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Database: UniProt
Entry: A0A0M8YQJ3_9ACTN
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ID   A0A0M8YQJ3_9ACTN        Unreviewed;       495 AA.
AC   A0A0M8YQJ3;
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|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=ADL06_00105 {ECO:0000313|EMBL:KOX38491.1};
OS   Streptomyces sp. NRRL F-6491.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX38491.1, ECO:0000313|Proteomes:UP000037743};
RN   [1] {ECO:0000313|EMBL:KOX38491.1, ECO:0000313|Proteomes:UP000037743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX38491.1,
RC   ECO:0000313|Proteomes:UP000037743};
RA   Noorani M.;
RL   Submitted (JUL-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:KOX38491.1}.
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DR   EMBL; LGEE01000001; KOX38491.1; -; Genomic_DNA.
DR   RefSeq; WP_053640066.1; NZ_LGEE01000001.1.
DR   AlphaFoldDB; A0A0M8YQJ3; -.
DR   PATRIC; fig|1519495.3.peg.23; -.
DR   OrthoDB; 3196725at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000037743; 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   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 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   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|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          241..384
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  49984 MW;  8A7B32EE8EFFD80E CRC64;
     MSLKESAPVA PDPADSASGP ADDPSGPADT PSGPVGGAKA GHPHRATSWP EARAVAGRAG
     AAARTGREPL ALPLGRALGQ VLAGPLPALA DLPSFDTSAM DGWAVAGPGP WHVREETAVL
     AGHAPAAALA GGEAVRIATG APVPPGTTAV LRTEHSRTEQ PRTEQPRTEH SRPERPDGPP
     RALLHALREV VAGQDIRPRG QECRSGDELL PAGAAVTPAV LGLAAAAGYD ELLVRPRPRV
     EILVLGDELL AAGLPHEGLI RDALGPMLGP WLAALGADVL ATRRIGDDAE ALYAAVTGSA
     ADLVVTTGGT AAGPVDHVHR VLDKAGATLL VDGVKVRPGH PMLLARLGTD PARPLHVRHL
     VGLPGNPLAA VSGLLTLAAP LLAALARAAS PASPAFPAED GAGSGARTPV PYRVPVRDEV
     HGHPHDTRLV PVVRRGGSAV PLRYNGPAML RGVAAADGLA VVPPGGARPG QELDVLDLPW
     PPTAGAAPAQ GACFT
//
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