GCH1L_PYRAB
ID GCH1L_PYRAB Reviewed; 250 AA.
AC Q9UYT3; G8ZHN2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=PYRAB14240; ORFNames=PAB1433;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248287; CAB50329.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70869.1; -; Genomic_DNA.
DR PIR; D75054; D75054.
DR RefSeq; WP_010868539.1; NC_000868.1.
DR AlphaFoldDB; Q9UYT3; -.
DR SMR; Q9UYT3; -.
DR STRING; 272844.PAB1433; -.
DR EnsemblBacteria; CAB50329; CAB50329; PAB1433.
DR GeneID; 1496815; -.
DR KEGG; pab:PAB1433; -.
DR PATRIC; fig|272844.11.peg.1514; -.
DR eggNOG; arCOG04454; Archaea.
DR HOGENOM; CLU_037423_3_0_2; -.
DR OMA; HGLFWRG; -.
DR OrthoDB; 40682at2157; -.
DR PhylomeDB; Q9UYT3; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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_0000147350"
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; 27569 MW; 93E487C86832FE38 CRC64;
MEREEIVSFL DEYLSISSYP DKSSNGLQVE GKEEVERIAF AVDACLDTIA KARAFNADML
IVHHGIIWGG VSYVKGLFAK RLKALLSSEM NLYVAHIPLD VHPEVGNNVQ LLKLLNLEPL
EPFGEYKGIK IGYIGEFEEP KPLPMIAQIL AEKLPVDYVR SYEFGLQEIK RVAVVSGAGG
FAIEEASEKA DLLITGEISH ADYRTAEDLR VSVIAAGHYA TETLGVKALM KLVREKFGVK
TIFIDSPTGL
