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MOBA_CLOPE
ID   MOBA_CLOPE              Reviewed;         198 AA.
AC   Q9WX94;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 112.
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=CPE1792;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10543 / DSM 798 / NCIB 8875 / BP6K / Type A;
RX   PubMed=10627036; DOI=10.1099/00221287-145-12-3377;
RA   Fujinaga K., Taniguchi Y., Sun Y., Katayama S., Minami J., Matsushita O.,
RA   Okabe A.;
RT   "Analysis of genes involved in nitrate reduction in Clostridium
RT   perfringens.";
RL   Microbiology 145:3377-3387(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAB81498.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB017192; BAA76926.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB81498.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041707861.1; NC_003366.1.
DR   AlphaFoldDB; Q9WX94; -.
DR   SMR; Q9WX94; -.
DR   STRING; 195102.gene:10491056; -.
DR   EnsemblBacteria; BAB81498; BAB81498; BAB81498.
DR   KEGG; cpe:CPE1792; -.
DR   HOGENOM; CLU_055597_2_0_9; -.
DR   OMA; LFNCNTP; -.
DR   Proteomes; UP000000818; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..198
FT                   /note="Probable molybdenum cofactor guanylyltransferase"
FT                   /id="PRO_0000134885"
FT   BINDING         9..11
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00316"
FT   CONFLICT        41
FT                   /note="K -> E (in Ref. 1; BAA76926)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="E -> G (in Ref. 1; BAA76926)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="S -> G (in Ref. 1; BAA76926)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   198 AA;  23318 MW;  72FD6656F8DA4654 CRC64;
     MIKKSAAILA GGKSSRMNYR NKAFLKYEED YFIERIIKAL KDYEEIIIIS NNPEEYKEFG
     LKVFKDIYPS QGPLSGIHSA LNHIKNDYCL VVACDMPFIN KDVVNYLGNI KEDYEILIPK
     FQERLQPLCA IYKKSCKDIM EKELINNSNK LIKTCFKFSM KVVEEFPFIE KVHKKEIKNF
     YNINTVDEYE DLIKKKEI
 
 
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