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