GLYA_METTM
ID GLYA_METTM Reviewed; 423 AA.
AC P50436; D9PYN7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
DE Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
DE Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
DE EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_00051};
GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051};
GN OrderedLocusNames=MTBMA_c17670;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8617278; DOI=10.1111/j.1432-1033.1996.00294.x;
RA Vaupel M., Dietz H., Linder D., Thauer R.K.;
RT "Primary structure of cyclohydrolase (Mch) from Methanobacterium
RT thermoautotrophicum (strain Marburg) and functional expression of the mch
RT gene in Escherichia coli.";
RL Eur. J. Biochem. 236:294-300(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00051};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00051}.
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DR EMBL; X92083; CAA63066.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL59335.1; -; Genomic_DNA.
DR RefSeq; WP_013296545.1; NC_014408.1.
DR AlphaFoldDB; P50436; -.
DR SMR; P50436; -.
DR STRING; 79929.MTBMA_c17670; -.
DR EnsemblBacteria; ADL59335; ADL59335; MTBMA_c17670.
DR GeneID; 9705478; -.
DR KEGG; mmg:MTBMA_c17670; -.
DR PATRIC; fig|79929.8.peg.1704; -.
DR HOGENOM; CLU_022477_2_1_2; -.
DR OMA; SHPAGLI; -.
DR OrthoDB; 22518at2157; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
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:0035999; P:tetrahydrofolate interconversion; IEA:InterPro.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..423
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_0000113717"
FT BINDING 121..123
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 242
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT SITE 226
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT MOD_RES 227
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT CONFLICT 406..423
FT /note="KVHYAFEESGAYKYMEIL -> RSTTPLRSQGPTSTWRSCR (in Ref.
FT 1; CAA63066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47077 MW; 7304C5383128C716 CRC64;
MVSNQDYTER IRDLMKDHNS WMESSINLIA SENITSSRVK EALISDLSHR YAEGLPGERL
YEGCRYIDEI EEITIELSKK LFRAEHANVQ PTSGVVANLA CFFATADVGD PMMAMEVPYG
GHISHAKVSA AGVRGFKIYT HPFDFENMNI DADAMKKKIL EVKPRIILFG GSLFLFPHPV
EEAVEAAEEV GARIMYDGAH VLGLIAGGYF QDPLREGADM LVGSTHKTFP GPQGGIILCR
EELADDIDEA VFPGLVSNHH LHHVAGLGIA TAEMLEFGSE YAAQTIRNAK KLAENLNELG
FNVLCEHLDF TESHQVVMDV SDIGRAAEIS KKLEANNIIL NKNLLPWDDV NRSDDPSGIR
IGTQEITRRG MKESEMSEVA EYIKKVVIDG RNVKEEVSEF MSSYTKVHYA FEESGAYKYM
EIL
