GCH1_BACSU
ID GCH1_BACSU Reviewed; 190 AA.
AC P19465;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=folE; Synonyms=mtrA; OrderedLocusNames=BSU22780;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2123343; DOI=10.1073/pnas.87.22.8726;
RA Gollnick P., Ishino S., Kuroda M.I., Henner D.J., Yanofsky C.;
RT "The mtr locus is a two-gene operon required for transcription attenuation
RT in the trp operon of Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8726-8730(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=168 / JH642;
RX PubMed=1902464; DOI=10.1128/jb.173.10.3191-3198.1991;
RA Micka B., Groch N., Heinemann U., Marahiel M.A.;
RT "Molecular cloning, nucleotide sequence, and characterization of the
RT Bacillus subtilis gene encoding the DNA-binding protein HBsu.";
RL J. Bacteriol. 173:3191-3198(1991).
RN [4]
RP FUNCTION.
RX PubMed=1551827; DOI=10.1128/jb.174.7.2059-2064.1992;
RA Babitzke P., Gollnick P., Yanofsky C.;
RT "The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA),
RT an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of
RT tryptophan biosynthesis.";
RL J. Bacteriol. 174:2059-2064(1992).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7887891;
RA de Saizieu A., Vankan P., van Loon A.P.;
RT "Enzymic characterization of Bacillus subtilis GTP cyclohydrolase I.
RT Evidence for a chemical dephosphorylation of dihydroneopterin
RT triphosphate.";
RL Biochem. J. 306:371-377(1995).
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 -!- ACTIVITY REGULATION: K(+) ions moderately increases the Vmax, whereas
CC UTP and Ca(2+) and Mg(2+) ions drastically increase the Km for GTP.
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC dimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; M37320; AAA22615.1; -; Genomic_DNA.
DR EMBL; M80245; AAA20852.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14194.1; -; Genomic_DNA.
DR EMBL; X52418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A38256; A38256.
DR RefSeq; NP_390159.1; NC_000964.3.
DR RefSeq; WP_003225516.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P19465; -.
DR SMR; P19465; -.
DR STRING; 224308.BSU22780; -.
DR PaxDb; P19465; -.
DR PRIDE; P19465; -.
DR EnsemblBacteria; CAB14194; CAB14194; BSU_22780.
DR GeneID; 64304058; -.
DR GeneID; 938994; -.
DR KEGG; bsu:BSU22780; -.
DR eggNOG; COG0302; Bacteria.
DR InParanoid; P19465; -.
DR OMA; CEHMCMS; -.
DR PhylomeDB; P19465; -.
DR BioCyc; BSUB:BSU22780-MON; -.
DR BioCyc; MetaCyc:BSU22780-MON; -.
DR UniPathway; UPA00848; UER00151.
DR PRO; PR:P19465; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.286.10; -; 1.
DR Gene3D; 3.30.1130.10; -; 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 PANTHER; PTHR11109; PTHR11109; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 1.
DR TIGRFAMs; TIGR00063; folE; 1.
DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome; Zinc.
FT CHAIN 1..190
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119386"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 190 AA; 21219 MW; E912535CC67A5551 CRC64;
MKEVNKEQIE QAVRQILEAI GEDPNREGLL DTPKRVAKMY AEVFSGLNED PKEHFQTIFG
ENHEELVLVK DIAFHSMCEH HLVPFYGKAH VAYIPRGGKV TGLSKLARAV EAVAKRPQLQ
ERITSTIAES IVETLDPHGV MVVVEAEHMC MTMRGVRKPG AKTVTSAVRG VFKDDAAARA
EVLEHIKRQD
