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MOC2B_MAGO7
ID   MOC2B_MAGO7             Reviewed;         182 AA.
AC   Q2KF83; A4RB33; G4NKV0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE            EC=2.8.1.12 {ECO:0000255|HAMAP-Rule:MF_03052};
DE   AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein H {ECO:0000255|HAMAP-Rule:MF_03052};
DE   AltName: Full=Molybdenum cofactor synthesis protein 2 large subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE   AltName: Full=Molybdenum cofactor synthesis protein 2B {ECO:0000255|HAMAP-Rule:MF_03052};
DE            Short=MOCS2B {ECO:0000255|HAMAP-Rule:MF_03052};
GN   Name=cnxH {ECO:0000255|HAMAP-Rule:MF_03052};
GN   ORFNames=MGCH7_ch7g803, MGG_03018;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a
CC       complex that catalyzes the conversion of precursor Z into
CC       molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms
CC       from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene
CC       group. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC         Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2
CC         [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly +
CC         4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160,
CC         Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:90778; EC=2.8.1.12; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03052};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03052}.
CC   -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC       (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03052}.
CC   -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR   EMBL; CM000230; EAQ71396.1; -; Genomic_DNA.
DR   EMBL; CM001237; EHA45928.1; -; Genomic_DNA.
DR   RefSeq; XP_003720671.1; XM_003720623.1.
DR   AlphaFoldDB; Q2KF83; -.
DR   SMR; Q2KF83; -.
DR   STRING; 318829.MGG_17889T0; -.
DR   EnsemblFungi; MGG_17889T0; MGG_17889T0; MGG_17889.
DR   GeneID; 12984757; -.
DR   KEGG; mgr:MGG_17889; -.
DR   VEuPathDB; FungiDB:MGG_17889; -.
DR   eggNOG; KOG3307; Eukaryota.
DR   HOGENOM; CLU_089568_3_1_1; -.
DR   InParanoid; Q2KF83; -.
DR   OMA; WPLQRVS; -.
DR   OrthoDB; 1419096at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000009058; Chromosome 7.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00756; MoaE; 1.
DR   Gene3D; 3.90.1170.40; -; 1.
DR   HAMAP; MF_03052; MOC2B; 1.
DR   InterPro; IPR036563; MoaE_sf.
DR   InterPro; IPR028888; MOCS2B_euk.
DR   InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR   Pfam; PF02391; MoaE; 1.
DR   SUPFAM; SSF54690; SSF54690; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Molybdenum cofactor biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..182
FT                   /note="Molybdopterin synthase catalytic subunit"
FT                   /id="PRO_0000369356"
FT   REGION          152..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119..120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT   BINDING         142..144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
SQ   SEQUENCE   182 AA;  19708 MW;  132470EC73475DA4 CRC64;
     MSQLDSAQLP NEANEVGEDG CYVGLTHDKL DVQRTMDRVR SPEAGAIVVF VGTTRNSFDG
     KPVKELNYTA YNPMALRTMI SICKAMKTKH GLKGIAMVHR LGVVPISEDS IVIAVSSPHR
     QAAWRAGEEA LEECKAKVEV WKREEFEGGE GVWRANRDGA PGQRIDTAEP AVGAGSGGEI
     DD
 
 
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