ID F5J2P7_9BACT Unreviewed; 135 AA.
AC F5J2P7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase {ECO:0000256|ARBA:ARBA00013253};
DE EC=2.7.6.3 {ECO:0000256|ARBA:ARBA00013253};
GN ORFNames=HMPREF9455_03614 {ECO:0000313|EMBL:EGK00025.1};
OS Dysgonomonas gadei ATCC BAA-286.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=742766 {ECO:0000313|EMBL:EGK00025.1, ECO:0000313|Proteomes:UP000004913};
RN [1] {ECO:0000313|EMBL:EGK00025.1, ECO:0000313|Proteomes:UP000004913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-286 {ECO:0000313|EMBL:EGK00025.1,
RC ECO:0000313|Proteomes:UP000004913};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dysgonomonas gadei ATCC BAA-286.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:EGK00025.1}.
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DR EMBL; ADLV01000044; EGK00025.1; -; Genomic_DNA.
DR AlphaFoldDB; F5J2P7; -.
DR STRING; 742766.HMPREF9455_03614; -.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_097916_4_1_10; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000004913; 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: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 Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000004913};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..133
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|Pfam:PF01288"
SQ SEQUENCE 135 AA; 15406 MW; 5B80F4DA7B9AFA33 CRC64;
MIKEIECIFA SVMNKALLSI GTNEDRESNL SLCHQFLNNI FTDISYSDSS VTMPYGTIYR
NDFLNQLAVI YTDRDMDEVI RLLKSIEKDM GRNGADKKNG IVKIDIDLVI WNNSVLKPED
FTRSYIADLL ASLDK
//