(data stored in ACNUC7421 zone)

SWISSPROT: MOBA_SHESH

ID   MOBA_SHESH              Reviewed;         196 AA.
AC   A8FPG1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 60.
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};
GN   OrderedLocusNames=Ssed_0121;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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:0000255|HAMAP-Rule:MF_00316}.
CC   -!- CATALYTIC ACTIVITY: GTP + molybdenum cofactor = diphosphate +
CC       guanylyl molybdenum cofactor. {ECO:0000255|HAMAP-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
CC       and specific binding, while the C-terminal domain determines the
CC       specific binding to the target protein. {ECO:0000255|HAMAP-
CC       Rule:MF_00316}.
CC   -!- SIMILARITY: Belongs to the MobA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00316}.
DR   EMBL; CP000821; ABV34734.1; -; Genomic_DNA.
DR   RefSeq; WP_012004260.1; NC_009831.1.
DR   ProteinModelPortal; A8FPG1; -.
DR   SMR; A8FPG1; -.
DR   STRING; 425104.Ssed_0121; -.
DR   EnsemblBacteria; ABV34734; ABV34734; Ssed_0121.
DR   KEGG; sse:Ssed_0121; -.
DR   eggNOG; ENOG4105C6R; Bacteria.
DR   eggNOG; COG0746; LUCA.
DR   HOGENOM; HOG000280423; -.
DR   KO; K03752; -.
DR   OMA; FVPCDVP; -.
DR   OrthoDB; POG091H05CW; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   PANTHER; PTHR19136:SF85; PTHR19136:SF85; 1.
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; A8FPG1.
DR   SWISS-2DPAGE; A8FPG1.
KW   Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN         1    196       Molybdenum cofactor guanylyltransferase.
FT                                /FTId=PRO_1000079115.
FT   NP_BIND      10     12       GTP. {ECO:0000255|HAMAP-Rule:MF_00316}.
FT   METAL        99     99       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00316}.
FT   BINDING      23     23       GTP. {ECO:0000255|HAMAP-Rule:MF_00316}.
FT   BINDING      51     51       GTP. {ECO:0000255|HAMAP-Rule:MF_00316}.
FT   BINDING      69     69       GTP. {ECO:0000255|HAMAP-Rule:MF_00316}.
FT   BINDING      99     99       GTP. {ECO:0000255|HAMAP-Rule:MF_00316}.
SQ   SEQUENCE   196 AA;  21701 MW;  A9842CB6DBF16F14 CRC64;
     MSLQIDAVIL AGGMARRMGG NDKGLVELQA QPMIKHAIDR IKPQVREILI NANRNQTRYA
     EFGYQVISDE DSGYLGPLAG MITAMGQTQA KYLLVVPCDC PLLPADLVER MLSQLEKENA
     DLAVASDGKR EQPVVLLLKP ELRDSMKAFL DAGERKIDFW YAKHNCAVAD FSDQPNAFVN
     VNTPEQKQQL SEAIAK
//

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