ID A6US69_METVS Unreviewed; 212 AA.
AC A6US69;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Probable 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=Mevan_1447 {ECO:0000313|EMBL:ABR55341.1};
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327 {ECO:0000313|EMBL:ABR55341.1, ECO:0000313|Proteomes:UP000001107};
RN [1] {ECO:0000313|EMBL:ABR55341.1, ECO:0000313|Proteomes:UP000001107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB
RC {ECO:0000313|Proteomes:UP000001107};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_00316};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00316};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00316}.
CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000256|HAMAP-
CC Rule:MF_00316}.
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DR EMBL; CP000742; ABR55341.1; -; Genomic_DNA.
DR RefSeq; WP_012066255.1; NC_009634.1.
DR AlphaFoldDB; A6US69; -.
DR STRING; 406327.Mevan_1447; -.
DR GeneID; 5324845; -.
DR KEGG; mvn:Mevan_1447; -.
DR eggNOG; arCOG01872; Archaea.
DR HOGENOM; CLU_055597_2_0_2; -.
DR OrthoDB; 28434at2157; -.
DR Proteomes; UP000001107; Chromosome.
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 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; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR PANTHER; PTHR19136:SF85; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE-RELATED; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00316}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00316};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00316};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_00316};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00316}; Transferase {ECO:0000256|HAMAP-Rule:MF_00316}.
FT DOMAIN 4..168
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT BINDING 7..9
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ SEQUENCE 212 AA; 24183 MW; 278733EFCB756D5D CRC64;
MISAVILSGG KAERMNGEKS FRTFGNKYLI ENIADILNSL KIPFTTVFKN PVFLKDSSSE
IEKQVYFYKK YNQAITWDMI PEMGPLVGML SGMINCDSSW VLLVPCDMPF ITEKSIENLI
NCIPIAEYKN CNAIVPKHEN GFIEPIFALY HRSTINALQK IVLETKEKKC SYPIRRLIDE
INPLFMNISK IDPTGNVFLN INTIEELNSN IF
//
