UniProt: L8TSZ0

Database: UniProt
Entry: L8TSZ0_9MICC

LinkDB:  L8TSZ0_9MICC 
Original site:  L8TSZ0_9MICC

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   L8TSZ0_9MICC            Unreviewed;       441 AA.
AC   L8TSZ0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=G205_09793 {ECO:0000313|EMBL:ELT44816.1};
OS   Arthrobacter nitrophenolicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT44816.1, ECO:0000313|Proteomes:UP000011189};
RN   [1] {ECO:0000313|Proteomes:UP000011189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX   PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA   Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT   "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT   Arthrobacter sp. Strain SJCon.";
RL   Genome Announc. 1:e0005813-e0005813(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELT44816.1}.
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DR   EMBL; AOFD01000017; ELT44816.1; -; Genomic_DNA.
DR   RefSeq; WP_009357612.1; NZ_AOFD01000017.1.
DR   AlphaFoldDB; L8TSZ0; -.
DR   PATRIC; fig|683150.5.peg.1935; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000011189; Unassembled WGS sequence.
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   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; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE   3: Inferred from homology;
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|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011189};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          203..345
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   441 AA;  44627 MW;  237EB44864120025 CRC64;
     MLITETMAGP RAGHAHPCHA APSWAEARRL AYECAGPLPP VWVPLADADG RVLHRDVTAL
     QDLPHYASSA MDGWAVNGAG PWLLPDPQQP GAHPGLATYG RLAPNHARVI ATGGLVPAGA
     QAILRKESGE VVPGPSGSLL LSVGPGARAD EPRRGQHIRP AGEEALAGDV LLPAGTVLNP
     ARIALAAVAG HDEVLVRARP SVAVVLTGSE VVTQGVPAAG EVRDTFGPQL GTVLSQLGGI
     AGGPARIGDS FSEWLSALDT ATAPDGGKAD VVITTGGTGR SGTDHFRAAI GSLGGRILLD
     GIAMRPGHPA VLAELPDGRF VAGLPGNPLA AMMALLTVGA PLIAALGGRP LPAATDVLSG
     SDMPPDPGRT RLVPCRILSG LAFPVQHTGP GMMRGLAWAE GVMVVPPDGV DSGQPVPVLP
     LPWSPGVDMV PGTNPQGRSI P
//

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