MOBA_AQUAE
ID MOBA_AQUAE Reviewed; 201 AA.
AC O67413;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable molybdenum cofactor guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE Short=MoCo guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE EC=2.7.7.77 {ECO:0000255|HAMAP-Rule:MF_00316};
DE AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE AltName: Full=Mo-MPT guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE AltName: Full=Molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316};
DE AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_00316};
DE Short=MGD synthase {ECO:0000255|HAMAP-Rule:MF_00316};
GN Name=mobA {ECO:0000255|HAMAP-Rule:MF_00316}; OrderedLocusNames=aq_1419;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00316};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00316};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00316}.
CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000255|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; AE000657; AAC07379.1; -; Genomic_DNA.
DR PIR; C70423; C70423.
DR RefSeq; NP_213978.1; NC_000918.1.
DR PDB; 2E8B; X-ray; 1.61 A; A=1-201.
DR PDBsum; 2E8B; -.
DR AlphaFoldDB; O67413; -.
DR SMR; O67413; -.
DR STRING; 224324.aq_1419; -.
DR EnsemblBacteria; AAC07379; AAC07379; aq_1419.
DR KEGG; aae:aq_1419; -.
DR PATRIC; fig|224324.8.peg.1109; -.
DR eggNOG; COG0746; Bacteria.
DR HOGENOM; CLU_055597_2_2_0; -.
DR InParanoid; O67413; -.
DR OMA; HENGYIE; -.
DR OrthoDB; 2019898at2; -.
DR EvolutionaryTrace; O67413; -.
DR Proteomes; UP000000798; 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:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02503; MobA; 1.
DR Gene3D; 3.90.550.10; -; 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 Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..201
FT /note="Probable molybdenum cofactor guanylyltransferase"
FT /id="PRO_0000134879"
FT BINDING 20..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2E8B"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 32..51
FT /evidence="ECO:0007829|PDB:2E8B"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:2E8B"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:2E8B"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:2E8B"
FT STRAND 124..142
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:2E8B"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2E8B"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:2E8B"
SQ SEQUENCE 201 AA; 23350 MW; A6CCA2EA209DBCAA CRC64;
MRTFTWRKGS LSKVNTCYVL AGGKSKRFGE DKLLYEIKGK KVIERVYETA KSVFKEVYIV
AKDREKFSFL NAPVVLDEFE ESASIIGLYT ALKHAKEENV FVLSGDLPLM KKETVLYVLE
NFKEPVSVAK TEKLHTLVGV YSKKLLEKIE ERIKKGDYRI WALLKDVGYN EVEIPEELRY
TLLNMNTKED LKRILAIENH Y
