(data stored in SCRATCH zone)

SWISSPROT: B6H2E1_PENRW

ID   B6H2E1_PENRW            Unreviewed;       528 AA.
AC   B6H2E1;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=Pc13g05010 {ECO:0000313|EMBL:CAP91570.1}, PCH_Pc13g05010
GN   {ECO:0000313|EMBL:CAP91570.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91570.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91570.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Interconversion of serine and glycine.
CC       {ECO:0000256|RuleBase:RU000585}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine +
CC         H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine;
CC         Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453;
CC         EC=2.1.2.1; Evidence={ECO:0000256|RuleBase:RU000585};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000412-50,
CC         ECO:0000256|RuleBase:RU000585};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|RuleBase:RU000585}.
CC   -!- SIMILARITY: Belongs to the SHMT family.
CC       {ECO:0000256|RuleBase:RU000585}.
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DR   EMBL; AM920428; CAP91570.1; -; Genomic_DNA.
DR   RefSeq; XP_002558936.1; XM_002558890.1.
DR   STRING; 1108849.XP_002558936.1; -.
DR   PRIDE; B6H2E1; -.
DR   EnsemblFungi; CAP91570; CAP91570; PCH_Pc13g05010.
DR   GeneID; 8312372; -.
DR   KEGG; pcs:Pc13g05010; -.
DR   eggNOG; KOG2467; Eukaryota.
DR   eggNOG; COG0112; LUCA.
DR   HOGENOM; HOG000239405; -.
DR   KO; K00600; -.
DR   OMA; SKYFQTM; -.
DR   OrthoDB; 372408at2759; -.
DR   BioCyc; PCHR:PC13G05010-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00051; SHMT; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; B6H2E1.
DR   SWISS-2DPAGE; B6H2E1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   One-carbon metabolism {ECO:0000256|RuleBase:RU000585};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000412-50,
KW   ECO:0000256|RuleBase:RU000585};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN       57    460       SHMT. {ECO:0000259|Pfam:PF00464}.
FT   MOD_RES     288    288       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000412-50}.
SQ   SEQUENCE   528 AA;  57484 MW;  0F16DD83135E7832 CRC64;
     MYLSRCGRSA ARLLPLGSSR AAVVSARASI VPRLAPQSRG VATSTRDTQH KLLAASLEES
     DPTVWNILQK EKQRQKHFIN LIPSENFTSQ AVLDALGSVM QNKYSEGYPG ARYYGGNEHI
     DASERLCQQR ALETFRLNPE EWGVNVQPLS GSPANLMAYS ALLNTHDRIM GLDLPHGGHL
     SHGYQTPTKK ISAISKYFET FPYRLDESTG LIDYDALEKS ATLYRPKLII AGTSAYSRLI
     DYPRMRAIAD SVGAYLLADM AHISGLVAAD VLPSPFPYSD VVTTTTHKSL RGPRGAMIFY
     RKGVRSTDKK GNPVMYDLEN PINASVFPGH QGGPHNHTIT ALSVALKQAQ SPDFEAYQKT
     VLRNASALAG RLGDSTSNGG LGYNIVSGGT DNHLVLVDLK NRGVDGARVE RVLELCGVAS
     NKNTVPGDKS ALKPGGLRLG TPAMTSRGFQ PEDFTRVADI VDRAVTITQK LDKAARESAQ
     SRGVKNPNTV KAFLDYVGEG EEISEIVVLR QEVEDWVGTF SLPWADDQ
//

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