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Database: UniProt
Entry: E0DDL6_9CORY
LinkDB: E0DDL6_9CORY
Original site: E0DDL6_9CORY 
ID   E0DDL6_9CORY            Unreviewed;       161 AA.
AC   E0DDL6;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:EFM49535.1};
GN   ORFNames=HMPREF0299_7533 {ECO:0000313|EMBL:EFM49535.1};
OS   Corynebacterium matruchotii ATCC 14266.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM49535.1, ECO:0000313|Proteomes:UP000004218};
RN   [1] {ECO:0000313|EMBL:EFM49535.1, ECO:0000313|Proteomes:UP000004218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM49535.1,
RC   ECO:0000313|Proteomes:UP000004218};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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:EFM49535.1}.
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DR   EMBL; ACSH02000004; EFM49535.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0DDL6; -.
DR   STRING; 553207.HMPREF0299_7533; -.
DR   eggNOG; COG0801; Bacteria.
DR   OrthoDB; 9808041at2; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000004218; 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.
DR   PROSITE; PS00794; 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:EFM49535.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004218};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFM49535.1}.
FT   DOMAIN          84..95
FT                   /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT                   /evidence="ECO:0000259|PROSITE:PS00794"
SQ   SEQUENCE   161 AA;  18220 MW;  415288887E5A3E25 CRC64;
     MIRAVLSIGS NMDDRYALLE TVFEEFRDET IAQSPIYSTP PWGVPDQDEF LNAILIVNVA
     QTPRELLRRG QHLEAAAERR RTRKWGPRTL DVDIIQVIDA NGVELVSEDP ELILPHPWAR
     HRAFVLVPWL AADPEARLLG VPVREIVEKL DIADVEAVVE A
//
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