GCH1L_MYCBO
ID GCH1L_MYCBO Reviewed; 379 AA.
AC P0A657; A0A1R3Y0K4; Q10514; X2BK75;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=BQ2027_MB2255C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00863.1; -; Genomic_DNA.
DR RefSeq; NP_855904.1; NC_002945.3.
DR RefSeq; WP_003411502.1; NC_002945.4.
DR AlphaFoldDB; P0A657; -.
DR SMR; P0A657; -.
DR EnsemblBacteria; SIU00863; SIU00863; BQ2027_MB2255C.
DR GeneID; 45426208; -.
DR PATRIC; fig|233413.5.peg.2472; -.
DR OMA; EVAYDIY; -.
DR Proteomes; UP000001419; 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; 1.
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.
FT CHAIN 1..379
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147319"
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 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 333
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 337
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 337
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ SEQUENCE 379 AA; 39598 MW; F4B5E2397426C3F3 CRC64;
MSVRLADVID VLDQAYPPRL AQSWDSVGLV CGDPDDVVDS VTVAVDATPA VVDQVPQAGL
LLVHHPLLLR GVDTVAANTP KGVLVHRLIR TGRSLFTAHT NADSASPGVS DALAHAVGLT
VDAVLDPVPG AADLDKWVIY VPRENSEAVR AAVFEAGAGH IGDYSHCSWS VAGTGQFLAH
DGASPAIGSV GTVERVAEDR VEVVAPARAR AEVLAAMRAA HPYEEPAFDI FALVPPPVGS
GLGRIGRLPK PEPLRTFVAR LEAALPPTAT GVRAAGDPDL LVSRVAVCGG AGDSLLATVA
AADVQAYVTA DLRHHPADEH CRASQVALID VAHWASEFPW CGQAAEVLRS HFGASLPVRV
CTICTDPWNL DHETGRDQA