GenomeNet

Database: UniProt
Entry: W1IZR0_9GAMM
LinkDB: W1IZR0_9GAMM
Original site: W1IZR0_9GAMM 
ID   W1IZR0_9GAMM            Unreviewed;       159 AA.
AC   W1IZR0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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:CDL83111.1};
GN   ORFNames=XSR1_290033 {ECO:0000313|EMBL:CDL83111.1};
OS   Xenorhabdus szentirmaii DSM 16338.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL83111.1, ECO:0000313|Proteomes:UP000019202};
RN   [1] {ECO:0000313|EMBL:CDL83111.1, ECO:0000313|Proteomes:UP000019202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL83111.1,
RC   ECO:0000313|Proteomes:UP000019202};
RA   Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT   "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT   Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT   16338.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDL83111.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBXF010000087; CDL83111.1; -; Genomic_DNA.
DR   RefSeq; WP_038238136.1; NZ_NIBV01000002.1.
DR   AlphaFoldDB; W1IZR0; -.
DR   STRING; 1427518.XSR1_290033; -.
DR   OrthoDB; 9794429at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000019202; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019202}.
FT   DOMAIN          15..150
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         113..114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   159 AA;  17266 MW;  CB2CACAE8E5A5F20 CRC64;
     MSRLTHINTA GEAHMVDISS KSDTVREAKA EAFVEMQPET LAMIVAGDHH KGDVFATARI
     AGIQAAKKTW DLIPLCHPLL LSKIDVRLEA QTEHNRVRIE SCCRLTGKTG VEMEALTAAS
     VAALTIYDMC KAVQKDMVIG PVRLLEKSGG KSGHFKVEA
//
DBGET integrated database retrieval system