GCH1L_ALKHC
ID GCH1L_ALKHC Reviewed; 372 AA.
AC Q9KD39;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=BH1380;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(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; BA000004; BAB05099.1; -; Genomic_DNA.
DR PIR; D83822; D83822.
DR RefSeq; WP_010897545.1; NC_002570.2.
DR AlphaFoldDB; Q9KD39; -.
DR SMR; Q9KD39; -.
DR STRING; 272558.10173996; -.
DR EnsemblBacteria; BAB05099; BAB05099; BAB05099.
DR KEGG; bha:BH1380; -.
DR eggNOG; COG0327; Bacteria.
DR HOGENOM; CLU_037423_1_0_9; -.
DR OMA; EVAYDIY; -.
DR OrthoDB; 502462at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR002678; DUF34/NIF3.
DR InterPro; IPR017221; DUF34/NIF3_bac.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR13799; PTHR13799; 2.
DR Pfam; PF01784; NIF3; 1.
DR PIRSF; PIRSF037489; UCP037489_NIF3_YqfO; 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..372
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147294"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 106
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 332
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 335
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 335
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ SEQUENCE 372 AA; 40813 MW; DD79BF6630DCEE5B CRC64;
MKIANGQTVI QLFERWSPKS LAVEGDKNGV LIGTLNKPIQ RVLTALDVTE SVIDEAIELG
AELILAHHPI IFRPLSSIRT DTAYGRIIEK AIKHDLTIYA AHTNLDITKG GVNDLMADAL
GLKDIEVLAP TTTESLYKLV VFVPHTHTDQ VREALGRAGA GHIGNYSYCT FNSKGTGTFK
PEEGTNPFIG KQGALEFVEE LKIETIVTEG QKNKVVAAMI KSHPYEEPAY DLYPLANEGE
TLGLGRIGYL HESMTLEEFA KQVKKAFDVP TARVVGSLET QIRKVAVLGG DGNKYMAHAL
RKGADVIVTG DVYYHVPHDA LMDGLNIVDP GHNVEKIMKQ GVKEKLEKLL KDKKYDTEVV
ASSVHTDPFT FI