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Database: UniProt
Entry: C8WPK0_EGGLE
LinkDB: C8WPK0_EGGLE
Original site: C8WPK0_EGGLE 
ID   C8WPK0_EGGLE            Unreviewed;       404 AA.
AC   C8WPK0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Elen_1118 {ECO:0000313|EMBL:ACV55088.1};
OS   Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS   KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV55088.1, ECO:0000313|Proteomes:UP000001377};
RN   [1] {ECO:0000313|EMBL:ACV55088.1, ECO:0000313|Proteomes:UP000001377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 /
RC   NCTC 11813 / VPI 0255 / 1899 B {ECO:0000313|Proteomes:UP000001377};
RX   PubMed=21304654; DOI=10.4056/sigs.33592;
RA   Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT   0255).";
RL   Stand. Genomic Sci. 1:174-182(2009).
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|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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DR   EMBL; CP001726; ACV55088.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8WPK0; -.
DR   STRING; 479437.Elen_1118; -.
DR   PaxDb; 479437-Elen_1118; -.
DR   KEGG; ele:Elen_1118; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_2_11; -.
DR   OMA; PVEDTHY; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001377; 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; 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; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF16; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 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:UP000001377};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          175..312
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   404 AA;  42983 MW;  E6431DC56E099FDC CRC64;
     MGEKIMDGFP SREEALADFF AAWEPARSVE YVALDDAVGR VLACDLASTN TLPVVRASSF
     DSIAVKSAAF ANGMPDTSSW KPGVDYVRAD TGDDFPDAFD AVVMIEKAVV REDGSVTFDD
     DVTVEPGSGV RPAGSTLRAG EPLMSAGSII RPTDLAALAM GGATMVPVRV KPRVAFIPTG
     SELVPAGIKP RRGQNVDTNS LMCKHLLIEY GAEPVVFPLV HDDPVELERA FEAALATADV
     VVVNGGSALG EEDFNVKLIE RRGQVVHHYI AAVPGRPLML AVADGKPVVD LPGPTMAAYF
     GSEWCLQAIT ARILGIPLRR RPVVQARADA AKTSIPKMAN IARVHVTRDD EGYAAHFLDF
     KAGELAACMT SNAQRVSPLG EAGWAEGDLL DVELLRGEEF VDQG
//
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