(data stored in SCRATCH zone)

SWISSPROT: Q47T05_THEFY

ID   Q47T05_THEFY            Unreviewed;       410 AA.
AC   Q47T05;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Tfu_0374 {ECO:0000313|EMBL:AAZ54412.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54412.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(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; CP000088; AAZ54412.1; -; Genomic_DNA.
DR   RefSeq; WP_011290821.1; NC_007333.1.
DR   STRING; 269800.Tfu_0374; -.
DR   EnsemblBacteria; AAZ54412; AAZ54412; Tfu_0374.
DR   KEGG; tfu:Tfu_0374; -.
DR   eggNOG; ENOG4105CVM; Bacteria.
DR   eggNOG; COG0303; LUCA.
DR   HOGENOM; HOG000280651; -.
DR   KO; K03750; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 651103at2; -.
DR   BioCyc; TFUS269800:G1G4Q-377-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000434; 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; Q47T05.
DR   SWISS-2DPAGE; Q47T05.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
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:UP000000434};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN      179    318       MoCF_biosynth. {ECO:0000259|SMART:
FT                                SM00852}.
SQ   SEQUENCE   410 AA;  42878 MW;  6AE4900D4CDC1049 CRC64;
     MKSVEQHVSD ILAVVSRPDP IELDLLRAHG AVLAEPVTAE LSLPPFDNSA MDGYAVCAAD
     VATATPQTPV TLPVIADIPA GDVFASAIPV GCCARIMTGA ALPKGADAVV PVEWTDAGVA
     EVAVHRAVEA GHAVRQAGSD VKEGTEVLPA GVRIGPAEVA VLAAVGRRSV SVYPRPRVVV
     LGTGEELVEP GRPLSPGQIW ESNSFMLTAA AIEAGCEGYR YGFVGDDPDQ VFEAIQDALV
     RADIVITSGG VSMGAHDAVK EVLSRLGTVQ FDKVAVQPGM PQGYGTVGES SIPIIALPGN
     PVSSYVSFYL FVLPALRKMS GLPQEQLPSV RARLLAPITS SPRGRRSYLR AVLDYDIESE
     EVAYTALPVA QQGSHQLSAL AKTNALVVVP EQVTELPEGS VVEAIQLPHR
//

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