ID L0HC46_METFS Unreviewed; 412 AA.
AC L0HC46;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 OrderedLocusNames=Metfor_0530 {ECO:0000313|EMBL:AGB01600.1};
OS Methanoregula formicica (strain DSM 22288 / NBRC 105244 / SMSP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=593750 {ECO:0000313|EMBL:AGB01600.1, ECO:0000313|Proteomes:UP000010824};
RN [1] {ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Imachi H.,
RA Tamaki H., Sekiguchi Y., Kamagata Y., Cadillo-Quiroz H., Zinder S.,
RA Liu W.-T., Woyke T.;
RT "Complete sequence of Methanoregula formicicum SMSP.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB01600.1, ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RX PubMed=25189582;
RA Yamamoto K., Tamaki H., Cadillo-Quiroz H., Imachi H., Kyrpides N.,
RA Woyke T., Goodwin L., Zinder S.H., Kamagata Y., Liu W.T.;
RT "Complete Genome Sequence of Methanoregula formicica SMSPT, a Mesophilic
RT Hydrogenotrophic Methanogen Isolated from a Methanogenic Upflow Anaerobic
RT Sludge Blanket Reactor.";
RL Genome Announc. 2:e00870-14(2014).
CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC glycine with tetrahydrofolate (THF) serving as the one-carbon carrier.
CC Also exhibits THF-independent aldolase activity toward beta-
CC hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol
CC 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; CP003167; AGB01600.1; -; Genomic_DNA.
DR RefSeq; WP_015284564.1; NC_019943.1.
DR AlphaFoldDB; L0HC46; -.
DR STRING; 593750.Metfor_0530; -.
DR GeneID; 14309203; -.
DR KEGG; mfo:Metfor_0530; -.
DR eggNOG; arCOG00070; Archaea.
DR HOGENOM; CLU_022477_2_1_2; -.
DR InParanoid; L0HC46; -.
DR OrthoDB; 5821at2157; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000010824; 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: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; 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:AGB01600.1};
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:UP000010824};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00051}.
FT DOMAIN 4..380
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 349..351
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 412 AA; 44293 MW; 79350E66E59C4205 CRC64;
MSYLAKTDPA IADIIEKERL RQVNGLELIA SENVVSRAVL EAMGSIMTNK YAEGYPGKRY
YGGCEFHDMA ENLARDRLKK LFGAEHANVQ AHSGTQANMA VYFAAIKLGE KILSMKLNQG
GHLSHGSPVS FTGKFYQVAQ YGVDPKTEVL DYGVVAEMAK KERPQIIVCG ASAYPRTIDF
KAFQEIADDV GAVCLADIAH IAGLVATGLH PTSVGVVNYT TTTTHKTLRG PRGGAIMCNA
DLGVGIDKAV FPGMQGGPLM HTIAAKAVCF EEALKPSFRE YNKQIIRNAK VLAETLMANG
LRLVSGGTDN HLMLLDLTEQ GITGLEAETA LGKAGITVNK NTIPNETKSP FVTSGLRIGT
PAVTSRGMKE AEMRLIGGWI ASVIKDIKNE KNTSDVRGKV EALASKFTLY PE
//
