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Database: UniProt
Entry: A0A3A9KB85_9THEO
LinkDB: A0A3A9KB85_9THEO
Original site: A0A3A9KB85_9THEO 
ID   A0A3A9KB85_9THEO        Unreviewed;       339 AA.
AC   A0A3A9KB85;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=DXT63_00505 {ECO:0000313|EMBL:RKL64565.1};
OS   Thermoanaerobacteraceae bacterium SP2.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae.
OX   NCBI_TaxID=2292448 {ECO:0000313|EMBL:RKL64565.1, ECO:0000313|Proteomes:UP000271566};
RN   [1] {ECO:0000313|Proteomes:UP000271566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|Proteomes:UP000271566};
RA   Grouzdev D.S., Krutkina M.S., Patutina E.O.;
RL   Submitted (AUG-2018) 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}.
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:RKL64565.1}.
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DR   EMBL; QSNL01000001; RKL64565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9KB85; -.
DR   OrthoDB; 9767940at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000271566; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000271566};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          174..306
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   339 AA;  37240 MW;  4A90DC9DC7EAF90A CRC64;
     MKQVPVEKAV GMILCQDITK IVPGEFKGRA FKKGHVIQKE DVDELLKLGK EHIYVWEPRA
     GEIHEDEAAV RLAGAMAGEN VEYGEPKEGK STLSSRIKGL YEVNSALLRK INSIDMVSVA
     SLPGNFAVEK GRKLAGARVI PLVIEEEKIQ KVENLCRDKG PTFRVIPYKR LKAAVITTGN
     EVFKGRIEDG FGPVILKKLE YFEADYMGQT LCPDDMEEIK RAILRAREKG ADLIILTGGM
     SVDPDDLTPG AIKSTGATVV TYGAPVQPGN MFMMAYLESA AVLGVPGCAM YYSTTILDVV
     LPRIFAGKVL KKQDFIDMGE GSLCSSCESC RYPNCYFCR
//
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