ID A0A1V8SRB5_9PEZI Unreviewed; 493 AA.
AC A0A1V8SRB5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN ORFNames=B0A48_06947 {ECO:0000313|EMBL:OQO08153.1}, B0A48_12600
GN {ECO:0000313|EMBL:OQO01564.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO01564.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|EMBL:OQO01564.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCFEE 5527 {ECO:0000313|EMBL:OQO01564.1};
RX PubMed=28684563;
RA Coleine C., Masonjones S., Selbmann L., Zucconi L., Onofri S., Pacelli C.,
RA Stajich J.E.;
RT "Draft Genome Sequences of the Antarctic Endolithic Fungi Rachicladosporium
RT antarcticum CCFEE 5527 and Rachicladosporium sp. CCFEE 5018.";
RL Genome Announc. 5:e00397-17(2017).
RN [2] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OQO01564.1}.
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DR EMBL; NAJO01000030; OQO01564.1; -; Genomic_DNA.
DR EMBL; NAJO01000013; OQO08153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SRB5; -.
DR STRING; 1507870.A0A1V8SRB5; -.
DR InParanoid; A0A1V8SRB5; -.
DR OrthoDB; 5358603at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000192596; Unassembled WGS sequence.
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:SF66; 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:OQO01564.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 36..439
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 493 AA; 54205 MW; FEDEAF692FA2D4F4 CRC64;
MNGTKTNGVN GTNGDHATAT YALPKSHQDL MERSLVDTDP EIAEIMEKEI KRQRESILLI
ASENVTSRAV FDALGSPMSN KYSEGYPGAR YYGGNEHIDA IELTCQKRAL ETFGLEPEKW
GVNVQCLSGS PANLQVYQAI MRPHERLMGL DLPHGGHLSH GYQTPTKKIS AVSTYFETFP
YRVNLDTGII DYDELEKNAL MYRPKVIVAG TSAYCRTIDY ARMRQIADVV GCYLVVDMAH
ISGLIAGRVN DSPFPHADIV TTTTHKSLRG PRGAMIFFRK GVRKTETKGG KEIQTLYDLE
GPINFSVFPG HQGGPHNHTI TALAVALKQA QTEDFRLYQQ QVIKNAKQLE HSFKALGYTL
VTGGTDNHMV LLDLKPISNP GLDGARVEAV LEQVNIACNK NTTPGDKSAL TPCGIRIGAP
AMTSRGMGEK DFERIAGYID QCIKLAQKIQ KELPKEANKQ KDFKAKVQGG EVEEIKSLKA
EIAAWAGTFP LPV
//
