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MOAC_BRADU
ID   MOAC_BRADU              Reviewed;         172 AA.
AC   P94328;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01224};
DE            EC=4.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01224};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_01224};
GN   Name=moaC; OrderedLocusNames=blr4811;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=9061023; DOI=10.1016/s0167-4781(96)00237-0;
RA   Kuykendall L.D., Hunter W.J.;
RT   "The sequence of a symbiotically essential Bradyrhizobium japonicum operon
RT   consisting of trpD, trpC and a moaC-like gene.";
RL   Biochim. Biophys. Acta 1350:277-281(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC       (cPMP). {ECO:0000255|HAMAP-Rule:MF_01224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC         pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC         EC=4.6.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01224};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01224}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01224}.
CC   -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01224}.
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DR   EMBL; U79771; AAB39008.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC50076.1; -; Genomic_DNA.
DR   PIR; T46960; T46960.
DR   RefSeq; NP_771451.1; NC_004463.1.
DR   RefSeq; WP_011087579.1; NZ_CP011360.1.
DR   AlphaFoldDB; P94328; -.
DR   SMR; P94328; -.
DR   STRING; 224911.27353075; -.
DR   EnsemblBacteria; BAC50076; BAC50076; BAC50076.
DR   GeneID; 64024565; -.
DR   KEGG; bja:blr4811; -.
DR   PATRIC; fig|224911.44.peg.4650; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_5; -.
DR   InParanoid; P94328; -.
DR   OMA; IWDMVKS; -.
DR   PhylomeDB; P94328; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01420; MoaC_PE; 1.
DR   Gene3D; 3.30.70.640; -; 1.
DR   HAMAP; MF_01224_B; MoaC_B; 1.
DR   InterPro; IPR023045; Mo_CF_biosynth-C.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; SSF55040; 1.
DR   TIGRFAMs; TIGR00581; moaC; 1.
PE   3: Inferred from homology;
KW   Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..172
FT                   /note="Cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_0000097788"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         90..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         128..129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   CONFLICT        105
FT                   /note="P -> T (in Ref. 1; AAB39008)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   172 AA;  18032 MW;  30F62636A9EAF915 CRC64;
     MARKPSKTRP SKAKSGPALT HIGATGEARM VDVSDKPATE RLAVAEGRVL MTRATLDLIV
     SGNAKKGDVL GTARIAGIMA AKRTSELIPL CHPLALSKVT VDIEPDAKLP GCLVRASVKV
     TGPTGVEMEA LTAVSVACLT IYDMIKAVER GVRIEGIHLV EKLGGKSGHY RA
 
 
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