ID   GCH1L_MYCTO             Reviewed;         379 AA.
AC   P9WFM0; L0TAK4; P0A656; Q10514;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=MT2289;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P0AFP6}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE000516; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B70777; B70777.
DR   RefSeq; WP_003411502.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFM0; -.
DR   SMR; P9WFM0; -.
DR   GeneID; 45426208; -.
DR   PATRIC; fig|83331.31.peg.2464; -.
DR   Proteomes; UP000001020; 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.
DR   TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE   3: Inferred from homology;
KW   Metal-binding.
FT   CHAIN           1..379
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000428515"
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   379 AA;  39598 MW;  F4B5E2397426C3F3 CRC64;
     MSVRLADVID VLDQAYPPRL AQSWDSVGLV CGDPDDVVDS VTVAVDATPA VVDQVPQAGL
     LLVHHPLLLR GVDTVAANTP KGVLVHRLIR TGRSLFTAHT NADSASPGVS DALAHAVGLT
     VDAVLDPVPG AADLDKWVIY VPRENSEAVR AAVFEAGAGH IGDYSHCSWS VAGTGQFLAH
     DGASPAIGSV GTVERVAEDR VEVVAPARAR AEVLAAMRAA HPYEEPAFDI FALVPPPVGS
     GLGRIGRLPK PEPLRTFVAR LEAALPPTAT GVRAAGDPDL LVSRVAVCGG AGDSLLATVA
     AADVQAYVTA DLRHHPADEH CRASQVALID VAHWASEFPW CGQAAEVLRS HFGASLPVRV
     CTICTDPWNL DHETGRDQA