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Database: UniProt
Entry: W0V3C5_9BURK
LinkDB: W0V3C5_9BURK
Original site: W0V3C5_9BURK 
ID   W0V3C5_9BURK            Unreviewed;       416 AA.
AC   W0V3C5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=GJA_1200 {ECO:0000313|EMBL:CDG81853.1};
OS   Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG81853.1, ECO:0000313|Proteomes:UP000027604};
RN   [1] {ECO:0000313|EMBL:CDG81853.1, ECO:0000313|Proteomes:UP000027604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX   PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA   Graupner K., Lackner G., Hertweck C.;
RT   "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT   agaricidamnosum.";
RL   Genome Announc. 3:e00277-e00277(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}.
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DR   EMBL; HG322949; CDG81853.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0V3C5; -.
DR   STRING; 1349767.GJA_1200; -.
DR   KEGG; jag:GJA_1200; -.
DR   PATRIC; fig|1349767.4.peg.2920; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_4; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000027604; Chromosome I.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
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:UP000027604};
KW   Transferase {ECO:0000256|RuleBase:RU365090};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          186..327
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   416 AA;  44071 MW;  6E0B5E5C6CEAD111 CRC64;
     MPGYRADALP VDYAQHIIRT LVTPLRAVEK VALRSALGRV LAADVISPIS VPSHDNSAMD
     GYALRGSDLL AGQTSILSIT GTAYAGHPYP SPVQTGQCIR IMTGAVMPDG CDSVVPQECV
     AEATGSAITL RPGTIKPGDN RRFKGEDLMQ GQAALKQGKV MRPADLGLLA SLGIAEVAVK
     RRLRVAFFST GDELRSIGEA LDAGSVYDSN RYTLFGMLNR LGCDMVDMGI VRDEPAALEE
     ALRCACENAD AVITSGGVST GAADYTRDIL AALGEVAFWK IGMRPGRPMA FGKINSHGHS
     AVLFGLPGNP VAVMVSFYFF ARSALLRMMG ADDTPLPLLR VVSSCAIRKK PGRTEYQRGI
     LSSDADGRHH VRITGSQGSG ILRSMSEANC MVILGERQGD VAAGDSVDVL MFEGLI
//
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