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Database: UniProt
Entry: U3TPQ9_9ENTR
LinkDB: U3TPQ9_9ENTR
Original site: U3TPQ9_9ENTR 
ID   U3TPQ9_9ENTR            Unreviewed;       413 AA.
AC   U3TPQ9;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=E05_09740 {ECO:0000313|EMBL:BAN95740.1};
OS   Plautia stali symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN95740.1, ECO:0000313|Proteomes:UP000016901};
RN   [1] {ECO:0000313|EMBL:BAN95740.1, ECO:0000313|Proteomes:UP000016901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA   Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT   "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT   lipopolysaccharide.";
RL   Microbiol. Res. 167:48-54(2011).
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP.
CC       {ECO:0000256|ARBA:ARBA00002901, 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; EC=2.10.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001529};
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|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; AP012551; BAN95740.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3TPQ9; -.
DR   KEGG; psts:E05_09740; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_6; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000016901; 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:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 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   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 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; SSF63867; MoeA C-terminal domain-like; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000016901};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          184..321
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   413 AA;  44027 MW;  CB0C642E693CC4F0 CRC64;
     MDMEPFTAGL ISLEDAQQKM LQQLQPISDC LSVALADAAG RITAKPVISP LDVPPFDNSA
     MDGYALRLSD LSADRVLPVT GKAFAGAPFN GDWPAGSVIR IMTGAPIPAG CDTVVMQEQT
     EPRDGGIVIT APVRAGQNIR RIGEDIQAGK QVLDAGVRLG AAELPLLASL GIAEVSVLRK
     LRVAIFSTGD ELQAVGQPLA EGQIYDTNRF TVALMLRKLG CEVIDLGVIA DDPALLRQAF
     SEADRQADVV ISTGGVSVGE ADFTKAMLEE LGAITFWKLA IKPGKPFAFG RLANSWFCGL
     PGNPVSAAVT FYQLVQPLLA TLTGQTTRIM PLRQRARATQ RLKKAPGRLD FQRGILSRGD
     DGVLEVRSTG AQGSHVFSSF ALANCFIVLE RDRGDVEPGE WVDVEAFNSL LEG
//
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