ID A0A3P3W065_9MICO Unreviewed; 310 AA.
AC A0A3P3W065;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Name=folK {ECO:0000313|EMBL:RRJ88370.1};
GN ORFNames=EG850_01685 {ECO:0000313|EMBL:RRJ88370.1};
OS Gulosibacter macacae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Gulosibacter.
OX NCBI_TaxID=2488791 {ECO:0000313|EMBL:RRJ88370.1, ECO:0000313|Proteomes:UP000274391};
RN [1] {ECO:0000313|EMBL:RRJ88370.1, ECO:0000313|Proteomes:UP000274391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102482-1 {ECO:0000313|EMBL:RRJ88370.1,
RC ECO:0000313|Proteomes:UP000274391};
RA Li G., Jiang Y.;
RT "YIM 102482-1 draft genome.";
RL Submitted (NOV-2018) 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:RRJ88370.1}.
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DR EMBL; RQVS01000002; RRJ88370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3W065; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000274391; 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:RRJ88370.1};
KW Lyase {ECO:0000256|RuleBase:RU362079};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000274391};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RRJ88370.1}.
FT DOMAIN 239..250
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 310 AA; 34684 MW; 88A10003F42A0485 CRC64;
MPTRPGPAAH PALPAPELDR ITIDRLHVRG RHGVFAHERA EGQDFYIDAE VWLDTRAAAQ
SDDIEDTLHY GHLMRALYQV ALREPVDLLE TLAERLAAVT FAFNGPQAVR ITVHKPQAPV
KLRFNDVAVS VLRYRPEGPE PETPRRPHAR AVIALGANLG DREAAIREAM DAIEALDGVW
PHRRSSIYET PALTTHGVDE SVPAYLNAVI TLHTDLDPHK LLDELNRIED AHGRERVERW
GSRTLDLDLI EHGDLESADE RLELPHPRAF ERAFVLAPWA EIEPDASLTG RGPIAELLAN
AADRVERYRA
//
