:Abm4_1690; -.
DR eggNOG; arCOG00070; Archaea.
DR HOGENOM; CLU_022477_2_1_2; -.
DR OrthoDB; 5821at2157; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000014066; 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: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:InterPro.
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; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW Methyltransferase {ECO:0000313|EMBL:AGN17546.1};
KW One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051,
KW ECO:0000256|PIRSR:PIRSR000412-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000014066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00051}.
FT DOMAIN 11..383
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT BINDING 120..122
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT BINDING 241
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 422 AA; 47003 MW; 038EC4BD0D75B2A8 CRC64;
MSNQEYITEF QGYLKQHNDW MKNSINLIAS ENITSADVKT AMVSDLSHRY AEGKSHERLY
EGCKYIDDIE DLTVDLNKKL FNAKYVDVRT VSGVTANLAA FFAFTKYNDK LMALEVPYGG
HISHANVSAA GIHGLKNVSH PFNPDIMNID ADKMKKTIIE EKPKVVLLGG SLFLFPHPVA
EAREAADEVG AKVLYDGAHV LGLIAGKQFQ DPLKEGADVL MGSTHKSFPG TQGGIILSDH
EEYADKIDNA VFPGVVSNYH LHHLAGLGIA TAEMLEFGEA YAKQIIKNAK ALAQALYELG
FNVLCEDLGF TESHQVAVDV TNITDGNTFA KKLERNNIIL NKNLLPWDDV NNSDNPSGIR
IGTSEITRRG LKEKNMSEIA EFIKRVVVDD ENVKDEVSEY MNNYTKVHYA FRETEAYEYL
QF
//
