ID   GCH1L_MYCLE             Reviewed;         385 AA.
AC   O69481;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=ML1639; ORFNames=MLCB1243.36;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL023635; CAA19217.1; -; Genomic_DNA.
DR   EMBL; AL583922; CAC30590.1; -; Genomic_DNA.
DR   PIR; T44719; T44719.
DR   RefSeq; NP_302129.1; NC_002677.1.
DR   RefSeq; WP_010908450.1; NC_002677.1.
DR   AlphaFoldDB; O69481; -.
DR   SMR; O69481; -.
DR   STRING; 272631.ML1639; -.
DR   EnsemblBacteria; CAC30590; CAC30590; CAC30590.
DR   KEGG; mle:ML1639; -.
DR   PATRIC; fig|272631.5.peg.3093; -.
DR   Leproma; ML1639; -.
DR   eggNOG; COG0327; Bacteria.
DR   eggNOG; COG3323; Bacteria.
DR   HOGENOM; CLU_037423_1_1_11; -.
DR   OMA; EVAYDIY; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.120; -; 1.
DR   InterPro; IPR002678; DUF34/NIF3.
DR   InterPro; IPR017221; DUF34/NIF3_bac.
DR   InterPro; IPR036069; DUF34/NIF3_sf.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   PANTHER; PTHR13799; PTHR13799; 1.
DR   Pfam; PF01784; NIF3; 1.
DR   PIRSF; PIRSF037489; UCP037489_NIF3_YqfO; 1.
DR   SUPFAM; SSF102705; SSF102705; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..385
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147317"
FT   BINDING         64
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         65
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         103
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         333
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         337
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         337
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ   SEQUENCE   385 AA;  40291 MW;  8D1B344F8BBF050E CRC64;
     MSARLADVIE VLDHAYPPRF AQSWDSVGLV CGDPEDVLEA ITIAVDATPA VIDEVPDSGL
     LLVHHPLLLH GVDTVAVSTP KGALVHRLIR SGRSLFTAHT NADSASPGVS DALAHVFGLT
     VDAVLEPLLG VASLDKWVIY VPLEHVAAVQ AAVFEAGAGH IGDYSHCSWS VTGTGQFMPH
     DGASPVVGSI GAIERVAEDR VEVVAPARAR AAVLSAMHAA HPYEEPAFDI FALVPPPGDV
     GLGRIGTLPR PESLSAFVAR VGAALPQTSS GVRATGDPDM LVSRVAVCGG AGDSLLSLAA
     VADVQAYVTA DLRHHPADEH RRASNVALID VAHWASEFPW CGQAADVLRS HFGTALSVRV
     CTIRTDPWNL GARRVNDVSD SGRDQ