UniProt: Q9WX95

Database: UniProt
Entry: Q9WX95_CLOPF

LinkDB:  Q9WX95_CLOPF 
Original site:  Q9WX95_CLOPF

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (14)   

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ID   Q9WX95_CLOPF            Unreviewed;       337 AA.
AC   Q9WX95;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeC {ECO:0000313|EMBL:BAA76927.1};
GN   ORFNames=G6Z34_05425 {ECO:0000313|EMBL:NGU29556.1}, HMPREF3222_00266
GN   {ECO:0000313|EMBL:KXA14691.1};
OS   Clostridium perfringens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502 {ECO:0000313|EMBL:BAA76927.1};
RN   [1] {ECO:0000313|EMBL:BAA76927.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PB6K {ECO:0000313|EMBL:BAA76927.1};
RX   PubMed=10627036;
RA   Fujinaga K., Taniguchi Y., Sun Y., Katayama S., Minami J., Matsushita O.,
RA   Okabe A.;
RT   "Analysis of genes involved in nitrate reduction in Clostridium
RT   perfringens.";
RL   Microbiology 145:3377-3387(1999).
RN   [2] {ECO:0000313|EMBL:KXA14691.1, ECO:0000313|Proteomes:UP000070646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJR7757A {ECO:0000313|EMBL:KXA14691.1,
RC   ECO:0000313|Proteomes:UP000070646};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:NGU29556.1, ECO:0000313|Proteomes:UP000481454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP-40 {ECO:0000313|EMBL:NGU29556.1,
RC   ECO:0000313|Proteomes:UP000481454};
RA   Feng Y., Hu Y.;
RT   "Genomic Insights into the Phylogeny and Genetic Plasticity of the Human
RT   and Animal Enteric Pathogen Clostridium perfringens.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC         molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC         ChEBI:CHEBI:71302, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; AB017192; BAA76927.1; -; Genomic_DNA.
DR   EMBL; LRPU01000007; KXA14691.1; -; Genomic_DNA.
DR   EMBL; JAALLZ010000001; NGU29556.1; -; Genomic_DNA.
DR   RefSeq; WP_003458733.1; NZ_VOVJ01000001.1.
DR   PATRIC; fig|1502.174.peg.269; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000070646; Unassembled WGS sequence.
DR   Proteomes; UP000481454; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03522; MoeA_like; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF28; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          172..304
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   337 AA;  37408 MW;  2DBD2277D0BAB340 CRC64;
     MKQIRVEDAV GTILSHDVTQ IIPGKFKGRA FKKGHVIREE DIEKLLSIGK EHVYVWEKEE
     GMLHENEAAE RLKDLVCGEG LSFGEIKEGK IEFLADKDGL LKIDKEKLLE LNMLGEIIVS
     TIHGNFPVKK GDKVGATRVI PLVIDENKII EAENLIKDKI IEVKEIKNKK TFAITTGNEV
     YSGRIKDAFG PVLKEKLKEF NIDLERQVIL PDDKEKIIEE IKRALDEGAE LILCTGGMSV
     DPDDVTPTAI KECGGELITY GSPVLPGAML LLAYYNDVPI IGIPSCAMYS KRTALDLVLP
     RVLADERLTL RDIAEYGHGG LCLNCPVCTF PHCSFGK
//

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