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Database: UniProt
Entry: F7QK44_9BRAD
LinkDB: F7QK44_9BRAD
Original site: F7QK44_9BRAD 
ID   F7QK44_9BRAD            Unreviewed;       418 AA.
AC   F7QK44;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=CSIRO_1939 {ECO:0000313|EMBL:EGP08213.1};
OS   Bradyrhizobiaceae bacterium SG-6C.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP08213.1, ECO:0000313|Proteomes:UP000003148};
RN   [1] {ECO:0000313|EMBL:EGP08213.1, ECO:0000313|Proteomes:UP000003148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-6C {ECO:0000313|EMBL:EGP08213.1,
RC   ECO:0000313|Proteomes:UP000003148};
RX   PubMed=21742875; DOI=10.1128/JB.05647-11;
RA   Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA   Pandey G.;
RT   "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT   Bradyrhizobiaceae Strain SG-6C.";
RL   J. Bacteriol. 193:5057-5057(2011).
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:EGP08213.1}.
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DR   EMBL; AFOF01000023; EGP08213.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7QK44; -.
DR   STRING; 709797.CSIRO_1939; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_5; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000003148; 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   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.
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          192..329
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   418 AA;  43737 MW;  DB1E85F7B59F9A50 CRC64;
     MAQLSDDCFA FGGPMMSVDD AVATIAARVN AVAECESVDL ADADGRVLSS DVRAPMALPP
     FTNSAVDGYA VRSADLPRDK ERAFSVSGRI QAGSPSPGAI AADHAIRIFT GAPMPEGADT
     VFMQEDVRID GTGNVVLPPG LKAGANVRPA GEDIPQGHLA LPAGRQLRPQ DIALLAALGI
     TRAEVKRQLR IAVFSTGNEV VSPGAPRSPV QLFDSNRFML TAMLKRLGCE VSDLGILRDD
     RASLASALQD AAARHDLILT SGGVSTGEED HVKAAVESVG TLVLWRMAIK PGRPVAMGII
     GGTPFIGLPG NPVASFVTFT YVVRPVVMAL AGAAQRRLAL TPVCAGFSYK KKAGRREYVR
     ASLRSNGNGT LEAVKFPREG AGLLSSLVDT DGLVELGEEI VKVEPGQTVG FLDYTALL
//
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