MOBB_METJA
ID MOBB_METJA Reviewed; 234 AA.
AC Q58720;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Putative molybdopterin-guanine dinucleotide biosynthesis adapter protein;
DE Short=MGD biosynthesis adapter protein;
DE AltName: Full=Molybdenum cofactor biosynthesis adapter protein;
DE Short=Moco biosynthesis adapter protein;
GN Name=mobB; OrderedLocusNames=MJ1324;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: GTP-binding protein that is not required for the biosynthesis
CC of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not
CC necessary for the formation of active molybdoenzymes using this form of
CC molybdenum cofactor. May act as an adapter protein to achieve the
CC efficient biosynthesis and utilization of MGD. Displays a weak
CC intrinsic GTPase activity (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00989};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00989};
CC -!- SIMILARITY: Belongs to the MobB family. {ECO:0000305}.
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DR EMBL; L77117; AAB99333.1; -; Genomic_DNA.
DR PIR; C64465; C64465.
DR RefSeq; WP_010870841.1; NC_000909.1.
DR AlphaFoldDB; Q58720; -.
DR SMR; Q58720; -.
DR STRING; 243232.MJ_1324; -.
DR PRIDE; Q58720; -.
DR EnsemblBacteria; AAB99333; AAB99333; MJ_1324.
DR GeneID; 1452226; -.
DR KEGG; mja:MJ_1324; -.
DR eggNOG; arCOG00532; Archaea.
DR HOGENOM; CLU_068199_0_1_2; -.
DR InParanoid; Q58720; -.
DR OMA; HCGYNCK; -.
DR OrthoDB; 62565at2157; -.
DR PhylomeDB; Q58720; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR004435; MobB_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04060; FeS; 1.
DR Pfam; PF03205; MobB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00176; mobB; 1.
DR PROSITE; PS51656; 4FE4S; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; GTP-binding; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome.
FT CHAIN 1..234
FT /note="Putative molybdopterin-guanine dinucleotide
FT biosynthesis adapter protein"
FT /id="PRO_0000107276"
FT DOMAIN 134..196
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 11..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 42..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 86..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
SQ SEQUENCE 234 AA; 26080 MW; F79BB9B1642A5E1B CRC64;
MRVIGVIGYK DSGKTTLIEE ILKHSDKKIA VIKHTKEDVE VDKKGTDTYR LSNAGAKITV
LATDSKTVFF TDRMDLENIL SVLSDYNIDF VIIEGFKEAL KRLNIPKIVM LKDKDGSDLI
DDHTAMIIED YNYNIDDVLK VIYEKAVVPT MNLNCGHCGY NCRTFVKAVV KGEARWDDCV
LAKGIKIIVD GKIIPAVPFV SKIVGSTIKA MIETLKGVDN PKTIKVEIDV SKLK
