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Database: UniProt
Entry: A0A0R0MNX4_9BURK
LinkDB: A0A0R0MNX4_9BURK
Original site: A0A0R0MNX4_9BURK 
ID   A0A0R0MNX4_9BURK        Unreviewed;       207 AA.
AC   A0A0R0MNX4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   ORFNames=AO057_13395 {ECO:0000313|EMBL:KRI00465.1};
OS   Curvibacter sp. PAE-UM.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Curvibacter.
OX   NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRI00465.1, ECO:0000313|Proteomes:UP000051912};
RN   [1] {ECO:0000313|EMBL:KRI00465.1, ECO:0000313|Proteomes:UP000051912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAE-UM {ECO:0000313|EMBL:KRI00465.1,
RC   ECO:0000313|Proteomes:UP000051912};
RA   Ma D.;
RT   "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT   river sediment.";
RL   Submitted (SEP-2015) 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   -!- SUBUNIT: Monomer. {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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRI00465.1}.
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DR   EMBL; LKCX01000018; KRI00465.1; -; Genomic_DNA.
DR   RefSeq; WP_057676413.1; NZ_KQ483358.1.
DR   AlphaFoldDB; A0A0R0MNX4; -.
DR   STRING; 1714344.AO057_13395; -.
DR   OrthoDB; 9788394at2; -.
DR   Proteomes; UP000051912; 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   NCBIfam; TIGR02665; molyb_mobA; 1.
DR   PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR19136:SF81; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 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|HAMAP-Rule:MF_00316};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:KRI00465.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051912};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00316}.
FT   DOMAIN          9..170
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         71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT   BINDING         101
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ   SEQUENCE   207 AA;  22505 MW;  F46C809BE8947CDC CRC64;
     MIDSSEITGL ILAGGRGSRM GGVDKGLQNF NGMPMALHTL MRLQMQVGQV MINANRNLAA
     YESFGAEVWP DVLADYAGPL AGFLTGLERC ETPYLVTAPC DSPRFPLDLV ARLAEAMDRE
     QAEIAMAAAP EKDEQGEVKV RTQPVFCLLR IELLESLVQF TQGGGRKIDA WTALHKTVVV
     PFDRPGDDPL AFANANTLAE LKQLENS
//
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