(data stored in SCRATCH zone)

SWISSPROT: A4F745_SACEN

ID   A4F745_SACEN            Unreviewed;       396 AA.
AC   A4F745;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moaA3 {ECO:0000313|EMBL:CAL99869.1};
GN   OrderedLocusNames=SACE_0523 {ECO:0000313|EMBL:CAL99869.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99869.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99869.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAL99869.1; -; Genomic_DNA.
DR   STRING; 405948.SACE_0523; -.
DR   EnsemblBacteria; CAL99869; CAL99869; SACE_0523.
DR   KEGG; sen:SACE_0523; -.
DR   eggNOG; ENOG4105CVM; Bacteria.
DR   eggNOG; COG0303; LUCA.
DR   HOGENOM; HOG000280651; -.
DR   KO; K03750; -.
DR   OMA; MTGAMVP; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000006728; Chromosome.
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   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; 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.
PE   3: Inferred from homology;
DR   PRODOM; A4F745.
DR   SWISS-2DPAGE; A4F745.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
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:UP000006728};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN      176    313       MoCF_biosynth. {ECO:0000259|SMART:
FT                                SM00852}.
SQ   SEQUENCE   396 AA;  41175 MW;  A4C80DAE55AB213D CRC64;
     MPEYQQRIAE LLAPTPVEPR ALEDCLGLAL ATDLTASIPL PPFDNSAMDG YAVRSVDLAG
     ADEQNPVVLP VPEDVPAGRV QNPPLQPGTA HRIMTGAQVP PGADAVIPVE RTDGGVTEVR
     AYAQVQPGAH IRRAGEDVAS GATVLSAGTS LTPPQLGVAA AVGAERLPVH RPVRVLILST
     GSELVAPGTP LEPGQIYESN GLMLASAVRA ADADARLLRF VPDDVHAFHA VLSPHLDSTD
     LIITSGGVSA GAYEVVKDAL SGNGVEFTKV AMQPGMPQGC GRYRGGPAVV ALPGNPVSAM
     VSFEVFVRPV LRAAAGHSRT RREVRQATLT EELVAPAGKR QYRRAVFDPA TGEVRTQGGT
     GSHLLTAMAA ANCLLEIPEE TTTLPEGSTV DVLLVD
//

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