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Database: UniProt
Entry: A7K6T4_9BURK
LinkDB: A7K6T4_9BURK
Original site: A7K6T4_9BURK 
ID   A7K6T4_9BURK            Unreviewed;       175 AA.
AC   A7K6T4;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   13-SEP-2023, entry version 76.
DE   RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE            EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575, 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   ECO:0000313|EMBL:ABS84671.1};
OS   Advenella mimigardefordensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=302406 {ECO:0000313|EMBL:ABS84671.1};
RN   [1] {ECO:0000313|EMBL:ABS84671.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17509837; DOI=10.1016/j.resmic.2006.12.013;
RA   Dam B., Mandal S., Ghosh W., Das Gupta S.K., Roy P.;
RT   "The S4-intermediate pathway for the oxidation of thiosulfate by the
RT   chemolithoautotroph Tetrathiobacter kashmirensis and inhibition of
RT   tetrathionate oxidation by sulfite.";
RL   Res. Microbiol. 158:330-338(2007).
CC   -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC       (cPMP). {ECO:0000256|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:0000256|ARBA:ARBA00001637,
CC         ECO:0000256|HAMAP-Rule:MF_01224};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_01224}.
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; EF017216; ABS84671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7K6T4; -.
DR   UniPathway; UPA00344; -.
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; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR   HAMAP; MF_01224_B; MoaC_B; 1.
DR   InterPro; IPR023045; MoaC.
DR   InterPro; IPR047594; MoaC_bact/euk.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   NCBIfam; TIGR00581; moaC; 1.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01224};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|HAMAP-Rule:MF_01224}.
FT   DOMAIN          32..167
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         92..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         130..131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   175 AA;  18593 MW;  7D06667287A64BDA CRC64;
     MKKTSVVSDT PAKADTAASA LSHLDEAGQV RMVDVLGKTA TARTAVARSI VRMTPRSYAA
     LNAAENSKGE VLNTARVAGV LAAKRCAELI PMCHSLPLTF AGIDFALDDQ AQCVTIRATC
     RSDYKTGVEM EALTACSIAA LTIYDMCKAA DKGIIIEDTR LEYKSGGKSG EWRCD
//
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