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Database: UniProt
Entry: D4K7W8_9FIRM
LinkDB: D4K7W8_9FIRM
Original site: D4K7W8_9FIRM 
ID   D4K7W8_9FIRM            Unreviewed;       339 AA.
AC   D4K7W8;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=FPR_05330 {ECO:0000313|EMBL:CBL00931.1};
OS   Faecalibacterium prausnitzii SL3/3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL00931.1, ECO:0000313|Proteomes:UP000007059};
RN   [1] {ECO:0000313|EMBL:CBL00931.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL00931.1,
RC   ECO:0000313|Proteomes:UP000007059};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL00931.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL00931.1,
RC   ECO:0000313|Proteomes:UP000007059};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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|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;
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; FP929046; CBL00931.1; -; Genomic_DNA.
DR   RefSeq; WP_005925006.1; NC_021020.1.
DR   AlphaFoldDB; D4K7W8; -.
DR   GeneID; 75068703; -.
DR   KEGG; fpa:FPR_05330; -.
DR   PATRIC; fig|657322.3.peg.212; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_068847_1_0_9; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007059; 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; cd03522; MoeA_like; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF28; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 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   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          173..305
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   339 AA;  36417 MW;  E6B53D5AD1D38098 CRC64;
     MKLIRTVDAA GQVLCHDITQ IIPGEYKDAR FRKGHVIQPE DIPVLLSIGK ENLYVWEKHP
     GILHEDEAAA LLYKAAAGKN IHGTAPKEGK IELIADCDGL LKINRKALMA VNSTPQMMIA
     TIHGDLPVKK GQKLAGTRII PLVIEQEKMD AMQAAAGAEP ILNVLPMQAK KVGIITTGSE
     VFKGRIEDKF TPILQSKLAV YGCEMVFHKV CDDDPAGITA AILEAKAAGC ELIFTTGGMS
     VDPDDRTPLA IKNTGADIIT YGAPVLPGAM FLVSYLDGVP VCGLPGCVMY AKRTIFDLLL
     PRLLADDPIT AEDIARLGEG GLCLNCEVCH WPNCGFGHC
//
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