ID K0NTE3_DESTT Unreviewed; 338 AA.
AC K0NTE3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN OrderedLocusNames=TOL2_C41710 {ECO:0000313|EMBL:CCK82327.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK82327.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK82327.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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; FO203503; CCK82327.1; -; Genomic_DNA.
DR RefSeq; WP_014959507.1; NC_018645.1.
DR AlphaFoldDB; K0NTE3; -.
DR STRING; 651182.TOL2_C41710; -.
DR KEGG; dto:TOL2_C41710; -.
DR PATRIC; fig|651182.5.peg.4907; -.
DR HOGENOM; CLU_068847_1_0_7; -.
DR OrthoDB; 9767940at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000007347; Chromosome.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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 Nucleotidyltransferase {ECO:0000313|EMBL:CCK82327.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:CCK82327.1}.
FT DOMAIN 173..305
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 338 AA; 36330 MW; 88869BE9F51257C3 CRC64;
MQSVTVEESI GMVLCHDITR IVPDLFKGRA FKKGHVIREE DIPRLLELGK EHIYVQSFDG
SVHENDAAQR IARAAAGNGL TLSEPYEGKV SFTAKTDGLL KVNIDAVNRM NDIQDIMFAT
LQSNHQVAAG TSLAGTRIIP LSTDEAKVEA VEQICRAAFP VIEIKPFARL RVGMVTTGNE
VYKGLIKDGF GPVVRKKFDA LGSVVSRQIF VPDDIEMTVA AVHELLDEGA EMIAVTGGMS
VDPDDLTPAS IKAAGGRIIS YGAPVLPGAM FLLAYIGDVP VVGLPGCVMY HKASIFDLIV
PRLLAGETVE RSDITAMGHG GFCSSCEHCR YPLCGFGK
//
