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Database: UniProt
Entry: A0A0C2W787_9BACL
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ID   A0A0C2W787_9BACL        Unreviewed;       423 AA.
AC   A0A0C2W787;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=KP78_02680 {ECO:0000313|EMBL:KIL51898.1};
OS   Jeotgalibacillus soli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX   NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL51898.1, ECO:0000313|Proteomes:UP000031938};
RN   [1] {ECO:0000313|EMBL:KIL51898.1, ECO:0000313|Proteomes:UP000031938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P9 {ECO:0000313|EMBL:KIL51898.1,
RC   ECO:0000313|Proteomes:UP000031938};
RA   Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT   "Genome sequencing of Jeotgalibacillus soli.";
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:KIL51898.1}.
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DR   EMBL; JXRP01000006; KIL51898.1; -; Genomic_DNA.
DR   RefSeq; WP_041085649.1; NZ_JXRP01000006.1.
DR   AlphaFoldDB; A0A0C2W787; -.
DR   STRING; 889306.KP78_02680; -.
DR   PATRIC; fig|889306.3.peg.272; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000031938; 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:UP000031938};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KIL51898.1}.
FT   DOMAIN          189..327
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   423 AA;  45838 MW;  BD2866E34D7A7859 CRC64;
     MAERRKPIPI GEAVSRVMSF AAPGTKEKIH VNDAYGRTLG EDIIAVHPVP PFDRSPYDGF
     AIRAEDSAQA SRGNPITFNV IETVGAGSVA TKEVKPYEAV RIMTGAQLPD QCDAVVMLEL
     TTESTEDGVS TMTIKRPFQP GDNVSFKGED TEQGAVLVKK GELINPGVVA VLATFGYEYV
     YVAKKPLIGV FATGSELLDV HEELQPGKIR NSNAHMIAAQ IERAGAEVKY FGKLEDDLER
     CYQSINEAAA EVDMLITTGG VSVGDFDYLP AVYEKLGAEV LFNKIAMRPG SVTTVAHWEG
     KYLFGLSGNP SACYVGFEVL VRPVVKTLLF SAKPHLPKVE ARLSEDFLKP NPFTRFVRSK
     LNITTEGLKA APSGFNKSNA VTSLATSDAL VVLPGGTRGY KDGDLVDVLL LESYEGSEWP
     WEK
//
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