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Database: UniProt
Entry: A0A0F0CC34_9CLOT
LinkDB: A0A0F0CC34_9CLOT
Original site: A0A0F0CC34_9CLOT 
ID   A0A0F0CC34_9CLOT        Unreviewed;       352 AA.
AC   A0A0F0CC34;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=cinA_2 {ECO:0000313|EMBL:KJJ69773.1};
GN   ORFNames=CLFS41_38280 {ECO:0000313|EMBL:KJJ69773.1};
OS   Clostridium sp. FS41.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ69773.1, ECO:0000313|Proteomes:UP000033604};
RN   [1] {ECO:0000313|EMBL:KJJ69773.1, ECO:0000313|Proteomes:UP000033604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FS41 {ECO:0000313|EMBL:KJJ69773.1,
RC   ECO:0000313|Proteomes:UP000033604};
RA   Poehlein A., Daniel R.;
RT   "Genome sequencing of Clostridium sp. FS41.";
RL   Submitted (FEB-2015) 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:KJJ69773.1}.
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DR   EMBL; JYHN01000064; KJJ69773.1; -; Genomic_DNA.
DR   RefSeq; WP_045093159.1; NZ_JYHN01000064.1.
DR   AlphaFoldDB; A0A0F0CC34; -.
DR   PATRIC; fig|1609975.3.peg.4094; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000033604; 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:UP000033604};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          177..317
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   352 AA;  38181 MW;  D44E59E8265052B5 CRC64;
     MKLIKTVDAE GTVLCHDITQ IIKGVTKDAV FRKGHVVTKE DIPVLLSVGK DQLYVWEKEE
     GMLHENEAAE VLCAMCRGDH MDRSQAKEGK IELTASCDGL LKVDNRGLKA VNGFGQMMIA
     TRHGNFAVKK GDKLAGTRII PLIIEEEKME AARTAASRAT GGKPILELMP FVHKKVGIVT
     TGNEVFHGRI KDTFTPVIEE KISEFDTEVI DHVIWDDDDT KVTAGILDMI QKGADVVICT
     GGMSVDPDDK TPLAIKNTGA RIVSYGAPVL PGAMFLLAYY EVTADEDRRT VAIMGLPGCV
     MYAKRTIFDL VLPRVMADDE VTAEDLAALG QGGLCLNCPV CTFPNCGFGK GL
//
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