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Database: UniProt
Entry: A0A0D6Z7M2_9BACI
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ID   A0A0D6Z7M2_9BACI        Unreviewed;       421 AA.
AC   A0A0D6Z7M2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN   ORFNames=UB32_15965 {ECO:0000313|EMBL:KIY21031.1};
OS   Mesobacillus subterraneus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY21031.1, ECO:0000313|Proteomes:UP000032512};
RN   [1] {ECO:0000313|EMBL:KIY21031.1, ECO:0000313|Proteomes:UP000032512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MITOT1 {ECO:0000313|EMBL:KIY21031.1,
RC   ECO:0000313|Proteomes:UP000032512};
RA   Peet K.C., Thompson J.R.;
RT   "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT   subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL   Submitted (JAN-2015) 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|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}.
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:KIY21031.1}.
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DR   EMBL; JXIQ01000134; KIY21031.1; -; Genomic_DNA.
DR   RefSeq; WP_044395509.1; NZ_JXIQ01000134.1.
DR   AlphaFoldDB; A0A0D6Z7M2; -.
DR   PATRIC; fig|285983.3.peg.2268; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000032512; 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; 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; 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.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032512};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KIY21031.1}.
FT   DOMAIN          189..327
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   421 AA;  46151 MW;  645A5BDC2566B47A CRC64;
     MLERRNPIPI GEAVKRVMEH KQSGSTEYVS INESYGRYLS EDLKATSDVP HFDRAPYDGY
     AIRSVDSEEA SQNQPVEFEV VDHIGAGMLT DKELGPFQAV RIMTGAQMPV GADAVVMLEL
     SKEVDRDGKK YMETKRKHHK GDNVSYRGED AQEGEVLVKK GTFINPGIQA MLATFGYAHV
     PVAKKPVIGL YATGTELLDV HEPLEPGKIR NSNSYMISAQ ILRAGAEVKY FGQLPDDFDT
     CFDAVSKAME EVDLFITTGG VSVGDYDYLP EIYAKLGAEV LFNKVAMRPG SVTTVAQLDG
     KLLFGLSGNP SACYVGFELF ARPIIRTMLF TDKPHLRKEK AILDANFPKA NPFTRFVRSA
     LAIENGKLSV TPSGLDKSNI IMSLAGANSL MILPGGSRGF ETGTEVEVLL LEDHAGSDWP
     W
//
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