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MOAC_GEOKA
ID   MOAC_GEOKA              Reviewed;         162 AA.
AC   Q5L3F4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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 {ECO:0000255|HAMAP-Rule:MF_01224}; OrderedLocusNames=GK0241;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Structure of GK0241 protein from Geobacillus kaustophilus.";
RL   Submitted (JUL-2011) to the PDB data bank.
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; BA000043; BAD74526.1; -; Genomic_DNA.
DR   RefSeq; WP_011229750.1; NC_006510.1.
DR   PDB; 2EEY; X-ray; 1.94 A; A=1-162.
DR   PDBsum; 2EEY; -.
DR   AlphaFoldDB; Q5L3F4; -.
DR   SMR; Q5L3F4; -.
DR   STRING; 235909.GK0241; -.
DR   EnsemblBacteria; BAD74526; BAD74526; GK0241.
DR   KEGG; gka:GK0241; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_9; -.
DR   OMA; IWDMVKS; -.
DR   UniPathway; UPA00344; -.
DR   EvolutionaryTrace; Q5L3F4; -.
DR   Proteomes; UP000001172; 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   1: Evidence at protein level;
KW   3D-structure; Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..162
FT                   /note="Cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_1000054095"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         115..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   STRAND          5..7
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   STRAND          24..36
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   HELIX           38..45
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   HELIX           54..72
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   STRAND          83..91
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   STRAND          93..111
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   HELIX           114..132
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:2EEY"
FT   STRAND          145..152
FT                   /evidence="ECO:0007829|PDB:2EEY"
SQ   SEQUENCE   162 AA;  17467 MW;  97E63C0D207471CA CRC64;
     MSSFTHFNEQ GRAKMVDITH KEDTVRVAVA QTSVTVSREI YEKMTSNAIE KGDVLAVAQV
     AGVMAAKKTA DLIPMCHPLM LKGVDIAFAW ENDGEAHKLV ITATVKTKGS TGVEMEALTA
     ASVCALTVYD MCKALDKGMV IGPTYLVEKT GGKSGHYRRK TD
 
 
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