UniProt: A0A0L6JRT9

Database: UniProt
Entry: A0A0L6JRT9_9FIRM

LinkDB:  A0A0L6JRT9_9FIRM 
Original site:  A0A0L6JRT9_9FIRM

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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)   
All databases (19)   

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ID   A0A0L6JRT9_9FIRM        Unreviewed;       407 AA.
AC   A0A0L6JRT9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN   ORFNames=Bccel_3684 {ECO:0000313|EMBL:KNY28410.1};
OS   Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Pseudobacteroides.
OX   NCBI_TaxID=398512 {ECO:0000313|EMBL:KNY28410.1, ECO:0000313|Proteomes:UP000036923};
RN   [1] {ECO:0000313|Proteomes:UP000036923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2933 {ECO:0000313|Proteomes:UP000036923};
RA   Dassa B., Utturkar S.M., Klingeman D.M., Hurt R.A., Keller M., Xu J.,
RA   Reddy Y.H.K., Borovok I., Grinberg I.R., Lamed R., Zhivin O., Bayer E.A.,
RA   Brown S.D.;
RT   "Near-Complete Genome Sequence of the Cellulolytic Bacterium Bacteroides
RT   (Pseudobacteroides) cellulosolvens ATCC 35603.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC       {ECO:0000256|ARBA:ARBA00003487}.
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:KNY28410.1}.
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DR   EMBL; LGTC01000001; KNY28410.1; -; Genomic_DNA.
DR   RefSeq; WP_036938743.1; NZ_LGTC01000001.1.
DR   AlphaFoldDB; A0A0L6JRT9; -.
DR   STRING; 398512.Bccel_3684; -.
DR   PATRIC; fig|398512.5.peg.3860; -.
DR   eggNOG; COG0303; Bacteria.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000036923; 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   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:UP000036923};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          185..324
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   407 AA;  43827 MW;  C41F75D3401F82D4 CRC64;
     MFSVKSVNEV FEIIEKNFKG YQLECETIEI NYAVGRICGE SVVSAEDIPG FNRSSVDGYA
     VMASDTFGSS DSCPAQLKLA GEIKMGEEAD VYLLKGEAIY VPTGGQIPRN ADAVVMIEYT
     DNFDDGFIYI NKSVAPGNNL VFKGDDIKSG NAVIKPGTRI RPQDIGALAA LGVTHISVKR
     RVKVGIVSTG DEIVDIKNKP EGSEVRDINS YFLHAGIVEY GCEPVMYGIC EDDFHKIKCK
     VDLALKECDI ILISGGSSVG LKDQTMKVIN SLGLPGVLVH GIAVKPGKPT ILGKIDHKAV
     VGLPGHPAAA YIVFKVFVLK LIDAFNDSKS IGSSVIRAKM AHNYPSNNGR EEFVTVRLEA
     SHDGFLAHPL FGKSGLISLV SQADGFLRIG RECEGIEEGK DVEVILL
//

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