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Database: UniProt
Entry: Q5L1X3_GEOKA
LinkDB: Q5L1X3_GEOKA
Original site: Q5L1X3_GEOKA 
ID   Q5L1X3_GEOKA            Unreviewed;       419 AA.
AC   Q5L1X3;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 90.
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   Name=moeA {ECO:0000313|EMBL:BAD75057.1};
GN   OrderedLocusNames=GK0772 {ECO:0000313|EMBL:BAD75057.1};
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD75057.1, ECO:0000313|Proteomes:UP000001172};
RN   [1] {ECO:0000313|EMBL:BAD75057.1, ECO:0000313|Proteomes:UP000001172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426 {ECO:0000313|EMBL:BAD75057.1,
RC   ECO:0000313|Proteomes:UP000001172};
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD75057.1; -; Genomic_DNA.
DR   RefSeq; WP_011230274.1; NC_006510.1.
DR   AlphaFoldDB; Q5L1X3; -.
DR   STRING; 235909.GK0772; -.
DR   KEGG; gka:GK0772; -.
DR   PATRIC; fig|235909.7.peg.856; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_9; -.
DR   OMA; MTGAMVP; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001172; 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|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001172};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          189..327
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   419 AA;  45619 MW;  ADFDDA33ECA681B0 CRC64;
     MVERRTPIPV AEAIERVMRY AGVGEEETVP LRQSYGRYLA EDLRADHDVP PFDRSPYDGF
     AIRAADSEGA GLDHPVEFEV IETIGAGQVA KQPVGPFQAV RLMTGAQIPE GCDAVVMLEL
     AKQYERDGKT YMSIKRSFRP GDNISFQGED AKKGQPLIEK GTRINPGVAA LLATFGYAEV
     KVAKRPRIGI FATGSELLDV SEPLVPGKIR NSNAYMIEAQ VLKSGAEPIY FGQLADDLEA
     CFHAVREALD QVDMLITTGG VSVGDFDYLP AIYERLGANV LFNKIAMRPG SVTTVAEWNG
     KLLFGLSGNP SACYVGYELF VRPVVRTRLF STKPHLKKAK ATLGADFPKP NPFTRFVRSR
     VEAVDGRLIV KPVGMDKSNI VTSLAFANAL MVLPGGTRGF AVGDEVDVWL LDDDEGSSE
//
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