ID A0A0A8B5M2_9ACTN Unreviewed; 420 AA.
AC A0A0A8B5M2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=JI75_08685 {ECO:0000313|EMBL:AJC12715.1};
OS Berryella intestinalis.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Berryella.
OX NCBI_TaxID=1531429 {ECO:0000313|EMBL:AJC12715.1, ECO:0000313|Proteomes:UP000031121};
RN [1] {ECO:0000313|Proteomes:UP000031121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-1-3 {ECO:0000313|Proteomes:UP000031121};
RA Looft T., Bayles D.O., Stanton T.B.;
RT "Coriobacteriaceae sp. complete genome.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJC12715.1, ECO:0000313|Proteomes:UP000031121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-1-3 {ECO:0000313|EMBL:AJC12715.1,
RC ECO:0000313|Proteomes:UP000031121};
RX PubMed=26450725;
RA Looft T., Bayles D.O., Alt D.P., Stanton T.B.;
RT "Complete Genome Sequence of Coriobacteriaceae Strain 68-1-3, a Novel
RT Mucus-Degrading Isolate from the Swine Intestinal Tract.";
RL Genome Announc. 3:e01143-15(2015).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00316}.
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DR EMBL; CP009302; AJC12715.1; -; Genomic_DNA.
DR RefSeq; WP_039690147.1; NZ_CP009302.1.
DR AlphaFoldDB; A0A0A8B5M2; -.
DR STRING; 1531429.JI75_08685; -.
DR KEGG; cbac:JI75_08685; -.
DR HOGENOM; CLU_677747_0_0_11; -.
DR OrthoDB; 9788394at2; -.
DR Proteomes; UP000031121; 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 CDD; cd03116; MobB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00316; MobA; 1.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR004435; MobB_dom.
DR InterPro; IPR013482; Molybde_CF_guanTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00176; mobB; 1.
DR PANTHER; PTHR40072:SF1; MOLYBDOPTERIN-GUANINE DINUCLEOTIDE BIOSYNTHESIS ADAPTER PROTEIN; 1.
DR PANTHER; PTHR40072; MOLYBDOPTERIN-GUANINE DINUCLEOTIDE BIOSYNTHESIS ADAPTER PROTEIN-RELATED; 1.
DR Pfam; PF03205; MobB; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Reference proteome {ECO:0000313|Proteomes:UP000031121};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00316}.
FT DOMAIN 9..123
FT /note="Molybdopterin-guanine dinucleotide biosynthesis
FT protein B (MobB)"
FT /evidence="ECO:0000259|Pfam:PF03205"
FT DOMAIN 219..374
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT BINDING 234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 315
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ SEQUENCE 420 AA; 45115 MW; EBAFFD955870EF94 CRC64;
MVEVKSPAVA FVGRHNSGKT TLIVKLIEEL VARGVDVGSV KHHSHVGFEI DIPGKDSYRH
RHAGASETVI AAPGQMACIK TVEGDVECAD IVAGMPGHDI VIVEGYRKSG LPTIEIMREG
NPADMKAASA FAQGAREGWP LDSDFTQIGR RVSDDEPRQI DYLDVSEKLP GAATVAVVAD
IPCAIEAARA YGIPSFGLDA VSELADFLEE RHVRPKVTVV IQAGGESRRM GRSKATVPFG
GRPLICRLVD RVSPVADELV VTTNEPDNLA FLLEEYPGLD IRLERDVCDA RGALPGLYTA
IEVASHPYVA VVACDMIFAS PRLIAAEAEA LTSSGADAVV PVNKHGYEPF HALYRKSACL
PVVKAGVEAG ERAAQYVVRH VNVRKFPQSE VLAAEPMGGC FVNANTPEEL ASFERWYLDA
//
