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GCH1L_CHLMU
ID   GCH1L_CHLMU             Reviewed;         251 AA.
AC   Q9PKS8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=TC_0384;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(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; AE002160; AAF39241.1; -; Genomic_DNA.
DR   PIR; B81709; B81709.
DR   RefSeq; WP_010230301.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKS8; -.
DR   SMR; Q9PKS8; -.
DR   STRING; 243161.TC_0384; -.
DR   EnsemblBacteria; AAF39241; AAF39241; TC_0384.
DR   GeneID; 1245736; -.
DR   KEGG; cmu:TC_0384; -.
DR   eggNOG; COG0327; Bacteria.
DR   HOGENOM; CLU_037423_3_0_0; -.
DR   OMA; HGLFWRG; -.
DR   OrthoDB; 502462at2; -.
DR   Proteomes; UP000000800; 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..251
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147301"
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         102
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"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ   SEQUENCE   251 AA;  27458 MW;  4F7DF6D57B069899 CRC64;
     MNVADLLHVL NELLYPELFN DYGPNGLQVG DAQAPVRKIA VAVTADLATI EKAIACESNV
     LLVHHGLFWK GMPYPITGML YQRMQRLIEN NIQLIAYHLP LDAHPEVGNN WKVAKDLGWE
     RLESFGSTKP SLGVKGVFPE IGIHDFVSQL SSYYQAPVLA KALGGKESIS SAALISGGAY
     KEISEAKSQE VDCFITGNFD EPAWSLAHEL AINFLAFGHT ATEKVGPKAL TQYLKQVGCD
     SVVFLDTENP F
 
 
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