(data stored in SCRATCH zone)

SWISSPROT: B6HG25_PENRW

ID   B6HG25_PENRW            Unreviewed;       402 AA.
AC   B6HG25;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
DE   Includes:
DE     RecName: Full=Molybdopterin adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE              Short=MPT adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE              EC=2.7.7.75 {ECO:0000256|RuleBase:RU365090};
DE     AltName: Full=Domain G {ECO:0000256|RuleBase:RU365090};
DE   Includes:
DE     RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE              Short=MPT Mo-transferase {ECO:0000256|RuleBase:RU365090};
DE              EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
DE     AltName: Full=Domain E {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=Pc20g03380 {ECO:0000313|EMBL:CAP85667.1}, PCH_Pc20g03380
GN   {ECO:0000313|EMBL:CAP85667.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85667.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85667.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Catalyzes two steps in the biosynthesis of the
CC       molybdenum cofactor. In the first step, molybdopterin is
CC       adenylated. Subsequently, molybdate is inserted into adenylated
CC       molybdopterin and AMP is released.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC         diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC         ChEBI:CHEBI:62727; Evidence={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; AM920435; CAP85667.1; -; Genomic_DNA.
DR   RefSeq; XP_002562889.1; XM_002562843.1.
DR   STRING; 1108849.XP_002562889.1; -.
DR   EnsemblFungi; CAP85667; CAP85667; PCH_Pc20g03380.
DR   GeneID; 8317566; -.
DR   KEGG; pcs:Pc20g03380; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   eggNOG; COG0303; LUCA.
DR   HOGENOM; HOG000280651; -.
DR   KO; K03750; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 666263at2759; -.
DR   BioCyc; PCHR:PC20G03380-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; 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:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; 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; 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; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
DR   SUPFAM; SSF63882; SSF63882; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HG25.
DR   SWISS-2DPAGE; B6HG25.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
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:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN      203    352       MoCF_biosynth. {ECO:0000259|SMART:
FT                                SM00852}.
SQ   SEQUENCE   402 AA;  43964 MW;  64080A395D20B35A CRC64;
     MALSYHEALR MVEAEAQRRA RTLQLNMEKL PLNLSLNRVT GCEMRSPIST PQYDTSAMDG
     YAVDSGATRD ASPDNPILFH VEGLVAAGNE PFPLFNTASQ SCSCVEIMTG GRFPTAVEPD
     NVRLDCCVKF EDTKKVPGPY TGDEYIEITK PARYRQNRRS AGEDFQRHHV IMPAGTIIRP
     HHIMALASVG ITEIAVLPKL RVGLYSTGAE LLASHGNQPV TGRVEDANGP YIAAALADSG
     VDVEFLGILD DDVEMMMHTL RSNLEKKDCD LIISTGAVST GRFDLIPSAL QRLGAHIVFH
     KIGIRPGHPV MFATVPNISP ERSDEIPFFG LPGNPVASAA CLRFLVMHYL KCLQSQLPET
     PLTARMSCPN DAKTARQSAH VITSFPSEKD VFRPGVFHSL EK
//

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