ID A0A095C687_CRYGR Unreviewed; 499 AA.
AC A0A095C687;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN ORFNames=CNBG_1047 {ECO:0000313|EMBL:KGB75209.1};
OS Cryptococcus gattii serotype B (strain R265) (Filobasidiella gattii)
OS (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=294750 {ECO:0000313|EMBL:KGB75209.1, ECO:0000313|Proteomes:UP000029445};
RN [1] {ECO:0000313|EMBL:KGB75209.1, ECO:0000313|Proteomes:UP000029445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R265 {ECO:0000313|EMBL:KGB75209.1};
RX PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
RN [2] {ECO:0000313|EMBL:KGB75209.1, ECO:0000313|Proteomes:UP000029445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R265 {ECO:0000313|EMBL:KGB75209.1};
RX PubMed=29507212;
RA Yadav V., Sun S., Billmyre R.B., Thimmappa B.C., Shea T., Lintner R.,
RA Bakkeren G., Cuomo C.A., Heitman J., Sanyal K.;
RT "RNAi is a critical determinant of centromere evolution in closely related
RT fungi.";
RL Proc. Natl. Acad. Sci. 115:3108-3113(2018).
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000256|ARBA:ARBA00002224, ECO:0000256|RuleBase:RU000585}.
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:0000256|ARBA:ARBA00001528,
CC ECO:0000256|RuleBase:RU000585};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000412-50, ECO:0000256|RuleBase:RU000585};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU000585}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC ECO:0000256|RuleBase:RU000585}.
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DR EMBL; CP025760; KGB75209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095C687; -.
DR STRING; 294750.A0A095C687; -.
DR VEuPathDB; FungiDB:CNBG_1047; -.
DR HOGENOM; CLU_022477_0_2_1; -.
DR OMA; HGMALNM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000029445; Chromosome 2.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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:SF35; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 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 Methyltransferase {ECO:0000313|EMBL:KGB75209.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000585};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000412-50};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 41..428
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 499 AA; 54437 MW; 50CD3156FBD46EF0 CRC64;
MPRLILAAFR TTIRPAISKQ IRMASSVPVP TDFNACLYKP LAEADPEINS LIEKETWRQF
SGLELIASEN LTSLAVMEAN GSMLTNKYSE GLPGARYYGG NEYIDVIENL TRERALKAFN
LDPKVWGVNV QPYSGSTANF AAFTALISPQ DRVMGLGLPD GGHLTHGYYT AKKKITASSI
YFQSFPYRVD PKTGIIDYPQ LETNANLFKP RLLVCGGSAY PRDWDYGRLR KIADGQGAYL
MSDMAHISGL VAAAEQNSPF EYCDVVTTTT HKTLRGPRAG LIFFRKDKES DLEARVNAAV
FPACQGGPHN NTIAGIAVAL KQAADPAFKE YAKQVRANAA SMASVLFKHG YRLQTDGTEN
HLILWDLRPI GLTGSKVEKI CDAAHITLNK NAVAGDTSAL VPGGVRIGTS ALTSRSMKEQ
DVEKVAEFLH RVVQIALKTQ EEAGSKLLKD FVKAYESGNG EAPKLIAELK EDVMKFATSF
PLPGIPDSSK IVRPEGVNL
//
