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Database: UniProt
Entry: A0A0F4RDH2_9RHOB
LinkDB: A0A0F4RDH2_9RHOB
Original site: A0A0F4RDH2_9RHOB 
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
//
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