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Database: UniProt
Entry: A0A0B4RBK7_9BACL
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ID   A0A0B4RBK7_9BACL        Unreviewed;       414 AA.
AC   A0A0B4RBK7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=Plano_1559 {ECO:0000313|EMBL:AIY05524.1};
OS   Planococcus sp. PAMC 21323.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY05524.1, ECO:0000313|Proteomes:UP000031496};
RN   [1] {ECO:0000313|EMBL:AIY05524.1, ECO:0000313|Proteomes:UP000031496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY05524.1,
RC   ECO:0000313|Proteomes:UP000031496};
RA   Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT   "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT   Antarctica.";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009129; AIY05524.1; -; Genomic_DNA.
DR   RefSeq; WP_038703948.1; NZ_CP009129.1.
DR   AlphaFoldDB; A0A0B4RBK7; -.
DR   STRING; 1526927.Plano_1559; -.
DR   KEGG; pln:Plano_1559; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_9; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000031496; 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; 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:UP000031496};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          185..323
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   414 AA;  44546 MW;  81D1B3B36463A354 CRC64;
     MVEKRIPLAV VEAVKKVVEN AFPIGIETVD LEESYGCILA EPIVASSDVP PFDRSPYDGY
     AIRSIDSRGA TGDTRIAFKV IDHIGAGEVS SKKLQAFEAI RIMTGAQLPE GADAIVMFEQ
     TKEIDDGITI RKSFMPLENV SLQGEDLRKE EVVIDSGSFI NPGTIALLAT FGYSKVRVAK
     QPIVGILSTG TELLAVEDDL VPGKIRNSNG PMIVAQLKRM GLGCKMYGMS VDNLEESYRI
     VKKAAEENDC LITTGGVSVG DFDFLPAIYE KLGAQVLFNK VAMRPGSVTT IALINNRLLF
     GLSGNPSACF TGFELFTRPA LLKMMGAQKI YMPHTTAVLG EDFTKANPFT RFVRAIYDGQ
     TASPAGFNKS NAVSSIARGN ALIVLPGGSR GYQTGDAVDV LLLGSEEGSD RWKV
//
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