ID A0A2N5SRV5_9BASI Unreviewed; 524 AA.
AC A0A2N5SRV5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN ORFNames=PCANC_05587 {ECO:0000313|EMBL:PLW54505.1}, PCANC_12391
GN {ECO:0000313|EMBL:PLW41147.1}, PCASD_01701
GN {ECO:0000313|EMBL:PLW50276.1}, PCASD_19868
GN {ECO:0000313|EMBL:PLW15920.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW15920.1, ECO:0000313|Proteomes:UP000235392};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW41147.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW15920.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLW15920.1}.
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DR EMBL; PGCI01000785; PLW15920.1; -; Genomic_DNA.
DR EMBL; PGCJ01000172; PLW41147.1; -; Genomic_DNA.
DR EMBL; PGCI01000011; PLW50276.1; -; Genomic_DNA.
DR EMBL; PGCJ01000045; PLW54505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5SRV5; -.
DR STRING; 200324.A0A2N5SRV5; -.
DR OrthoDB; 5358603at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; Unassembled WGS sequence.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
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: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 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 Reference proteome {ECO:0000313|Proteomes:UP000235388};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 68..456
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 299
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 524 AA; 57423 MW; 6B253790B873C757 CRC64;
MASTVLRRGR ALLPPRTPAL RTLRSTHRYS MTRTNSGIIA AAAARPPLCS ASMSLSTQPY
NQLLYTPLSE YDPEVQKIIE DETYRQFSGL ELIASENLTS LAVMQANGSI LTNKYSEGLP
GARYYGGNEH IDKLEILCQQ RALKAFRLDP QVWGVNVQPY SGSTANFATF TALIEPQDRI
MGLGLPDGGH LTHGFYTAKR KISASSIYFQ SFPYNINPQS KLIDYDYLEQ TAKVFKPRIL
ICGASAYPRD WDYSRLRKIA DDQGAYLMMD MAHISGLVAG QVQNNPFEQC DVVTTTTHKT
LRGPRAGLIF FRKDKDASIE SRINNAVFPA CQGGPHNNTI AAIAVALKQA ADPSFQQYAQ
AVIQNSRALA ARLVELGYSL QTGGSDNHLV LWDLRPIGLT GSKVEKICDL CHITINKNAV
SGDTSAQVPG GVRLGTSALT SRSMGPSEMV EVANFMHRVV QISLKLQEEA GSKQLKDFLN
RATQGDGEGK KLLAQLHHDV GTFSRRFGLP GVDVNSIKKP PSEA
//
