(data stored in SCRATCH zone)

SWISSPROT: Q47T04_THEFY

ID   Q47T04_THEFY            Unreviewed;       162 AA.
AC   Q47T04;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 108.
DE   RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000256|HAMAP-Rule:MF_01224};
DE            EC=4.6.1.17 {ECO:0000256|HAMAP-Rule:MF_01224};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_01224};
GN   Name=moaC {ECO:0000256|HAMAP-Rule:MF_01224};
GN   OrderedLocusNames=Tfu_0375 {ECO:0000313|EMBL:AAZ54413.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54413.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate to cyclic pyranopterin
CC       monophosphate (cPMP). {ECO:0000256|HAMAP-Rule:MF_01224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate =
CC         cyclic pyranopterin phosphate + diphosphate;
CC         Xref=Rhea:RHEA:49580, ChEBI:CHEBI:33019, ChEBI:CHEBI:59648,
CC         ChEBI:CHEBI:131766; EC=4.6.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01224, ECO:0000256|SAAS:SAAS01115723};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01224, ECO:0000256|SAAS:SAAS00100831}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_01224}.
CC   -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01224}.
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DR   EMBL; CP000088; AAZ54413.1; -; Genomic_DNA.
DR   RefSeq; WP_011290822.1; NC_007333.1.
DR   STRING; 269800.Tfu_0375; -.
DR   EnsemblBacteria; AAZ54413; AAZ54413; Tfu_0375.
DR   KEGG; tfu:Tfu_0375; -.
DR   eggNOG; ENOG4108YXW; Bacteria.
DR   eggNOG; COG0315; LUCA.
DR   HOGENOM; HOG000228417; -.
DR   KO; K03637; -.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 1595361at2; -.
DR   BioCyc; TFUS269800:G1G4Q-378-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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;
DR   PRODOM; Q47T04.
DR   SWISS-2DPAGE; Q47T04.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Hydrolase {ECO:0000313|EMBL:AAZ54413.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01224,
KW   ECO:0000256|SAAS:SAAS00703322};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01224,
KW   ECO:0000256|SAAS:SAAS00100825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN       20    153       MoaC. {ECO:0000259|Pfam:PF01967}.
FT   REGION       80     82       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   REGION      116    117       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01224}.
FT   ACT_SITE    131    131       {ECO:0000256|HAMAP-Rule:MF_01224}.
SQ   SEQUENCE   162 AA;  16707 MW;  F214E2C7E00A1179 CRC64;
     MSHPSTPGFP HLDASGAARM VDVSGKEVTA RSAVATGRVL LSPAAVAALR EGAVPKGDAL
     AVARIAGIQG AKRTPDLVPL CHPIAIHGVD VALTVVDRGV DIRATVRTAD RTGVEMEALT
     CVMTAALALI DMVKALDPEA VVTDVRVEEK TGGKTGQWRR SG
//

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