MOEA_SALTY
ID MOEA_SALTY Reviewed; 413 AA.
AC Q56066;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Molybdopterin molybdenumtransferase;
DE Short=MPT Mo-transferase;
DE EC=2.10.1.1;
GN Name=moeA; OrderedLocusNames=STM0846;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Wong K.-K., Kwan H.S.;
RT "Cloning and sequencing of moeAB operon from Salmonella typhimurium LT2.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC molybdopterin with the concomitant release of AMP. {ECO:0000250}.
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; EC=2.10.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000305}.
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DR EMBL; U53178; AAA96529.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19782.1; -; Genomic_DNA.
DR RefSeq; NP_459823.3; NC_003197.2.
DR RefSeq; WP_014343820.1; NC_003197.2.
DR AlphaFoldDB; Q56066; -.
DR SMR; Q56066; -.
DR STRING; 99287.STM0846; -.
DR PaxDb; Q56066; -.
DR PRIDE; Q56066; -.
DR EnsemblBacteria; AAL19782; AAL19782; STM0846.
DR GeneID; 1252365; -.
DR KEGG; stm:STM0846; -.
DR HOGENOM; CLU_010186_7_0_6; -.
DR OMA; MTGAMVP; -.
DR PhylomeDB; Q56066; -.
DR BioCyc; SENT99287:STM0846-MON; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR CDD; cd00887; MoeA; 1.
DR Gene3D; 2.40.340.10; -; 1.
DR Gene3D; 3.40.980.10; -; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192; PTHR10192; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; SSF53218; 1.
DR SUPFAM; SSF63867; SSF63867; 1.
DR SUPFAM; SSF63882; SSF63882; 1.
DR TIGRFAMs; TIGR00177; molyb_syn; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..413
FT /note="Molybdopterin molybdenumtransferase"
FT /id="PRO_0000170993"
FT CONFLICT 126
FT /note="V -> E (in Ref. 1; AAA96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="G -> D (in Ref. 1; AAA96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="C -> WR (in Ref. 1; AAA96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="AA -> G (in Ref. 1; AAA96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..254
FT /note="GG -> R (in Ref. 1; AAA96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="V -> E (in Ref. 1; AAA96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="V -> D (in Ref. 1; AAA96529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 44343 MW; 3D2F9F8D52FC5B9F CRC64;
MFMEFSAGLM PLETALTQML SRITPLTAVE TLPLVNCFGR ILATDIVSPL DVPGFDNSAM
DGYAVRVADL SADKPLPVAG KAFAGQPYQG EWPAGTCIRI MTGAPVPAGC EAVVMQEQTE
QTDDGVRFTA DVRCGQNIRR RGEDIRQDAV VFPAGTRLTT AELPVLASLG IADAQVVRKV
RVALFSTGDE LQLPGQPLEA GQIYDTNRLT IHLMLQQLGC EVINLGIIPD DPGKLRAAFI
DADSQADVVI SSGGVSVGEA DYTKTILEEL GEIAFWKLAI KPGKPFAFGK LSNSWFCGLP
GNPVSAALTF YQLVQPLLAK LGGNTASAVP PRQRVRTASR LKKTPGRLDF QRGILQRSAN
GELEVTTTGH QGSHIFSSFS LGNCFIVLER ERGNVEPGEW VEVEPFNALF GGL
