ID   GCH1L_BUCAI             Reviewed;         247 AA.
AC   P57387;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=BU301;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13010.1; -; Genomic_DNA.
DR   RefSeq; NP_240124.1; NC_002528.1.
DR   RefSeq; WP_009874254.1; NC_002528.1.
DR   AlphaFoldDB; P57387; -.
DR   SMR; P57387; -.
DR   STRING; 107806.10038975; -.
DR   EnsemblBacteria; BAB13010; BAB13010; BAB13010.
DR   KEGG; buc:BU301; -.
DR   PATRIC; fig|107806.10.peg.312; -.
DR   eggNOG; COG0327; Bacteria.
DR   HOGENOM; CLU_037423_3_0_6; -.
DR   OMA; HGLFWRG; -.
DR   BioCyc; BAPH107806:GBZJ-295-MON; -.
DR   Proteomes; UP000001806; 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; Reference proteome.
FT   CHAIN           1..247
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147297"
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;  28327 MW;  7E8CAA8D475D9F63 CRC64;
     MNNFLLEDII NKKLLSNQYQ DTVPNGLQIE GTEIVKKIIT GVTACQALLD KALFYNADTL
     IVHHGYFWKN ESKYIHNMQR QRLKTILSHN INLYSWHLPL DVHPKLGNNA QIAKKLNIDI
     QGSILPYVLW GTTKNKMTGF EFANKIERKF KKYPIHLYEN APLYISRVAW CSGRGQGFIK
     KACAFGIDAF LTGEISEETT HIAKELGIHF FSLGHHATEK DGVKSLGEWL QRKYDLCVDF
     IDIYNPA