GLYA_SACS2
ID GLYA_SACS2 Reviewed; 433 AA.
AC Q9UWT5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=SSO0530;
GN ORFNames=C22_021;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, MODIFIED FOLATE-DEPENDENT SERINE
RP HYDROXYMETHYLTRANSFERASE ACTIVITY, CATALYTIC ACTIVITY, ALDOLASE ACTIVITY,
RP COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=9393711; DOI=10.1128/jb.179.23.7456-7461.1997;
RA Delle Fratte S., White R.H., Maras B., Bossa F., Schirch V.;
RT "Purification and properties of serine hydroxymethyltransferase from
RT Sulfolobus solfataricus.";
RL J. Bacteriol. 179:7456-7461(1997).
CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC glycine with the modified folate sulfopterin serving as the one-carbon
CC carrier. Cannot use tetrahydrofolate (THF or H4PteGlu) as the pteridine
CC substrate. Also exhibits a pteridine-independent aldolase activity
CC toward beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC retro-aldol mechanism. Thus, is able to catalyze the cleavage of both
CC allo-threonine and beta-phenylserine. {ECO:0000269|PubMed:9393711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methylenetetrahydrosulfopterin + glycine + H2O = L-serine
CC + tetrahydrosulfopterin; Xref=Rhea:RHEA:56608, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:140605,
CC ChEBI:CHEBI:140606;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051,
CC ECO:0000269|PubMed:9393711};
CC -!- ACTIVITY REGULATION: Is completely inhibited by addition of NaCNBH(3)
CC in vitro; this reagent is a known inhibitor of PLP enzymes, that
CC reduces the internal aldimine of PLP to the catalytically inactive and
CC stable secondary amine. Is also inhibited by L-cysteine, which forms a
CC thiazolidine complex with the active site PLP.
CC {ECO:0000269|PubMed:9393711}.
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 ECO:0000305|PubMed:9393711}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00051, ECO:0000305}.
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DR EMBL; Y18930; CAB57769.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40850.1; -; Genomic_DNA.
DR PIR; C90199; C90199.
DR RefSeq; WP_009991046.1; NC_002754.1.
DR AlphaFoldDB; Q9UWT5; -.
DR SMR; Q9UWT5; -.
DR STRING; 273057.SSO0530; -.
DR EnsemblBacteria; AAK40850; AAK40850; SSO0530.
DR GeneID; 44129548; -.
DR KEGG; sso:SSO0530; -.
DR PATRIC; fig|273057.12.peg.529; -.
DR eggNOG; arCOG00070; Archaea.
DR HOGENOM; CLU_022477_2_1_2; -.
DR InParanoid; Q9UWT5; -.
DR OMA; SHPAGLI; -.
DR PhylomeDB; Q9UWT5; -.
DR BRENDA; 2.1.2.1; 6163.
DR UniPathway; UPA00288; UER01023.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:InterPro.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing;
KW One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..433
FT /note="Serine hydroxymethyltransferase"
FT /id="PRO_0000113725"
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 243
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"
SQ SEQUENCE 433 AA; 48509 MW; 8C239FA0FA3A285E CRC64;
MSLPKELEKV LEITKAQNVW RRTQTLNLIA SENVMSPLAE SVYMSDFMSR YAEGKPYKRY
YQGTKYTDEI ETLTMELMNE ITNSKDCDLR PTSGTIANAA VFRVLAEPGD KALIAPVQAG
AHVSHTKFGT LGALGIQHIE MPFDEENINV DVDKAIKMIE EVKPKFVVLG GSLYLFPHPT
KELAQHVHAV GAKLVYDAAH VYGLIEGKVW SNPLKDGADI MTVSTHKTFP GPQGGAIFSD
GSEVFKQVSK TIFPWFVSNH HLHRLPATAV TAIEMKYFGE SYANQILRNS KALAEALAER
GFKVIGENLG YTKSHQVAVD VRQFGGGNKI AKLLEDANII VNKNLLPYDK PEDVSDPSGL
RIGVQEMTRY GMKEGEMEEI AELFKKVIID KKDVNEVKKE VIEMRRNFLE VKYTFDDMKD
LEKYSSKSLK LII
