(data stored in ACNUC7421 zone)

SWISSPROT: B8I9P1_METNO

ID   B8I9P1_METNO            Unreviewed;       370 AA.
AC   B8I9P1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 66.
DE   RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_00179};
DE            EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_00179};
DE   AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_00179};
GN   Name=ribA {ECO:0000256|HAMAP-Rule:MF_00179};
GN   OrderedLocusNames=Mnod_0250 {ECO:0000313|EMBL:ACL55294.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55294.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55294.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC       ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC       pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00179}.
CC   -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
CC       hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00179, ECO:0000256|SAAS:SAAS00711743}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00179};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00179};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00179}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC       {ECO:0000256|HAMAP-Rule:MF_00179}.
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DR   EMBL; CP001349; ACL55294.1; -; Genomic_DNA.
DR   RefSeq; WP_015927007.1; NC_011894.1.
DR   ProteinModelPortal; B8I9P1; -.
DR   STRING; 460265.Mnod_0250; -.
DR   EnsemblBacteria; ACL55294; ACL55294; Mnod_0250.
DR   KEGG; mno:Mnod_0250; -.
DR   eggNOG; ENOG4107QJN; Bacteria.
DR   eggNOG; COG0807; LUCA.
DR   HOGENOM; HOG000115442; -.
DR   KO; K01497; -.
DR   OMA; HSACFTG; -.
DR   OrthoDB; POG091H0120; -.
DR   UniPathway; UPA00275; UER00400.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   HAMAP; MF_00179; RibA; 1.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; SSF142695; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8I9P1.
DR   SWISS-2DPAGE; B8I9P1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00179,
KW   ECO:0000256|SAAS:SAAS00711691};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00179,
KW   ECO:0000256|SAAS:SAAS00711696, ECO:0000313|EMBL:ACL55294.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00179,
KW   ECO:0000256|SAAS:SAAS00711702};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00179,
KW   ECO:0000256|SAAS:SAAS00711707};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00179,
KW   ECO:0000256|SAAS:SAAS00711711};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00179}.
FT   DOMAIN      171    330       GTP_cyclohydro2. {ECO:0000259|Pfam:
FT                                PF00925}.
FT   NP_BIND     212    216       GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
FT   NP_BIND     255    257       GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
FT   ACT_SITE    289    289       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00179}.
FT   ACT_SITE    291    291       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00179}.
FT   METAL       217    217       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00179}.
FT   METAL       228    228       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00179}.
FT   METAL       230    230       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00179}.
FT   BINDING     233    233       GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
FT   BINDING     277    277       GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
FT   BINDING     312    312       GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
FT   BINDING     317    317       GTP. {ECO:0000256|HAMAP-Rule:MF_00179}.
SQ   SEQUENCE   370 AA;  38888 MW;  B5C3305DA30C69CF CRC64;
     MSLTVTNVDE RLRREQVQVE RAIAEMRAGR AVAILGEEPA LAVSAESVDA RLAADWERLG
     TAVRLVLPAP RLRRIGLANR FEAGAVALPV VDPARITALA LKVDGRIDAP VACARRVDAV
     ALELARLAQV IPAMVVAPVS GVPEDALTVD PAAVELFRTR QAAALRIVSR APVPLDGAPE
     TEFVVFRGGE GLRDQVAVVV GRPNLAEPVA VRVHSACLTG DLFGSLKCDC GDQLRGTARW
     MAGNGGGIIL YLDQEGRGNG LANKIRAYDL QAKGFDTYAA DAALGFGLDQ RRFDFAAAML
     RCLGVGAVRV LSNNPEKIAA LAEAGLTVVG AQRAPGRVTP ENARYLAAKR DIAGHVLELG
     GFSCAEVSGG
//

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