ID A0A090DVK0_9BACT Unreviewed; 172 AA.
AC A0A090DVK0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 Name=folK {ECO:0000313|EMBL:CDR33009.1};
GN ORFNames=CSEC_0170 {ECO:0000313|EMBL:CDR33009.1};
OS Criblamydia sequanensis CRIB-18.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC Criblamydia.
OX NCBI_TaxID=1437425 {ECO:0000313|EMBL:CDR33009.1, ECO:0000313|Proteomes:UP000031552};
RN [1] {ECO:0000313|EMBL:CDR33009.1, ECO:0000313|Proteomes:UP000031552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR33009.1,
RC ECO:0000313|Proteomes:UP000031552};
RA Linke B.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDR33009.1, ECO:0000313|Proteomes:UP000031552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR33009.1,
RC ECO:0000313|Proteomes:UP000031552};
RA Bertelli C., Goesmann A., Greub G.;
RT "Criblamydia sequanensis harbors a mega-plasmid encoding arsenite
RT resistance.";
RL Submitted (SEP-2014) 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:CDR33009.1}.
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DR EMBL; CCEJ010000001; CDR33009.1; -; Genomic_DNA.
DR RefSeq; WP_041016511.1; NZ_CCEJ010000001.1.
DR AlphaFoldDB; A0A090DVK0; -.
DR STRING; 1437425.CSEC_0170; -.
DR eggNOG; COG0801; Bacteria.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000031552; 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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDR33009.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDR33009.1}.
FT DOMAIN 7..135
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|Pfam:PF01288"
SQ SEQUENCE 172 AA; 19890 MW; B92000C5A575314C CRC64;
MAAQDVYLGL GGNIGDTKEI FRSVVNTLKG FSDCEWVGIS KLYRTSPVSS IPQPHFLNAA
CHLRTTSNLE FFFERIESLE KAHGKIDKTK DEPRTIDIDL LFFGKEVRMD QKLSLPHPRW
SERLFVLIPL FDLTPVIHFP LNDLKFDEIN LLEKIRTFDN KQNECVLFDS FL
//
