(data stored in ACNUC7421 zone)

SWISSPROT: A1AY05_PARDP

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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