ID GLYA_STAMF Reviewed; 439 AA.
AC A3DNJ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=Smar_1110;
OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=399550;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA Woese C., Bristow J., Kyrpides N.;
RT "The complete genome sequence of Staphylothermus marinus reveals
RT differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL BMC Genomics 10:145-145(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=21304655; DOI=10.4056/sigs.30527;
RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT type strain F1.";
RL Stand. Genomic Sci. 1:183-188(2009).
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}.
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DR EMBL; CP000575; ABN70206.1; -; Genomic_DNA.
DR RefSeq; WP_011839397.1; NC_009033.1.
DR AlphaFoldDB; A3DNJ6; -.
DR SMR; A3DNJ6; -.
DR STRING; 399550.Smar_1110; -.
DR GeneID; 4908039; -.
DR KEGG; smr:Smar_1110; -.
DR eggNOG; arCOG00070; Archaea.
DR HOGENOM; CLU_022477_2_1_2; -.
DR OrthoDB; 5821at2157; -.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000000254; 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; 3.90.1150.10; 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; IPR019798; Ser_HO-MeTrfase_PLP_BS.
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.
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..439
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_0000369976"
FT BINDING 126..128
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT SITE 231
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT MOD_RES 232
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ SEQUENCE 439 AA; 49466 MW; AA9225483DE402CF CRC64;
MVIDITKKYP ELKEIYELTV NHTIWRKKEC INLIASENVM SPLAMLLYLN DMMHRYAEGK
PFKRFYQGLK FVDELEVKAQ RIIGELLETD YVELRPISGT IANATVFKAF AEHGDKAVVV
PVQAGAHVSH TRYGTLGGLG IEQVEMPFNI EEWNIDVDGA KKVIEKVKPK IVILGGSLYI
FPHPVKEIAE AAHSVGAKLM YDVAHVLGLI TGKVWENPLK QGADILTSST HKTFPGPQGG
LIATVTKDDY KKVSKIVFPV FVSNHHLHRL AALAVTGLEM KYFGRQYAEQ IVKNAKAFAE
ALAENGFKVI GENKGYTESH QVIIDVREHG GGAKNAKLLE EANIIVNKNM LPWDKPEDIK
NPSGIRLGVQ EVTRWGMKEE DMKTIAEFMR LVVIDKRDPK EIRNKVIEFR KNFLEIHYGF
KISGEEETKL LKIMLHGEV
//
