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
//