ID   MOBA_STAA8              Reviewed;         199 AA.
AC   Q2FVY4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable molybdenum cofactor guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE            Short=MoCo guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE            EC=2.7.7.77 {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=Mo-MPT guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=Molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE   AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_00316};
DE            Short=MGD synthase {ECO:0000255|HAMAP-Rule:MF_00316};
GN   Name=mobA {ECO:0000255|HAMAP-Rule:MF_00316};
GN   OrderedLocusNames=SAOUHSC_02537;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00316};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00316};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00316}.
CC   -!- SIMILARITY: Belongs to the MobA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00316}.
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DR   EMBL; CP000253; ABD31552.1; -; Genomic_DNA.
DR   RefSeq; WP_000643988.1; NZ_LS483365.1.
DR   RefSeq; YP_501001.1; NC_007795.1.
DR   AlphaFoldDB; Q2FVY4; -.
DR   SMR; Q2FVY4; -.
DR   STRING; 1280.SAXN108_2518; -.
DR   EnsemblBacteria; ABD31552; ABD31552; SAOUHSC_02537.
DR   GeneID; 3921127; -.
DR   KEGG; sao:SAOUHSC_02537; -.
DR   PATRIC; fig|93061.5.peg.2288; -.
DR   eggNOG; COG0746; Bacteria.
DR   HOGENOM; CLU_055597_2_0_9; -.
DR   OMA; FVIACDI; -.
DR   PRO; PR:Q2FVY4; -.
DR   Proteomes; UP000008816; Chromosome.
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:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02503; MobA; 1.
DR   Gene3D; 3.90.550.10; -; 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   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..199
FT                   /note="Probable molybdenum cofactor guanylyltransferase"
FT                   /id="PRO_1000019157"
FT   BINDING         6..8
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         65
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
SQ   SEQUENCE   199 AA;  22542 MW;  049B67072F209982 CRC64;
     MKAIILAGGH SVRFGKPKAF AEVNGETFYS RVIKTLESTN MFNEIIISTN AQLATQFKYP
     NVVIDDENHN DKGPLAGIYT IMKQHPEEEL FFVVSVDTPM ITGKAVSTLY QFLVSHLIEN
     HLDVAAFKED GRFIPTIAFY SPNALGAITK ALHSDNYSFK NVYHELSTDY LDVRDVDAPS
     YWYKNINYQH DLDALIQKL