HPPK_HAEIN
ID HPPK_HAEIN Reviewed; 160 AA.
AC P43777;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=HI_0064;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10080886; DOI=10.1006/jmbi.1999.2623;
RA Hennig M., Dale G.E., D'Arcy A., Danel F., Fischer S., Gray C.P.,
RA Jolidon S., Mueller F., Page M.G.P., Pattison P., Oefner C.;
RT "The structure and function of the 6-hydroxymethyl-7,8-dihydropterin
RT pyrophosphokinase from Haemophilus influenzae.";
RL J. Mol. Biol. 287:211-219(1999).
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P26281}.
CC -!- SIMILARITY: Belongs to the HPPK family. {ECO:0000305}.
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DR EMBL; L42023; AAC21742.1; -; Genomic_DNA.
DR RefSeq; NP_438237.1; NC_000907.1.
DR RefSeq; WP_005693858.1; NC_000907.1.
DR PDB; 1CBK; X-ray; 2.02 A; A/B=1-160.
DR PDBsum; 1CBK; -.
DR AlphaFoldDB; P43777; -.
DR SMR; P43777; -.
DR STRING; 71421.HI_0064; -.
DR DrugBank; DB02278; 7,8-dihydro-7,7-dimethyl-6-hydroxypterin.
DR EnsemblBacteria; AAC21742; AAC21742; HI_0064.
DR KEGG; hin:HI_0064; -.
DR PATRIC; fig|71421.8.peg.65; -.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_097916_0_1_6; -.
DR OMA; QVILRQN; -.
DR PhylomeDB; P43777; -.
DR BioCyc; HINF71421:G1GJ1-65-MON; -.
DR UniPathway; UPA00077; UER00155.
DR EvolutionaryTrace; P43777; -.
DR Proteomes; UP000000579; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Folate biosynthesis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..160
FT /note="2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
FT pyrophosphokinase"
FT /id="PRO_0000168250"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1CBK"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1CBK"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1CBK"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1CBK"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1CBK"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:1CBK"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:1CBK"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1CBK"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1CBK"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1CBK"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:1CBK"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1CBK"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:1CBK"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1CBK"
SQ SEQUENCE 160 AA; 18299 MW; 136CD15F8844FDDD CRC64;
MITAYIALGS NLNTPVEQLH AALKAISQLS NTHLVTTSSF YKSKPLGPQD QPDYVNAVAK
IETELSPLKL LDELQRIENE QGRVRLRRWG ERTLDLDILL YGNEIIQNER LTIPHYDMHN
REFVIVPLFE IASDLVLPNS QIITELVKQF ADHKMIKLNP
