ID   GCH1L_BUCAP             Reviewed;         247 AA.
AC   Q8K9N4;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=BUsg_291;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P0AFP6}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
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DR   EMBL; AE013218; AAM67846.1; -; Genomic_DNA.
DR   RefSeq; WP_011053813.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9N4; -.
DR   SMR; Q8K9N4; -.
DR   STRING; 198804.BUsg_291; -.
DR   EnsemblBacteria; AAM67846; AAM67846; BUsg_291.
DR   KEGG; bas:BUsg_291; -.
DR   eggNOG; COG0327; Bacteria.
DR   HOGENOM; CLU_037423_3_0_6; -.
DR   OMA; HGLFWRG; -.
DR   OrthoDB; 502462at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002678; DUF34/NIF3.
DR   InterPro; IPR036069; DUF34/NIF3_sf.
DR   PANTHER; PTHR13799; PTHR13799; 1.
DR   Pfam; PF01784; NIF3; 1.
DR   SUPFAM; SSF102705; SSF102705; 1.
DR   TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE   3: Inferred from homology;
KW   Metal-binding.
FT   CHAIN           1..247
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147298"
FT   BINDING         63
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         64
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         101
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         215
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ   SEQUENCE   247 AA;  28348 MW;  251E4AD36DD3BEE1 CRC64;
     MENFLLEKII NKKLSSDQYS DVVPNGLQIE GEKIIKKIIT GVTACQELLD KALSYGANAI
     IVHHGYFWKN ESQCIHNMTR KRLTTILSNN INLYSWHIPL DIHPKLGNNA QIAKKLNIRI
     KGYILPYLFW GTLEENINAF DFSKKIEKKY EKKPIHIYAN APIYISRIAW CSGRGQNFIK
     QAYNFGIDAF LTGEISEETM HIAKELGIHF FSIGHHATEK DGIKSLGKWL NNKYDLDVTF
     IDIHNPA