ID A0A0F4RDH2_9RHOB Unreviewed; 699 AA.
AC A0A0F4RDH2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=TW80_16285 {ECO:0000313|EMBL:KJZ18046.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ18046.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ18046.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ18046.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ18046.1}.
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DR EMBL; JXYE01000010; KJZ18046.1; -; Genomic_DNA.
DR RefSeq; WP_045998516.1; NZ_JXYE01000010.1.
DR AlphaFoldDB; A0A0F4RDH2; -.
DR STRING; 579483.TW80_16285; -.
DR PATRIC; fig|579483.3.peg.3347; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000033741; 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; IPR008284; MoCF_biosynth_CS.
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.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000033741};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 477..614
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 699 AA; 74708 MW; 4C56BCB5F8347CDA CRC64;
MPFDSILIVD WSGGNDRGPR PKSDAIWACV AREGNADEPK YFRNRQLAEQ WITSYLQSES
HAGRRVLAGF DFSFGFPVGF GHALTGSDDP LALWDWLEQH VQDGPSANNR FDLAGQINSR
FPGIGPFWGN GLRRDIPHLP RKGSERTCDI FPEKRAAEAS AKGAFPIWQL SGAGAVGSQV
IMGLPMLARL RRALDVSVWP FEKCTSSVVL AEIWPSLVAS AIRDTMPEHA IKDAHQVRCI
ALALSVLPSA DLQRLIDVDY TPEGTILGLN APELLENAIK SSALTPPPLR NDCFAMPQGA
HWTPVDIALD HLRDHLQPVT GTEQCALGEC IGRLLAHDVT ALRSHPPAPN SAVDGYALAG
PAPDGPTNLP LVDGRSAAGQ PYPGHVPAGH AIRILTGANM PAGTDTVILQ EDVNASDSAI
AFHGPLKRGA NARTAGEDMK KGEVILTAGR KITPGDLGML AAAGVGTVTV HKRLRVGILS
TGDELCEPGE TADVGQIFDA NRPMLNATVA GWGYEVIDLG RAADKREPLT KILNSAAQQC
DVIISSGGAS AGDEDHMSAL LQGTGSFALW RIAMKPGRPL ALGMWENTPV IGLPGNPVAA
MVCALIFARP ALQRMAGGRW ERTEGYLLPA AFEKSKKAGR REYLRARVQD GKVQIFPSEG
SGRVSGLSWA TGLVELSDEA QVITPGDQVY FLPFGNFAK
//