FOLKE_LACLA
ID FOLKE_LACLA Reviewed; 349 AA.
AC Q9CGE3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Bifunctional protein FolKE;
DE Includes:
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase;
DE EC=2.7.6.3;
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase;
DE Short=PPPK;
DE AltName: Full=7,8 dihydro-6-hydroxymethylpterin-pyrophosphokinase;
DE Short=HPPK;
DE Includes:
DE RecName: Full=GTP cyclohydrolase 1;
DE EC=3.5.4.16;
DE AltName: Full=GTP cyclohydrolase I;
DE Short=GTP-CH-I;
GN Name=folKE; OrderedLocusNames=LL1154; ORFNames=L0175;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
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 -!- SUBUNIT: Homomer. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HPPK family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; AE005176; AAK05252.1; -; Genomic_DNA.
DR PIR; B86769; B86769.
DR RefSeq; NP_267310.1; NC_002662.1.
DR RefSeq; WP_010905789.1; NC_002662.1.
DR AlphaFoldDB; Q9CGE3; -.
DR SMR; Q9CGE3; -.
DR STRING; 272623.L0175; -.
DR PaxDb; Q9CGE3; -.
DR EnsemblBacteria; AAK05252; AAK05252; L0175.
DR KEGG; lla:L0175; -.
DR PATRIC; fig|272623.7.peg.1234; -.
DR eggNOG; COG0302; Bacteria.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_775655_0_0_9; -.
DR OMA; HPEAFNR; -.
DR UniPathway; UPA00077; UER00155.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000002196; Chromosome.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 1.10.286.10; -; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR Gene3D; 3.30.70.560; -; 1.
DR HAMAP; MF_00223; FolE; 1.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR043134; GTP-CH-I_N.
DR InterPro; IPR001474; GTP_CycHdrlase_I.
DR InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR PANTHER; PTHR11109; PTHR11109; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 1.
DR Pfam; PF01288; HPPK; 1.
DR SUPFAM; SSF55083; SSF55083; 1.
DR TIGRFAMs; TIGR00063; folE; 1.
DR TIGRFAMs; TIGR01498; folK; 1.
DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Folate biosynthesis; GTP-binding; Hydrolase; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..349
FT /note="Bifunctional protein FolKE"
FT /id="PRO_0000119471"
FT REGION 1..226
FT /note="2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
FT pyrophosphokinase"
FT REGION 226..349
FT /note="GTP cyclohydrolase 1"
SQ SEQUENCE 349 AA; 40268 MW; 143C36D2E84E2A88 CRC64;
MQTTYLSMGS NIGDRQYYLH EAIRLLGKHP KIMIEKVSNF YESTPVGGVK QDDFTNLALK
VATLLEPLEL LSFIHEVELS LNRERKIHWG PRTIDIDIIF YDDLEMQVEN LVIPHKEAFN
RLFVLKPIFE LIDKDFKYYA SIEKAIAELS VSEQELHVIK EEKTPRNRIE DAVKEILFAV
GENPNREGLL ETPARVAKMY EEILSSQRLS KFNEYKLFEI DSSKTDSIVL IKDIPFYSMC
EHHMLPFFGK AHVAYIPADG KIIGLSKIPR LVDYVSRKLS VQENITHDIG DILTDILNPK
GVAVLVEGRH MCVEMRGVKK VNSITKTSYF LGEFKENNEK RMEFLESLL
