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ID A1AY05_PARDP Unreviewed; 200 AA.
AC A1AY05;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 08-MAY-2019, entry version 96.
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 OrderedLocusNames=Pden_0032 {ECO:0000313|EMBL:ABL68149.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68149.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA van Spanning R.J.M., Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-
CC MPT) cofactor (Moco or molybdenum cofactor) to form Mo-
CC molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
CC {ECO:0000256|HAMAP-Rule:MF_00316, ECO:0000256|SAAS:SAAS01086198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-
CC molybdopterin guanine dinucleotide; Xref=Rhea:RHEA:34243,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:71302, ChEBI:CHEBI:71310; EC=2.7.7.77;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00316,
CC ECO:0000256|SAAS:SAAS01121598};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00316, ECO:0000256|SAAS:SAAS01086208};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316,
CC ECO:0000256|SAAS:SAAS01086219}.
CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition
CC and specific binding, while the C-terminal domain determines the
CC specific binding to the target protein. {ECO:0000256|HAMAP-
CC Rule:MF_00316}.
CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000256|HAMAP-
CC Rule:MF_00316, ECO:0000256|SAAS:SAAS01086209}.
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DR EMBL; CP000489; ABL68149.1; -; Genomic_DNA.
DR RefSeq; WP_011746382.1; NC_008686.1.
DR STRING; 318586.Pden_0032; -.
DR PRIDE; A1AY05; -.
DR EnsemblBacteria; ABL68149; ABL68149; Pden_0032.
DR KEGG; pde:Pden_0032; -.
DR eggNOG; ENOG4105C6R; Bacteria.
DR eggNOG; COG0746; LUCA.
DR HOGENOM; HOG000280423; -.
DR KO; K03752; -.
DR OMA; FVPCDVP; -.
DR BioCyc; PDEN318586:G1GW1-32-MONOMER; -.
DR Proteomes; UP000000361; 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 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;
DR PRODOM; A1AY05.
DR SWISS-2DPAGE; A1AY05.
KW Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316,
KW ECO:0000256|SAAS:SAAS01086201};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00316,
KW ECO:0000256|SAAS:SAAS01086211};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00316,
KW ECO:0000256|SAAS:SAAS01086207};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00316,
KW ECO:0000256|SAAS:SAAS01086210};
KW Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_00316,
KW ECO:0000256|SAAS:SAAS01086212};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00316,
KW ECO:0000256|SAAS:SAAS01086200};
KW Nucleotidyltransferase {ECO:0000313|EMBL:ABL68149.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00316,
KW ECO:0000256|SAAS:SAAS01086206, ECO:0000313|EMBL:ABL68149.1}.
FT DOMAIN 6 164 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
FT NP_BIND 9 11 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}.
FT METAL 101 101 Magnesium. {ECO:0000256|HAMAP-Rule:
FT MF_00316}.
FT BINDING 22 22 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}.
FT BINDING 50 50 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}.
FT BINDING 68 68 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}.
FT BINDING 101 101 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}.
SQ SEQUENCE 200 AA; 20689 MW; 3C47671AD2E28762 CRC64;
MSPVPAVILA GGLSTRMGGG NKALRMLAGE TLLSRVIARL SPQCGPLAIN ANGEPGQFEE
YGLPVIADGI AGFAGPLAGV LAGMEWAAGE GADSVVSVSV DTPFLPEDLV HRLREAAGRS
GVAIAASPDD SGQLRDHPTC ALWPVSLRGE LRDALESGLH RIGQFAAAHD PGRAVFDSRP
VDPFLNLNTP EDLARAARLV
//
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