位置:首页 > 蛋白库 > MOBA_HELPJ
MOBA_HELPJ
ID   MOBA_HELPJ              Reviewed;         209 AA.
AC   Q9ZL74;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=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=jhp_0706;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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   -!- SUBUNIT: Monomer. {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; AE001439; AAD06291.1; -; Genomic_DNA.
DR   PIR; E71897; E71897.
DR   RefSeq; WP_000795345.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZL74; -.
DR   SMR; Q9ZL74; -.
DR   STRING; 85963.jhp_0706; -.
DR   EnsemblBacteria; AAD06291; AAD06291; jhp_0706.
DR   KEGG; hpj:jhp_0706; -.
DR   PATRIC; fig|85963.30.peg.271; -.
DR   eggNOG; COG0746; Bacteria.
DR   OMA; HYLISLW; -.
DR   Proteomes; UP000000804; 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   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   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Magnesium; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN           1..209
FT                   /note="Molybdenum cofactor guanylyltransferase"
FT                   /id="PRO_0000134893"
FT   BINDING         14..16
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         104
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
SQ   SEQUENCE   209 AA;  23918 MW;  055B7E1FF932DE12 CRC64;
     MKNPIINNIP CVLLAGGKSS RFIINNIPIN KALMPLKSYP SLLEYQYTRL LKLFKQVIIS
     AKKSYELNAP YLLEKEGGLF SPLFGIHNAF LTLQTPYIFF IAIDTPLVSF ESIKILCGIQ
     NFSVVYAKSP TKEHYLISLW HQSILNALNY TLKTQNYRLS DLIKNASSTA IHFDKEEEFL
     NLNTLKDYEL AVQILKEGSN GRRRKDRTP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024