GCH4_BACSU
ID GCH4_BACSU Reviewed; 304 AA.
AC P94398; Q797Q1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=GTP cyclohydrolase FolE2;
DE EC=3.5.4.16;
DE AltName: Full=GTP cyclohydrolase 1B;
GN Name=folE2; Synonyms=yciA; OrderedLocusNames=BSU03340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
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 SEQUENCE REVISION TO 202-209; 222 AND 290-295.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=12426338; DOI=10.1128/jb.184.23.6508-6514.2002;
RA Gaballa A., Wang T., Ye R.W., Helmann J.D.;
RT "Functional analysis of the Bacillus subtilis Zur regulon.";
RL J. Bacteriol. 184:6508-6514(2002).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17032654; DOI=10.1074/jbc.m607114200;
RA El Yacoubi B., Bonnett S., Anderson J.N., Swairjo M.A., Iwata-Reuyl D.,
RA de Crecy-Lagard V.;
RT "Discovery of a new prokaryotic type I GTP cyclohydrolase family.";
RL J. Biol. Chem. 281:37586-37593(2006).
CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC {ECO:0000269|PubMed:17032654}.
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:0000269|PubMed:17032654};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- INDUCTION: Repressed by zinc, via zur. {ECO:0000269|PubMed:12426338}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a zinc uptake system.
CC {ECO:0000305|PubMed:12426338}.
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DR EMBL; D50453; BAA08968.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12128.2; -; Genomic_DNA.
DR PIR; H69759; H69759.
DR RefSeq; NP_388216.2; NC_000964.3.
DR RefSeq; WP_003246378.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P94398; -.
DR SMR; P94398; -.
DR IntAct; P94398; 1.
DR MINT; P94398; -.
DR STRING; 224308.BSU03340; -.
DR TCDB; 9.B.10.1.1; the putative tripartite zn(2+) transporter (tzt) family.
DR PRIDE; P94398; -.
DR EnsemblBacteria; CAB12128; CAB12128; BSU_03340.
DR GeneID; 938325; -.
DR KEGG; bsu:BSU03340; -.
DR PATRIC; fig|224308.179.peg.348; -.
DR eggNOG; COG1469; Bacteria.
DR InParanoid; P94398; -.
DR OMA; PCSQGMS; -.
DR PhylomeDB; P94398; -.
DR BioCyc; BSUB:BSU03340-MON; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003933; F:GTP cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR PANTHER; PTHR36445; PTHR36445; 1.
DR Pfam; PF02649; GCHY-1; 1.
DR TIGRFAMs; TIGR00294; TIGR00294; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..304
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000147701"
FT SITE 183
FT /note="May be catalytically important"
FT /evidence="ECO:0000250"
FT CONFLICT 202..209
FT /note="SIWADIHP -> KHLGRIFTR (in Ref. 1; BAA08968)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="L -> P (in Ref. 1; BAA08968)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..295
FT /note="DAYAKL -> RCLCEV (in Ref. 1; BAA08968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 34564 MW; 90A28F90FE9BDAB3 CRC64;
MNQHTLLPKK TERLQYFGSV SPIKGEKPVE KEKMKDLQNI RKDYFFDIQH VGVANVSHPV
TITSAMMPAE QTTAANFTMT CNLPRNQKGI NMSRLTELLQ VYHQNGWILS FSSLQQFTKE
LAENMDTSSA TVEVRFPWFF ERKSPKLEKA GLMHADIFMS VTYRKDQPFK QRAGISAKVT
TLCPCSKEIS EYSAHNQRGT VSIWADIHPA ASLPSDVKAD LLHAAESNAS ARLHPVLKRP
DEKAVTETAY ENPRFVEDLA RLIAADLFEL EWVSAFEIEC RNEESIHLHD AYAKLCFSKE
VDKI