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Database: UniProt
Entry: A0A0D8IEL2_9CLOT
LinkDB: A0A0D8IEL2_9CLOT
Original site: A0A0D8IEL2_9CLOT 
ID   A0A0D8IEL2_9CLOT        Unreviewed;       403 AA.
AC   A0A0D8IEL2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=moeA3 {ECO:0000313|EMBL:AKL94360.1};
GN   ORFNames=CACET_c08510 {ECO:0000313|EMBL:AKL94360.1};
OS   Clostridium aceticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL94360.1, ECO:0000313|Proteomes:UP000035704};
RN   [1] {ECO:0000313|EMBL:AKL94360.1, ECO:0000313|Proteomes:UP000035704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL94360.1,
RC   ECO:0000313|Proteomes:UP000035704};
RA   Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT   "Genome sequence of Clostridium aceticum DSM 1496.";
RL   Submitted (OCT-2014) 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   -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC       {ECO:0000256|ARBA:ARBA00003487}.
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; CP009687; AKL94360.1; -; Genomic_DNA.
DR   RefSeq; WP_044823491.1; NZ_JYHU01000003.1.
DR   AlphaFoldDB; A0A0D8IEL2; -.
DR   STRING; 84022.CACET_c08510; -.
DR   KEGG; cace:CACET_c08510; -.
DR   PATRIC; fig|84022.5.peg.2474; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000035704; 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; IPR008284; MoCF_biosynth_CS.
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.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 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:UP000035704};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AKL94360.1}.
FT   DOMAIN          179..317
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   403 AA;  44582 MW;  0F3EAB1ADF4C1A3E CRC64;
     MIKISEAINI ITKEAKLLEV EKVHILSSLN KILAEDIYSK DNLPSFDKSA MDGYAIKSED
     TKNCESKNPV ELRIKGIIKA GDYYEEEIKC GEAIKIMTGA AVPRGANAVI EIEKVNTVKD
     KLILNSVVKK ENNIIKMGEE IEIGDLAIQK GKMIRPAEIG LLASLGYKYI HVYKSPVISL
     IITGDELIEI DEEPFMGKIR NSNEYSLRAL IDNLNGKYIS LGVVSDDKNI LKEKIKYAFE
     NSDIVITSGG ASVGDYDFIE DVLKELGADI KFTTISIKPG KPVTFAVYNE KLFFGLPGNP
     MSIITAFEEF VVPAVNKMMG KNNLVKEEIT VVLADDFKGK KGRTKYVYAD IIKENGRYYA
     YNVGSQCSNH LITLSRANGI VIIPADIGSV NKGEILNGKF IFK
//
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