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Database: UniProt
Entry: A0A0M4FPD5_9BACI
LinkDB: A0A0M4FPD5_9BACI
Original site: A0A0M4FPD5_9BACI 
ID   A0A0M4FPD5_9BACI        Unreviewed;       429 AA.
AC   A0A0M4FPD5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-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=AM592_04335 {ECO:0000313|EMBL:ALC80898.1};
OS   Bacillus gobiensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC80898.1, ECO:0000313|Proteomes:UP000067625};
RN   [1] {ECO:0000313|Proteomes:UP000067625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALC80898.1, ECO:0000313|Proteomes:UP000067625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC80898.1,
RC   ECO:0000313|Proteomes:UP000067625};
RX   PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA   Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT   "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL   Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
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; CP012600; ALC80898.1; -; Genomic_DNA.
DR   RefSeq; WP_053602647.1; NZ_CP012600.1.
DR   AlphaFoldDB; A0A0M4FPD5; -.
DR   STRING; 1441095.AM592_04335; -.
DR   PATRIC; fig|1441095.3.peg.952; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000067625; 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:UP000067625};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:ALC80898.1}.
FT   DOMAIN          189..327
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   429 AA;  46600 MW;  0C6594D732CC33C1 CRC64;
     MVVTRKPIPV GQAVERVMNV SKKGETEWVP LEQSLHRHLA ETIIADHDIP AFDRSPYDGF
     AIRAEDSIHA SKENPLTFHV VDHIGAGSVS EKKIGRYEAV RIMTGAKIPD GADTIVMLEL
     ANVISENGNE RIELKRPFYS GDNISKKGED TAEGERLIPA GTVIDSGVIA LLATFGYAAV
     NVVKKPKIGI IATGTELLDI SDPLEPGKIR NSNASMIYAQ IQEAGGEPLN LGKMADHFDS
     CYEAVKKAID KVDFLITTGG VSVGDFDFLP AIYERLGANV LFNKVGMRPG SVTTVAEYKG
     KLLFGLSGNP SACFVGFELF VKPVIKNWLL SDKPYSLYHQ ATLSKDFLKA NPFTRFVRSS
     VSSENGKLFV DPVGLDKSSS VISLASTNAL LVLPGGTKGY QKGDQVIVLM IKEERGCEWP
     WDIILSSSK
//
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