ID Q31FF4_HYDCU Unreviewed; 170 AA.
AC Q31FF4;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000256|ARBA:ARBA00016218};
DE EC=2.7.6.3 {ECO:0000256|ARBA:ARBA00013253};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000256|ARBA:ARBA00029766};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase {ECO:0000256|ARBA:ARBA00033413};
GN OrderedLocusNames=Tcr_1527 {ECO:0000313|EMBL:ABB42119.1};
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB42119.1};
RN [1] {ECO:0000313|EMBL:ABB42119.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XCL-2 {ECO:0000313|EMBL:ABB42119.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C.,
RA Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J.,
RA Richardson P.;
RT "Complete sequence of Thiomicrospira crunogena XCL-2.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00029409}.
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 HPPK family.
CC {ECO:0000256|ARBA:ARBA00005810}.
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DR EMBL; CP000109; ABB42119.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31FF4; -.
DR STRING; 317025.Tcr_1527; -.
DR KEGG; tcx:Tcr_1527; -.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_097916_2_3_6; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00155.
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; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
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; PF01288; HPPK; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABB42119.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABB42119.1}.
FT DOMAIN 91..102
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
SQ SEQUENCE 170 AA; 19024 MW; 3A773D7586BEABFD CRC64;
MAAWQDVYIG LGSNLSNPEE QVLNALDSLK TLPESQWVTH SKLYFSRPQG PQDQPDFVNA
VALLKTQLSP VALLDCLQAL EAAQGKVKQR HWGERLIDLD IVLYGNETLN TERLTIPHPF
MAERDFVLLP LAEISPGLIL PNGSKIKDLI AELPEGFIIN DRTAEKNREK
//
