GLYC2_DICDI
ID GLYC2_DICDI Reviewed; 481 AA.
AC Q54EW1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Serine hydroxymethyltransferase 2;
DE Short=SHMT 2;
DE EC=2.1.2.1 {ECO:0000250|UniProtKB:P34896};
DE AltName: Full=Glycine hydroxymethyltransferase 2;
DE AltName: Full=Serine methylase 2;
GN Name=shmt2; ORFNames=DDB_G0291652;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000250|UniProtKB:P34896}.
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:0000250|UniProtKB:P34896};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P34896};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000250|UniProtKB:P34896}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P34896}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61810.1; -; Genomic_DNA.
DR RefSeq; XP_635129.1; XM_630037.1.
DR AlphaFoldDB; Q54EW1; -.
DR SMR; Q54EW1; -.
DR STRING; 44689.DDB0230073; -.
DR PaxDb; Q54EW1; -.
DR EnsemblProtists; EAL61810; EAL61810; DDB_G0291652.
DR GeneID; 8628075; -.
DR KEGG; ddi:DDB_G0291652; -.
DR dictyBase; DDB_G0291652; shmt2.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_2_1; -.
DR InParanoid; Q54EW1; -.
DR OMA; VTNRNAI; -.
DR PhylomeDB; Q54EW1; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:Q54EW1; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:dictyBase.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..481
FT /note="Serine hydroxymethyltransferase 2"
FT /id="PRO_0000327958"
FT MOD_RES 264
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P34896"
SQ SEQUENCE 481 AA; 53584 MW; FF08CBD911B2F727 CRC64;
MLKSLSKLTP SIRGVVSINR SFCTKKFLPT NRSVSESDPE IYDLMMKEKQ RQFTGLELIA
SENFTSRAVM ESIGSCFTNK YAEGLPGARY YGGNEVVDQL ENLCIKRALE TFNLNPEEWG
VNVQPYSGST ANFAAFTGLL KPHDRIMGLD LPSGGHLTHG YQTDKKKISA TSIFFESMPY
QVNETGYVDY NKMEANAALF RPKLLIAGAS AYPREWDYER MRKIADKHGA YLLCDMAHIS
GMVAGKQAIS PFLFCDVVTT TTHKTLRGPR AGLIFFRKTK RRDAKGNIID DDLENRINFA
VFPSCQGGPH ENTIAGIAVA LKEASSPDFQ EYTKQVRRNS QTMGEELKKR GYSLVTEGTD
NHLVLWDLRP QGITGSKIEK ACDEAHITVN KNAVYGDTNA IAPGGVRLGA PALTSRGLKE
QDFVKVVDFL DRVVKISLDI QSKVGKKMPD FQRAIADNQD LKQIRQEVKE FSTKFGMPGE
L
