ID C7ML65_CRYCD Unreviewed; 484 AA.
AC C7ML65;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=Ccur_13350 {ECO:0000313|EMBL:ACU95012.1};
OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS 12-3).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Cryptobacterium.
OX NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU95012.1, ECO:0000313|Proteomes:UP000000954};
RN [1] {ECO:0000313|EMBL:ACU95012.1, ECO:0000313|Proteomes:UP000000954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC {ECO:0000313|Proteomes:UP000000954};
RX PubMed=21304644; DOI=10.40456/sigs.12260;
RA Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL Stand. Genomic Sci. 1:93-100(2009).
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; CP001682; ACU95012.1; -; Genomic_DNA.
DR RefSeq; WP_015778875.1; NC_013170.1.
DR AlphaFoldDB; C7ML65; -.
DR STRING; 469378.Ccur_13350; -.
DR KEGG; ccu:Ccur_13350; -.
DR eggNOG; COG0746; Bacteria.
DR eggNOG; COG1763; Bacteria.
DR HOGENOM; CLU_677747_0_0_11; -.
DR Proteomes; UP000000954; 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:UP000000954};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00316}.
FT DOMAIN 13..130
FT /note="Molybdopterin-guanine dinucleotide biosynthesis
FT protein B (MobB)"
FT /evidence="ECO:0000259|Pfam:PF03205"
FT DOMAIN 223..379
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT REGION 435..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 289
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 318
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00316"
SQ SEQUENCE 484 AA; 52113 MW; 365BAFC2889AE8AD CRC64;
MISNTSIIPS PAVSVVGRHN SGKTTLVEAV IARLVADGLD IGSVKHHGHV GFDIDIPGKD
SYRHRAAGAS ETVISAPGQV ACIKTISGEA ECSQLVKSMP GHDLVIVEGY RKSGLPSIEV
MRAANTADTN VAQIFLKAAQ SGQPLTTDFI QAARASHTPA PDPGAPVDAG KIPQASTVAV
VSDIPSAHEA AGIYGIPAFN LNDVDGLCAF LRERYARPRI SVVLQAGGES RRMGHSKALV
SFEGRPLIMR LIERVAPAAD EIIVTTNEAK KLAFLQQEYP QLSLRLETDR LDYRGALPGM
LTALSAAHNE QVAIIACDMV FASPRLIVAE SQEMQRTGAD VVVPVNRNGF EPFHALYRRS
SCLPQIEVRL KQGESRAQAI FPFVSLCEFP QAKVLETEPG GRCFINVNTP DDLDFAERLA
EKDTLWKPAL QPAEHNRPSC AVKKSSQQAV SQLKEDAQRA ASQSAVDQSS FSQTNQDSQI
EECR
//
