(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 108.
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}.
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   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; BSU03340.
DR   GeneID; 938325; -.
DR   KEGG; bsu:BSU03340; -.
DR   PATRIC; fig|224308.179.peg.348; -.
DR   HOGENOM; HOG000280679; -.
DR   InParanoid; P94398; -.
DR   KO; K09007; -.
DR   OMA; PCSQGMS; -.
DR   PhylomeDB; P94398; -.
DR   BioCyc; BSUB:BSU03340-MONOMER; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001570; Chromosome.
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;
DR   PRODOM; P94398.
DR   SWISS-2DPAGE; P94398.
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
//

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