ID C7LBQ6_BRUMC Unreviewed; 221 AA.
AC C7LBQ6;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Molybdenum cofactor guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE Short=MoCo guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE EC=2.7.7.77 {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=Mo-MPT guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=Molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316};
DE AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000256|HAMAP-Rule:MF_00316};
DE Short=MGD synthase {ECO:0000256|HAMAP-Rule:MF_00316};
GN Name=mobA {ECO:0000256|HAMAP-Rule:MF_00316,
GN ECO:0000313|EMBL:ACU47941.1};
GN OrderedLocusNames=BMI_I955 {ECO:0000313|EMBL:ACU47941.1};
OS Brucella microti (strain CCM 4915).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU47941.1, ECO:0000313|Proteomes:UP000002188};
RN [1] {ECO:0000313|EMBL:ACU47941.1, ECO:0000313|Proteomes:UP000002188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU47941.1,
RC ECO:0000313|Proteomes:UP000002188};
RX PubMed=19653890; DOI=10.1186/1471-2164-10-352;
RA Audic S., Lescot M., Claverie J.-M., Scholz H.C.;
RT "Brucella microti: the genome sequence of an emerging pathogen.";
RL BMC Genomics 10:352-352(2009).
CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT)
CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine
CC dinucleotide (Mo-MGD) cofactor. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin
CC guanine dinucleotide; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302,
CC ChEBI:CHEBI:71310; EC=2.7.7.77; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00316};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00316};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition and
CC specific binding, while the C-terminal domain determines the specific
CC binding to the target protein. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000256|HAMAP-
CC Rule:MF_00316}.
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DR EMBL; CP001578; ACU47941.1; -; Genomic_DNA.
DR RefSeq; WP_002964077.1; NC_013119.1.
DR AlphaFoldDB; C7LBQ6; -.
DR SMR; C7LBQ6; -.
DR GeneID; 55590655; -.
DR KEGG; bmr:BMI_I955; -.
DR HOGENOM; CLU_055597_5_0_5; -.
DR Proteomes; UP000002188; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02503; MobA; 1.
DR HAMAP; MF_00316; MobA; 1.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR013482; Molybde_CF_guanTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR PANTHER; PTHR19136:SF81; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00316}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00316};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00316};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_00316};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00316}; Transferase {ECO:0000256|HAMAP-Rule:MF_00316}.
FT DOMAIN 15..170
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT BINDING 18..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ SEQUENCE 221 AA; 23735 MW; BC68362E9B96D1BA CRC64;
MRAGQPKITG AKITGAIIAG GQSSRMQAGG VSGDKFLQPL GSAPVIAHVI ARLQPQVDTL
FINSKGDLSR FAAFGLPAVK DIAMNHGGPL VGLLTCLAHA SPCRLLLTSA ADTPFLPCDL
ASNLIRKQAE TGARIILACS NERVHPIVGL WHTDLVPDLE KWLQHAEKAS IFWFAKHIGF
EVVNIPLAHA PRLAESYDPF FNINLPDDLL KAREINEALQ A
//
