ID W9GBL4_9MICO Unreviewed; 295 AA.
AC W9GBL4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Bifunctional folate synthesis protein {ECO:0000256|RuleBase:RU362079};
DE Includes:
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE Short=DHNA {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE Includes:
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE EC=2.7.6.3 {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE Short=PPPK {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE Short=HPPK {ECO:0000256|RuleBase:RU362079};
GN ORFNames=N865_09020 {ECO:0000313|EMBL:EWT03581.1};
OS Intrasporangium oryzae NRRL B-24470.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT03581.1, ECO:0000313|Proteomes:UP000019489};
RN [1] {ECO:0000313|EMBL:EWT03581.1, ECO:0000313|Proteomes:UP000019489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT03581.1,
RC ECO:0000313|Proteomes:UP000019489};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin +
CC glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25;
CC Evidence={ECO:0000256|RuleBase:RU362079};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 3/4.
CC {ECO:0000256|RuleBase:RU362079}.
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 -!- SIMILARITY: Belongs to the DHNA family.
CC {ECO:0000256|RuleBase:RU362079}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
CC {ECO:0000256|ARBA:ARBA00009640}.
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:EWT03581.1}.
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DR EMBL; AWSA01000001; EWT03581.1; -; Genomic_DNA.
DR RefSeq; WP_034800296.1; NZ_AWSA01000001.1.
DR AlphaFoldDB; W9GBL4; -.
DR STRING; 1386089.N865_09020; -.
DR PATRIC; fig|1386089.3.peg.65; -.
DR eggNOG; COG0801; Bacteria.
DR eggNOG; COG1539; Bacteria.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000019489; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; cd00534; DHNA_DHNTPE; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR NCBIfam; TIGR00525; folB; 1.
DR NCBIfam; TIGR00526; folB_dom; 1.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR43071; 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR43071:SF1; 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE; 1.
DR Pfam; PF02152; FolB; 1.
DR Pfam; PF01288; HPPK; 1.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU362079};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EWT03581.1};
KW Lyase {ECO:0000256|RuleBase:RU362079};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019489};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 207..218
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 295 AA; 31456 MW; ED0CE6DB393611C7 CRC64;
MTDRIVLQGV SARGTHGVLD FEKRDGQTFV VDVTMTLDLA PAGRSDDLAR TVNYAAVADA
VVARISGPSF DLIERLAEVI ADDVLTHDRV DAVEVVVHKP EAPVGHPFTD VQVRIVRTGA
PQVVIALGSN LGDRGQTLAA AVDELRSKAG ITVTSVSPIV ETDPVGGPEQ PPYLNAVVVG
RSDLPPRHLL DTLHSIEASH GRTREVRWGA RTLDLDLIAY GAPGSRHEVV SDDPELTLPH
PRARERAFVL VPWEAADARA RLRVGVGDGG IRPVSELLAG VDRSGVRPGP DWGNA
//