ID A0A1K1NFP8_SELRU Unreviewed; 331 AA.
AC A0A1K1NFP8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN02910323_1339 {ECO:0000313|EMBL:SFW34163.1};
OS Selenomonas ruminantium.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=971 {ECO:0000313|EMBL:SFW34163.1, ECO:0000313|Proteomes:UP000182958};
RN [1] {ECO:0000313|Proteomes:UP000182958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|Proteomes:UP000182958};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000198};
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}.
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DR EMBL; FPJA01000006; SFW34163.1; -; Genomic_DNA.
DR RefSeq; WP_072306019.1; NZ_FPJA01000006.1.
DR AlphaFoldDB; A0A1K1NFP8; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000182958; 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:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
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; cd00209; DHFR; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR001796; DHFR_dom.
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; PF00186; DHFR_1; 1.
DR Pfam; PF01288; HPPK; 1.
DR PRINTS; PR00070; DHFR.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS51330; DHFR_2; 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:SFW34163.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000182958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..331
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 331 AA; 37549 MW; 1FFFCFAF618A22E7 CRC64;
MKIYLSLGAN LGNRGETLRE ALRQIACLPQ TALKAVAPFY ETAPWGNQEQ PAFINTAAMV
ETELSPLNFL HKTQQIELDL GRVRHEHWGA RTIDIDFLWA EGVASDTEEL KLPHPYLTER
AFVLLPLRDI APDLLLQGRA VADWCREEKI QQQEIHPAAE LCEPYPLSMI ACVDEQMGIG
RQGKLLVHHA EDMQHFRQET LGQVVIMGRK TLESLPDGKP LRGRVNIVLS RSLVRDDVLI
CRNLAELWAL LGRLQVEQPR RKFICIGGGE IYSLLLPYAK EIMLTKVTGK FAADTFFPAH
EEFFEAAREA RSGLSFVRLW RAGADYFSPR R
//
