ID L0JN57_NATP1 Unreviewed; 210 AA.
AC L0JN57;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Natpe_2902 {ECO:0000313|EMBL:AGB32699.1};
GN ORFNames=C488_08622 {ECO:0000313|EMBL:ELY75910.1};
OS Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / NCIMB
OS 786 / 157).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB32699.1, ECO:0000313|Proteomes:UP000010843};
RN [1] {ECO:0000313|Proteomes:UP000010843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC {ECO:0000313|Proteomes:UP000010843};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB32699.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:AGB32699.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|Proteomes:UP000011593};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ELY75910.1, ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:ELY75910.1,
RC ECO:0000313|Proteomes:UP000011593};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003372; AGB32699.1; -; Genomic_DNA.
DR EMBL; AOIE01000061; ELY75910.1; -; Genomic_DNA.
DR RefSeq; WP_006181090.1; NZ_AOIE01000061.1.
DR AlphaFoldDB; L0JN57; -.
DR STRING; 797303.Natpe_2902; -.
DR GeneID; 14333482; -.
DR KEGG; npe:Natpe_2902; -.
DR PATRIC; fig|797303.5.peg.1723; -.
DR eggNOG; arCOG01872; Archaea.
DR HOGENOM; CLU_055597_2_1_2; -.
DR OrthoDB; 28434at2157; -.
DR Proteomes; UP000010843; Chromosome.
DR Proteomes; UP000011593; Unassembled WGS sequence.
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 9..167
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT BINDING 12..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ SEQUENCE 210 AA; 22631 MW; 669D7F562791FADD CRC64;
MTLESDRSAV VLAGGGSTRF GDADKAVADL AGTPMVRRVV DRLEPVVDEV VVNCREAQVP
ALEDALAGGP DPSFAVDPVP DRGPMAGIMT GLQEATGEYA AVVACDMPFV DPALIAHLFE
RAAGRDAAVP RVDDQWFQTT QAVYRADPMI AACERALERG DRRVVEPLSD LDYVVCEDDD
VREYASLETF ENLNTREEFE AAAERLAADS
//
