ID H2AUI1_KAZAF Unreviewed; 785 AA.
AC H2AUI1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Folic acid synthesis protein fol1 {ECO:0000256|PIRNR:PIRNR000741};
GN Name=KAFR0D03830 {ECO:0000313|EMBL:CCF58031.1};
GN ORFNames=KAFR_0D03830 {ECO:0000313|EMBL:CCF58031.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58031.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58031.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Catalyzes three sequential steps of tetrahydrofolate
CC biosynthesis. {ECO:0000256|PIRNR:PIRNR000741}.
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 ECO:0000256|PIRNR:PIRNR000741};
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, ECO:0000256|PIRNR:PIRNR000741}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
CC {ECO:0000256|ARBA:ARBA00009640, ECO:0000256|PIRNR:PIRNR000741}.
CC -!- SIMILARITY: In the central section; belongs to the HPPK family.
CC {ECO:0000256|PIRNR:PIRNR000741}.
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DR EMBL; HE650824; CCF58031.1; -; Genomic_DNA.
DR RefSeq; XP_003957166.1; XM_003957117.1.
DR AlphaFoldDB; H2AUI1; -.
DR STRING; 1071382.H2AUI1; -.
DR GeneID; 13882276; -.
DR KEGG; kaf:KAFR_0D03830; -.
DR eggNOG; KOG2544; Eukaryota.
DR HOGENOM; CLU_008023_2_0_1; -.
DR InParanoid; H2AUI1; -.
DR OrthoDB; 5411at2759; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000005220; Chromosome 4.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR016261; Folic_acid_synth.
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 PIRSF; PIRSF000741; Folic_acid_synth; 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; PS00794; HPPK; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000741};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|PIRNR:PIRNR000741};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000741};
KW Lyase {ECO:0000256|PIRNR:PIRNR000741};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000741};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000741};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000741}.
FT DOMAIN 475..775
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 785 AA; 89219 MW; 8B4CF5B105FDF5A7 CRC64;
MKMNKDNLHI KNLKLKTITG PNLWNQIQPQ NCRLSVDVET NFSECSRTDD LKYSLNYASL
ASDITKFVKK KENWNSLNNL SKSVYDYVQD YKKSIKSLEV SIQNENLHAR TNKISWCYGN
RFNRLMINDL KVMTIIGIFN FERVQKQTIS IDLTIESKNI NSCSFPIKKI INDCVTFTEN
SDFKTVEALA EAINNIVAEI IDTDEDTIVT VKVMKLNAIT DTDSVGVSCQ RKASKLINAH
QKLPSTERIK AEQPSFDNET VTNGQNTVYL SFGSNIGDRI MNIQEAIKIL DEHESITVKN
ISSFFESEPM YYLNQNQFIN GCVECQTILT PRELLKAIKD IEYNKLNRVK EFDNGPRTLD
LDIIMYLDSK GNQIIVNEPD LIVPHDKMLE RSFVLEPLCE LIPSNFEHPI STEPISKHLS
AIYERGNDED YLWKVIPIPN HNKETEKGTR FLKFKTICKT NEFTAKRKRI TISPTYLMGI
LNTTPDSFSD GGKYNTLEKQ LDCIKVMCQE HFKLHENIII DVGGCSTRPN SVQATVEEEL
ARTIPIIEQI RQCKELPQDK IIISIDTYRS EVAEKAIQVG ADIINDISGG AFDSDLFNII
SSHPNVAYVL SHTRGDIATM TKLTSYDEFT GSEGCEFFNE EEYTGNNLKF IRVLGRELAT
RYQIALSKGV RRWQIIVDPG LGFAKDLNSN LKVIRELPFL KNYSFLEDGT NNYTSFRNLP
FLLGPSRKKF IGTITKDDDA QNRDFATGSI VASCIGFGAD LVRVHNVADC SKSIKLADAT
YKLLE
//
