GenomeNet

Database: UniProt
Entry: M5DVU6_9GAMM
LinkDB: M5DVU6_9GAMM
Original site: M5DVU6_9GAMM 
ID   M5DVU6_9GAMM            Unreviewed;       415 AA.
AC   M5DVU6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=TOL_3131 {ECO:0000313|EMBL:CCU73527.1};
OS   Thalassolituus oleivorans MIL-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Thalassolituus.
OX   NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU73527.1, ECO:0000313|Proteomes:UP000011866};
RN   [1] {ECO:0000313|EMBL:CCU73527.1, ECO:0000313|Proteomes:UP000011866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIL-1 {ECO:0000313|EMBL:CCU73527.1,
RC   ECO:0000313|Proteomes:UP000011866};
RX   PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA   Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA   Yakimov M.M., Teeling H., Golyshina O.V.;
RT   "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL   Genome Announc. 1:1-3(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HF680312; CCU73527.1; -; Genomic_DNA.
DR   RefSeq; WP_015488235.1; NC_020888.1.
DR   AlphaFoldDB; M5DVU6; -.
DR   STRING; 187493.CN03_15670; -.
DR   KEGG; tol:TOL_3131; -.
DR   PATRIC; fig|1298593.3.peg.3027; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_6; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000011866; 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   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   NCBIfam; TIGR00177; molyb_syn; 1.
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; PS01079; MOCF_BIOSYNTHESIS_2; 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:UP000011866};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          188..325
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   415 AA;  44257 MW;  6A0E93EE55D0829C CRC64;
     MKQTQDHCNK PGLTPIEDAL QYLLETISVL TETEAIPLSE AHGRVLAADV ISPINVPPHD
     NSAMDGYALH HLSDVTQPVE IVATVLAGHP YIEALAQGKT VRIMTGAPIP QGASAVVMQE
     DAQRTGDSVV FAAGVALNEG MNIRRAGEDI RKLVTILPAG RRLRVADCGL LASIGIATVT
     VVRRLRVALV TTGDELQPPG TPLLPGNIYE SNSFTLTPML QRLGVELITM PAVADDLMAL
     RAAFTQADEQ ADVVITSGGV SVGEADLTRT VLEELGQLNF WKLAIKPGKP FAFGRLPSSW
     FIGLPGNPVS ALVTLHQLAL PLLRTMAGET LAKPLRFNAT TLTDLRKSPG RTDYQRAIAK
     PNEEGQLVVA TTGAQGSGVL SSMSQANCYI VLEKERGRVT AGETVTVEVF DEWLA
//
DBGET integrated database retrieval system