ID   GCH1L_TREPA             Reviewed;         286 AA.
AC   O83942;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=TP_0977;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65932.1; -; Genomic_DNA.
DR   PIR; G71257; G71257.
DR   RefSeq; WP_010882421.1; NC_021490.2.
DR   AlphaFoldDB; O83942; -.
DR   SMR; O83942; -.
DR   STRING; 243276.TPANIC_0977; -.
DR   EnsemblBacteria; AAC65932; AAC65932; TP_0977.
DR   GeneID; 57879486; -.
DR   KEGG; tpa:TP_0977; -.
DR   eggNOG; COG0327; Bacteria.
DR   HOGENOM; CLU_037423_3_0_12; -.
DR   OMA; HGLFWRG; -.
DR   OrthoDB; 502462at2; -.
DR   Proteomes; UP000000811; 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..286
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147341"
FT   BINDING         66
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         67
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         254
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         258
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         258
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ   SEQUENCE   286 AA;  30882 MW;  94FBB294BBBC48F6 CRC64;
     MTARELDAYF RSFLNFGPFV SCDVALNGLQ VANSGAPVHK VAFAVDACAQ SIDAAARAGA
     RMLFVHHGLF WGRIEPLTGM QYRRVQALLT HDIALYAVHL PLDAHPQYGN NAGLAARVGL
     RQGGPFGFIR GTAVGLWGTV AENTTPSQEA MQQHAACTAP DTHRVTHANA ISPSAGLSLQ
     QVVHRLFPAE EQPVRLLPFG KQRIERVGIL SGKAGTYLAE AIALDLDLFI TGEIEHSCYH
     TAREHSISVI AGGHYQTETV GLQLVARKLQ RDTGIETLFL DIPTGM