ID Q1GBX8_LACDA Unreviewed; 357 AA.
AC Q1GBX8;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=GTP cyclohydrolase 1 {ECO:0000256|HAMAP-Rule:MF_00223};
DE EC=3.5.4.16 {ECO:0000256|HAMAP-Rule:MF_00223};
DE AltName: Full=GTP cyclohydrolase I {ECO:0000256|HAMAP-Rule:MF_00223};
DE Short=GTP-CH-I {ECO:0000256|HAMAP-Rule:MF_00223};
GN Name=folKE {ECO:0000313|EMBL:CAI97087.1};
GN Synonyms=folE {ECO:0000256|HAMAP-Rule:MF_00223};
GN OrderedLocusNames=Ldb0247 {ECO:0000313|EMBL:CAI97087.1};
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI97087.1, ECO:0000313|Proteomes:UP000001259};
RN [1] {ECO:0000313|EMBL:CAI97087.1, ECO:0000313|Proteomes:UP000001259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC {ECO:0000313|Proteomes:UP000001259};
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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 Evidence={ECO:0000256|ARBA:ARBA00001052, ECO:0000256|HAMAP-
CC Rule:MF_00223};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005080, ECO:0000256|HAMAP-Rule:MF_00223}.
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 -!- SUBUNIT: Homopolymer. {ECO:0000256|HAMAP-Rule:MF_00223}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC {ECO:0000256|HAMAP-Rule:MF_00223}.
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DR EMBL; CR954253; CAI97087.1; -; Genomic_DNA.
DR RefSeq; WP_011543576.1; NZ_JQAV01000030.1.
DR AlphaFoldDB; Q1GBX8; -.
DR STRING; 390333.Ldb0247; -.
DR KEGG; ldb:Ldb0247; -.
DR PATRIC; fig|390333.13.peg.1328; -.
DR eggNOG; COG0302; Bacteria.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_775655_0_0_9; -.
DR BioCyc; LDEL390333:LDB_RS01025-MONOMER; -.
DR UniPathway; UPA00077; UER00155.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000001259; 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; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 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; IPR020602; GTP_CycHdrlase_I_dom.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR NCBIfam; TIGR00063; folE; 1.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR11109:SF7; GTP CYCLOHYDROLASE 1; 1.
DR PANTHER; PTHR11109; GTP CYCLOHYDROLASE I; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 1.
DR Pfam; PF01288; HPPK; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00223};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAI97087.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00223};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_00223}; Reference proteome {ECO:0000313|Proteomes:UP000001259};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAI97087.1};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00223}.
FT DOMAIN 89..100
FT /note="7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase"
FT /evidence="ECO:0000259|PROSITE:PS00794"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00223"
SQ SEQUENCE 357 AA; 40324 MW; C6BBA0DCF823F7D9 CRC64;
MMENVILSLG SNIGNREAYI NKAVALLGND PAILIDKASS FYETSPVGNV NQRAFINIAL
KIATTDSPED LLTKIHQIEL HLHRTRDVHW GPRTLDVDII FWGDQKIKTE SLIIPHPEAF
NRLFVLVPTL GIVTPEFPFY NQIKAQIQKL QKADQTIQLV QKQTQSKQVV ESAIRQILNA
IGDDPDRPGL VETPDRVARM YNEIFSSEGL DNFEDYKLFN TKETDNSKMV MVKNITFYSM
CEHHMMPFWG KAHIAYVPDH GKIIGLSKIP RLVDFVSHKL GLQEKLTDDI VAQMNRILAP
KGVAVIVDSR HMCVEMRGVK KADSLTRTIR FSGVFETDQA LRMAFLNSIG DVNGKTI
//
