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Database: UniProt
Entry: B0G4Y4_9FIRM
LinkDB: B0G4Y4_9FIRM
Original site: B0G4Y4_9FIRM 
ID   B0G4Y4_9FIRM            Unreviewed;       404 AA.
AC   B0G4Y4;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=DORFOR_01324 {ECO:0000313|EMBL:EDR47358.1};
OS   Dorea formicigenerans ATCC 27755.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=411461 {ECO:0000313|EMBL:EDR47358.1, ECO:0000313|Proteomes:UP000005359};
RN   [1] {ECO:0000313|EMBL:EDR47358.1, ECO:0000313|Proteomes:UP000005359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27755 {ECO:0000313|EMBL:EDR47358.1,
RC   ECO:0000313|Proteomes:UP000005359};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Dorea formicigenerans(ATCC 27755).";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDR47358.1, ECO:0000313|Proteomes:UP000005359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27755 {ECO:0000313|EMBL:EDR47358.1,
RC   ECO:0000313|Proteomes:UP000005359};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Wang C., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (OCT-2007) 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   -!- 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:EDR47358.1}.
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DR   EMBL; AAXA02000012; EDR47358.1; -; Genomic_DNA.
DR   RefSeq; WP_005332314.1; NZ_AAXA02000012.1.
DR   AlphaFoldDB; B0G4Y4; -.
DR   STRING; 411461.DORFOR_01324; -.
DR   PaxDb; 411461-DORFOR_01324; -.
DR   GeneID; 42421917; -.
DR   eggNOG; COG0303; Bacteria.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000005359; 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; 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   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          182..320
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   404 AA;  42669 MW;  C1A7FB1DE5BD9D36 CRC64;
     MNIQTLKEAS DCLLNLAKPE TQTIEHILLQ DAFERILAED ITAKIPVPSF AKSAYDGYAL
     RQADTAAASP EHPVTLDVTG VIPAGSVPTY PITEGKAARI MTGAPVPEGA DAIIMHERTS
     FTENTVTLTA PVTSANIIPP GEDVAAGTLL VPKGKILTAS DLALIAGQGI AEIGVYKKLS
     IGLISTGSEL LNTGSPLEYG KIYNTNPYLL GGYIQKHHMT ANYLNTVSDD LDSLCRAVLD
     ALKTNDIVIT TGGVSAGDFD YMPEVIRRIG GDLLFHRLKF KPGGAMLGAF KDGKVILGLS
     GNPGAAATGL LCVGFPFMRK LSGRSDITFS QATAYLGVDF KKSSPVTRIL KGHSDFKNGM
     LYFTPLSNQH NGSVSSMSDC DLLAVIPAGS KPLAAGDKLE VYIL
//
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