GCH1L_PYRHO
ID GCH1L_PYRHO Reviewed; 250 AA.
AC O58361;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=PH0627;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q58337}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA29716.1; -; Genomic_DNA.
DR PIR; B71107; B71107.
DR RefSeq; WP_010884725.1; NC_000961.1.
DR AlphaFoldDB; O58361; -.
DR SMR; O58361; -.
DR STRING; 70601.3257033; -.
DR EnsemblBacteria; BAA29716; BAA29716; BAA29716.
DR GeneID; 1442959; -.
DR KEGG; pho:PH0627; -.
DR eggNOG; arCOG04454; Archaea.
DR OMA; HGLFWRG; -.
DR OrthoDB; 40682at2157; -.
DR Proteomes; UP000000752; 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..250
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147351"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 64
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 100
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 218
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 222
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 222
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ SEQUENCE 250 AA; 27384 MW; 821C0E0516CF5D31 CRC64;
MDRDEIVSFL DEFLNISAYP DKSKNGLQVE GKEEVNTIAF AVDASLDTIL KAKVFNADML
IVHHGIIWGG ISYVRGLIAK RLKELLVAGI NLYAVHLPLD AHPEVGNNVQ LLKLLNLEAK
EPFGEYHGVK IGYIGEFDEP KPLPLIAQIL AEKLPAEYVK SYEFGLQEVK RIAVVSGGGG
FAIEEASRKA DLLITGEITH EDYRVAEDLR VSVIAAGHYA TETLGVKALM GVLKEKFGVK
TVFIDNPTGL
