MOAC_PSEU2
ID MOAC_PSEU2 Reviewed; 161 AA.
AC Q4ZXJ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Psyr_1067;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY36123.1; -; Genomic_DNA.
DR RefSeq; WP_003341741.1; NC_007005.1.
DR RefSeq; YP_234161.1; NC_007005.1.
DR AlphaFoldDB; Q4ZXJ9; -.
DR SMR; Q4ZXJ9; -.
DR STRING; 205918.Psyr_1067; -.
DR EnsemblBacteria; AAY36123; AAY36123; Psyr_1067.
DR GeneID; 64442251; -.
DR GeneID; 65075206; -.
DR KEGG; psb:Psyr_1067; -.
DR PATRIC; fig|205918.7.peg.1097; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_074693_1_1_6; -.
DR OMA; IWDMVKS; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000426; 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.
FT CHAIN 1..161
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_1000054122"
FT ACT_SITE 125
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 73..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 161 AA; 16932 MW; 9F14BC41400D3D9F CRC64;
MLTHLDSQGR ANMVDVTDKA VTSREAVAEA FVRMLPTTLQ MIVSGGHPKG DVFAVARIAG
IQAAKKTSDL IPLCHPLMLT SIKVHLAAEG DDAVRITASC KLAGQTGVEM EALTAASVAA
LTIYDMCKAV DRGMVIESVR LLEKLGGKSG HFIADQAQVS S
