MOBA_YERPB
ID MOBA_YERPB Reviewed; 195 AA.
AC B2JYK0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=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}; OrderedLocusNames=YPTS_0015;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001048; ACC87014.1; -; Genomic_DNA.
DR RefSeq; WP_002213171.1; NZ_CP009780.1.
DR AlphaFoldDB; B2JYK0; -.
DR SMR; B2JYK0; -.
DR GeneID; 66843590; -.
DR KEGG; ypb:YPTS_0015; -.
DR PATRIC; fig|502801.10.peg.3690; -.
DR OMA; IDFWYAK; -.
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 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.
DR TIGRFAMs; TIGR02665; molyb_mobA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Transferase.
FT CHAIN 1..195
FT /note="Molybdenum cofactor guanylyltransferase"
FT /id="PRO_1000115811"
FT BINDING 10..12
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
SQ SEQUENCE 195 AA; 21445 MW; 9F85C6684B2FC127 CRC64;
MQPNITGVIL AGGRSSRMGG NDKGLIPLNG KPLFQYVIDR FKPQVSDLVI NANRNQGLYK
ESGIPVIDDI ITGFVGPLAG MHAGLSYAST EWVVFAPCDV PALPSDLVSQ LWQGKKQALA
AYANDDERAH PTFALMHISL KTQLADYLIR GDRKLMLFLD SINAQRVKFS GKADLFSNLN
TPADCDLWEQ KRRGQ
