(data stored in SCRATCH zone)

SWISSPROT: Q5LX88_RUEPO

ID   Q5LX88_RUEPO            Unreviewed;       419 AA.
AC   Q5LX88;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeA {ECO:0000313|EMBL:AAV93628.1};
GN   OrderedLocusNames=SPO0310 {ECO:0000313|EMBL:AAV93628.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93628.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93628.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93628.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O +
CC         Mo-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;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family.
CC       {ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP000031; AAV93628.1; -; Genomic_DNA.
DR   RefSeq; WP_011046071.1; NC_003911.12.
DR   STRING; 246200.SPO0310; -.
DR   EnsemblBacteria; AAV93628; AAV93628; SPO0310.
DR   KEGG; sil:SPO0310; -.
DR   eggNOG; ENOG4105CVM; Bacteria.
DR   eggNOG; COG0303; LUCA.
DR   HOGENOM; HOG000280652; -.
DR   KO; K03750; -.
DR   OMA; PHQASPI; -.
DR   OrthoDB; 651103at2; -.
DR   BioCyc; RPOM246200:G1G48-317-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; ISS:TIGR.
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; ISS:TIGR.
DR   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 2.40.340.10; -; 1.
DR   Gene3D; 3.40.980.10; -; 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   PANTHER; PTHR10192; PTHR10192; 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; SSF53218; SSF53218; 1.
DR   SUPFAM; SSF63867; SSF63867; 1.
DR   SUPFAM; SSF63882; SSF63882; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LX88.
DR   SWISS-2DPAGE; Q5LX88.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
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|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN      197    334       MoCF_biosynth. {ECO:0000259|SMART:
FT                                SM00852}.
SQ   SEQUENCE   419 AA;  43704 MW;  BDE85DEE84C4A0F4 CRC64;
     MTGIEPPPLR NDCFALPAGV EWTPVDTALD MLRDRLGPVT GVEMRLLSQA LGGVLAADAV
     ALRSSPPQAN SAVDGYGFAG AVPEGAHVMP LEEGRAAAGV PFDGVLPAGR ALRVLTGAAL
     PEGVETVILE EDVTLGTGEI AFRGPLKRGA NTRKAGEDVA EGAVVLPAGR RLTPADLALL
     ASVGLGVVPL RRQLRVAVLS TGDELVEPGE TAGPGQIFDA NRPMLLSLIH RLGHAPVDLG
     RVPDDRTTLR ATFDRAAAEA DVILTSGGAS AGDEDHVSAL LRAAGAMQQW RIALKPGRPL
     ALGLWQGKPV FGLPGNPVAA LVCSLVFARP AMAVLAGESW SVPQGYDLPA GFEKRKKPGR
     REYLRARVRD GRVEVFASEG SGRVSGLSWA EGLVEIGDDA CHIRPGDPVR FIPYGSFGL
//

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