FOLKE_LACLM
ID FOLKE_LACLM Reviewed; 349 AA.
AC Q8GJP4; A2RKW2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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; Synonyms=folE; OrderedLocusNames=llmg_1337;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12788700; DOI=10.1128/aem.69.6.3069-3076.2003;
RA Sybesma W., Starrenburg M., Kleerebezem M., Mierau I., de Vos W.M.,
RA Hugenholtz J.;
RT "Increased production of folate by metabolic engineering of Lactococcus
RT lactis.";
RL Appl. Environ. Microbiol. 69:3069-3076(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AY156932; AAN64306.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL97928.1; -; Genomic_DNA.
DR RefSeq; WP_011835210.1; NZ_WJVF01000034.1.
DR AlphaFoldDB; Q8GJP4; -.
DR SMR; Q8GJP4; -.
DR STRING; 416870.llmg_1337; -.
DR EnsemblBacteria; CAL97928; CAL97928; llmg_1337.
DR KEGG; llm:llmg_1337; -.
DR eggNOG; COG0302; Bacteria.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_775655_0_0_9; -.
DR OMA; HPEAFNR; -.
DR PhylomeDB; Q8GJP4; -.
DR BioCyc; LLAC416870:LLMG_RS06775-MON; -.
DR UniPathway; UPA00077; UER00155.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000364; 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 Transferase.
FT CHAIN 1..349
FT /note="Bifunctional protein FolKE"
FT /id="PRO_0000119472"
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; 40261 MW; 105B058C80E3A8B4 CRC64;
MQTTYLSMGS NIGDRQYYLH EAIRLLGKHP KIMIEKVSNF YESSPVGGVK QDDFTNLALK
VATLLEPLEL LDFIHEVELS LNRERKIHWG PRTIDIDIIF YGNSEIQEEN LIVPHKEAFN
RLFVLKPIFE LLSNDFKYYE PIREAIAKLS ESEQELHVIE EEKSPKNRIE EAVKEILFAV
GENPNREGLL ETPARVAKMY EEILSSQRLT NFNEYKLFEI DSSKNDSIVL IKDIPFYSMC
EHHMLPFFGK AHVAYIPDGG RIIGLSKIPR LVNYVSRKLS VQENITHDIA DILTDILKPK
GVAVLVEGRH MCVEMRGVKK VNSLTKTSYF LGEFKENGEK RMEFLESLL
