MOBA_SYNE7
ID MOBA_SYNE7 Reviewed; 194 AA.
AC O06866; Q31P00; Q79PE7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Synpcc7942_1189; ORFNames=se00039;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rubio L.M., Flores E., Herrero A.;
RT "The narC locus of Synechococcus sp. strain PCC 7942 corresponds to a mobA
RT gene for molybdopterin guanine dinucleotide biosynthesis.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S.,
RA Gonzalez A., Salinas I., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC7942 cosmid 7G3.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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 -!- 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; Y13330; CAA73772.1; -; Genomic_DNA.
DR EMBL; AY120853; AAM82714.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57219.1; -; Genomic_DNA.
DR RefSeq; WP_011242674.1; NC_007604.1.
DR AlphaFoldDB; O06866; -.
DR SMR; O06866; -.
DR STRING; 1140.Synpcc7942_1189; -.
DR PRIDE; O06866; -.
DR EnsemblBacteria; ABB57219; ABB57219; Synpcc7942_1189.
DR KEGG; syf:Synpcc7942_1189; -.
DR eggNOG; COG0746; Bacteria.
DR HOGENOM; CLU_055597_2_2_3; -.
DR OMA; LFNCNTP; -.
DR OrthoDB; 2019898at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1189-MON; -.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Transferase.
FT CHAIN 1..194
FT /note="Probable molybdenum cofactor guanylyltransferase"
FT /id="PRO_0000134920"
FT BINDING 8..10
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 20
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 194 AA; 21572 MW; D90C18E26B2FC111 CRC64;
MNFAALILAG GSSRRMGQDK ALLRLNGEPL LIRTSRIAAA VCDSVWICSP EPDRYQSLLS
QPVQWLTEPQ PTGPQGPLTA LAWALPQIDA DWILLLACDL PRLAIAPLQA WRQQVELLPE
DCRAAIARTE QGWEPLIGFY RPAIAPTIAP WLSQGRRDFQ GWLATVAVQE LPLSDRDWLV
NCNTPTDWQA LQLS
