HPPK_MYCTO
ID HPPK_MYCTO Reviewed; 188 AA.
AC P9WNC6; L0TDA6; O06276; P64143;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000250|UniProtKB:P26281};
DE EC=2.7.6.3 {ECO:0000250|UniProtKB:P26281};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000250|UniProtKB:P26281};
DE Short=PPPK {ECO:0000250|UniProtKB:P26281};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase {ECO:0000250|UniProtKB:P26281};
DE Short=HPPK {ECO:0000250|UniProtKB:P26281};
GN Name=folK; OrderedLocusNames=MT3711;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the transfer of pyrophosphate from adenosine
CC triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic
CC step in folate biosynthesis pathway. {ECO:0000250|UniProtKB:P26281}.
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:0000250|UniProtKB:P26281};
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:0000250|UniProtKB:P26281}.
CC -!- SIMILARITY: Belongs to the HPPK family. {ECO:0000305}.
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DR EMBL; AE000516; AAK48069.1; -; Genomic_DNA.
DR PIR; G70955; G70955.
DR RefSeq; WP_003419536.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNC6; -.
DR SMR; P9WNC6; -.
DR DrugCentral; P9WNC6; -.
DR EnsemblBacteria; AAK48069; AAK48069; MT3711.
DR GeneID; 45427592; -.
DR KEGG; mtc:MT3711; -.
DR PATRIC; fig|83331.31.peg.3994; -.
DR HOGENOM; CLU_097916_0_0_11; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000001020; Chromosome.
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: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; -; 1.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR Pfam; PF01288; HPPK; 1.
DR SUPFAM; SSF55083; SSF55083; 1.
DR TIGRFAMs; TIGR01498; folK; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Folate biosynthesis; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..188
FT /note="2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
FT pyrophosphokinase"
FT /id="PRO_0000427150"
SQ SEQUENCE 188 AA; 20732 MW; D14AE440760CDCF4 CRC64;
MTRVVLSVGS NLGDRLARLR SVADGLGDAL IAASPIYEAD PWGGVEQGQF LNAVLIADDP
TCEPREWLRR AQEFERAAGR VRGQRWGPRN LDVDLIACYQ TSATEALVEV TARENHLTLP
HPLAHLRAFV LIPWIAVDPT AQLTVAGCPR PVTRLLAELE PADRDSVRLF RPSFDLNSRH
PVSRAPES