ID C4R281_KOMPG Unreviewed; 775 AA.
AC C4R281;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Multifunctional enzyme of the folic acid biosynthesis pathway {ECO:0000313|EMBL:CAY69605.1};
GN OrderedLocusNames=PAS_chr2-2_0302 {ECO:0000313|EMBL:CAY69605.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY69605.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY69605.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000012};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-
CC 6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841,
CC ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004763}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
CC {ECO:0000256|ARBA:ARBA00009951}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
CC {ECO:0000256|ARBA:ARBA00009640}.
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DR EMBL; FN392320; CAY69605.1; -; Genomic_DNA.
DR RefSeq; XP_002491885.1; XM_002491840.1.
DR AlphaFoldDB; C4R281; -.
DR SMR; C4R281; -.
DR STRING; 644223.C4R281; -.
DR EnsemblFungi; CAY69605; CAY69605; PAS_chr2-2_0302.
DR GeneID; 8198202; -.
DR KEGG; ppa:PAS_chr2-2_0302; -.
DR eggNOG; KOG2544; Eukaryota.
DR HOGENOM; CLU_008023_2_0_1; -.
DR InParanoid; C4R281; -.
DR OMA; LFESEPM; -.
DR OrthoDB; 5411at2759; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000000314; Chromosome 2.
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:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; cd00739; DHPS; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.1130.10; -; 2.
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; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR NCBIfam; TIGR00526; folB_dom; 2.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF02152; FolB; 2.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SMART; SM00905; FolB; 2.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 2.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS00794; HPPK; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 478..769
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 775 AA; 86377 MW; BEA49785D87A964C CRC64;
MISGTSKSPD LVKISRLHFN AQLTNGNFWH QTSLQPFTCS VILKTDFFKA SETDDLRYSL
NYATISNNIL SVFRNSDEVY GSIESIAHRI AESVFSDESN GRSAEISVSS EKSEIRCDSI
DLSISRYRKN DSTNELIAPS LDKFTFKGLN LFTIIGVYTF ERYNKQSVVL NLSVHYNTNK
DKLKFSQLTE TVSSYVESTQ FKTVEALAGN VASLVLQEFE FIEAADVEVV KLNAIIFADG
VGVATSKLRN QLQRSKIVVN PTKSEFSTLP NLNKETSFEG HPNIENHRVF IAFGTNEGDY
LENIEKTIIE LDKRGCKVEK TSSLYESAPM YHLDQARFQN GVFQISTKLS PRDLLKTLKE
IEYGELKRVK HFDNGPRTID LDILLYDDLI HDEPDLKIPH VSLIERNFVL YPLCDLLPPT
AIHPVTAEPF HQHLKKLSAH DTSIQADDGL VNIIPIPSIP NRKADIRIDT IGNKLTKSLV
MAVLNVTPDS FSDGGLHNTN ESIISVYEEM VHSGVDIIDI GGVSTRPGAA APSEEEELSR
VIPAIQLIRN HEKENNLQPQ VISVDTFRSQ VALKSLESGA NIVNDISGGR FDEQIFDVVA
KFGAPYMVGH TRGENMTDMH THTKYKHTQK IGEVEFWQSS PLIDTIGREI AESIQLATRK
GVKRWQLIVD PGLGFAKTVE QNISLIRNLP NLAKYGVEAD GDYQSLHRVP FLLGPSRKRF
IGVITGEELP RSVGTCAAVM SCIGFGGHLI RVHDFKAVKV TCGMADAIYK GLIQS
//
