ID B2G491_ZYGRO Unreviewed; 537 AA.
AC B2G491;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase {ECO:0000256|ARBA:ARBA00013253};
DE EC=2.7.6.3 {ECO:0000256|ARBA:ARBA00013253};
DE Flags: Fragment;
GN Name=Zr_FOL1 {ECO:0000313|EMBL:CAQ43400.1};
GN ORFNames=Zrou_4p1 {ECO:0000313|EMBL:CAQ43400.1};
OS Zygosaccharomyces rouxii (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=4956 {ECO:0000313|EMBL:CAQ43400.1};
RN [1] {ECO:0000313|EMBL:CAQ43400.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 732 {ECO:0000313|EMBL:CAQ43400.1};
RA Gordon J.L., Wolfe K.H.;
RT "Zygosaccharomyces rouxii homologs of Saccharomyces cerevisiae chromosome
RT III.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005051}.
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DR EMBL; AM989983; CAQ43400.1; -; Genomic_DNA.
DR AlphaFoldDB; B2G491; -.
DR UniPathway; UPA00077; UER00155.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS00794; HPPK; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 223..528
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAQ43400.1"
SQ SEQUENCE 537 AA; 61183 MW; 8904A23D1F6395B7 CRC64;
DLPIYSDEIK TNTDDRWNKA YLAFGSNLGD RFQNIQLAID LLKTNPQVTV NQVSSLFESE
PMYFTNQNLF MNGCIEISTN LKPLELLKLC KEIEYKELKR VKQIDNGPRT IDLDIIMYLN
ADNEQVLLND SELTIPHARM LERSFVLEPL CELVPFDLIH PLTCEPLTSH LSQIYAKGNL
EDQLWKLIPL PTINGHNRFL KFKTVEKFDD FTGKTTMVSQ SPSYMMCVLN TTPDSFSDGN
EFYHNLDKQL DRVQHMYDEG LKLHDSIIID IGGCSTRPNS EQIEQDIELQ RTVPLIKAIR
SRKDWEQEKI IISIDTYRSQ VALKTIEAGA DMINDISGGT FDASMFDVVA QHPEVSYVLS
HTRGDISNMV HMAKYDDDGL ESGDTQTKEF MFYQRLPSKT GTNVIRSIAR EISDRYSWAL
LKNVRRWQLV LDPGLGFAKN GKNNLQVIRH LSLLKNYCKF TKDGEYVNFR NIPILVGPSR
KAFIGKITDE PDASKRDFAT GSVITSCVGF GADVIRIHDY ANCSKAIRMA DAIYKGV
//
