GLYA_THEAC
ID GLYA_THEAC Reviewed; 426 AA.
AC Q9HI38;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 118.
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}; OrderedLocusNames=Ta1509;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC glycine with a modified folate serving as the one-carbon carrier. Also
CC exhibits a pteridine-independent aldolase activity toward beta-
CC hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol
CC mechanism. {ECO:0000255|HAMAP-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC12627.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445067; CAC12627.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048162191.1; NC_002578.1.
DR AlphaFoldDB; Q9HI38; -.
DR SMR; Q9HI38; -.
DR STRING; 273075.Ta1509; -.
DR EnsemblBacteria; CAC12627; CAC12627; CAC12627.
DR GeneID; 1456954; -.
DR KEGG; tac:Ta1509; -.
DR eggNOG; arCOG00070; Archaea.
DR HOGENOM; CLU_022477_2_1_2; -.
DR OMA; SHPAGLI; -.
DR OrthoDB; 22518at2157; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000001024; 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; Reference proteome; Transferase.
FT CHAIN 1..426
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_0000113727"
FT BINDING 115
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT BINDING 119..121
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT SITE 224
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT MOD_RES 225
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ SEQUENCE 426 AA; 46975 MW; 2FF2525003EB5DB5 CRC64;
MSYEDAEYIR EMAMKHSEMF GEGIALIASE NVMSPLAKEV MISDLESRYA EGLPHHRYYQ
GNYYVDLIED RTNELLSKLF RTSQTDPRPI SGTNANSAAI YALAGPGDLV ATPSLSGGGH
ISAAEFGILG MRSVRTINYP YDMDTMTIDP DQASKMIIKE KPKVCLFGQS VFMFPAPLKE
MAEAFHEVGC KVWYDGAHVL GLIAGGRFQD PLREGADIVT GSTHKTFPGP QHGVILGNTD
DETWKAVRRA VFPGVLSNHH LNAMAALGIT AAEELEFGKR YADDIISNAK VLAEELYANG
FNVLAEKRGF TESHTMAVDV SKNGGGKYVA ETLEKCGIIL NKNLLPWDDN KKSQNPSGIR
IGVQEATRVG MGKSEMKEIA SLITRAIIRH EDPEKIKAEV KQLKSGFREV KYCYGKMDGY
SYIKLI
