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Database: UniProt
Entry: D7GGM0_PROFC
LinkDB: D7GGM0_PROFC
Original site: D7GGM0_PROFC 
ID   D7GGM0_PROFC            Unreviewed;       476 AA.
AC   D7GGM0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeA2 {ECO:0000313|EMBL:CBL57681.1};
GN   OrderedLocusNames=PFREUD_21790 {ECO:0000313|EMBL:CBL57681.1};
OS   Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS   4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL57681.1, ECO:0000313|Proteomes:UP000000936};
RN   [1] {ECO:0000313|EMBL:CBL57681.1, ECO:0000313|Proteomes:UP000000936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC   {ECO:0000313|Proteomes:UP000000936};
RX   PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA   Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA   Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA   Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA   Lortal S.;
RT   "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT   actinobacterium with food and probiotic applications.";
RL   PLoS ONE 5:E11748-E11748(2010).
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}.
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DR   EMBL; FN806773; CBL57681.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7GGM0; -.
DR   STRING; 754252.PFREUD_21790; -.
DR   KEGG; pfr:PFREUD_21790; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_11; -.
DR   OMA; PRFDNSQ; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000936; 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; 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.
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:UP000000936};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          236..375
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          42..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  48488 MW;  7C09D5AA27876350 CRC64;
     MRANEPLAGH EPLTVEGPLT VNEHRALVDA LAAPLAPLTL PLLGDDPATQ PTGVGSRSSA
     QTGGTAEPRP DKGFPAPGRP ARDCLGAVLA RDMDARLAVP PFTNSAMDGF AVRFADVTPG
     TPLPVAGDIP AGDTSPHELV AGTAWRIMTG APLPAGADTV VKVEHTDHAP GVRRPPASVT
     ITELPRRGAN IRQAGEDVAV GTPVLAAGTL LDATALAAAA SVGYRELAVH PRPRVGIVTT
     GAELVGAGDE LAAGQVPDSN SVLLRGLVRG AGADVAAVVR TDDDPQHLRE ALAGWHDVDL
     VLTAGGISAG AYEVVRQVLE PMGVRFHHVA QQPGGPQGVG TLGVAEGRVP VLCLPGNPVS
     VFVSFHVYAA GLIAVLAGRA TTTAPRTVDV SAGEGWSSPP AKTQFIPLRL ASDGAVHPIH
     RLGSGSHLVA SLPLADGLGV VPAGVGRVAP GDRLQFIDTR AGTPLSARRS SEDFHE
//
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