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Database: UniProt
Entry: H6LFI6_ACEWD
LinkDB: H6LFI6_ACEWD
Original site: H6LFI6_ACEWD 
ID   H6LFI6_ACEWD            Unreviewed;       329 AA.
AC   H6LFI6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeA3 {ECO:0000313|EMBL:AFA49473.1};
GN   OrderedLocusNames=Awo_c27200 {ECO:0000313|EMBL:AFA49473.1};
OS   Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS   / WB1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA49473.1, ECO:0000313|Proteomes:UP000007177};
RN   [1] {ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RA   Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA   Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT   "Complete genome sequence of Acetobacterium woodii.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFA49473.1, ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RX   PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA   Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA   Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA   Gottschalk G., Muller V.;
RT   "An ancient pathway combining carbon dioxide fixation with the generation
RT   and utilization of a sodium ion gradient for ATP synthesis.";
RL   PLoS ONE 7:E33439-E33439(2012).
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}.
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DR   EMBL; CP002987; AFA49473.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6LFI6; -.
DR   STRING; 931626.Awo_c27200; -.
DR   KEGG; awo:Awo_c27200; -.
DR   eggNOG; COG0521; Bacteria.
DR   HOGENOM; CLU_068847_1_0_9; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007177; 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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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   Nucleotidyltransferase {ECO:0000313|EMBL:AFA49473.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007177};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AFA49473.1}.
FT   DOMAIN          163..295
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   329 AA;  35774 MW;  BBE6CE63563BFDE4 CRC64;
     MFLAHDMTQI IPGKFKGAAF KKGHIVQEED IPRLLSMGKE HIAIIEFNDG TIHEDEAALR
     LGKAASGIGV EFVSASEGKV TITATQTGLL KINVNVLQEI NELGEMMMAT LHTDTMVTKG
     TLVGSTRIIP LSIENEKLVK MEELCARNEP VVQVVPLKKF KVGVVTTGNE IFYGRIEDKF
     GDVIREKFAE LDSYVFKQVF SRDDSDMIAQ CILDLIKEGA EIVTVTGGMS VDPDDVTPEG
     IGKTGAKFVS YGAPTLPGAM FLLSYLGDIP ILGLPGCIMY SHRTVFDLVV PKLMVGERLT
     RRDISKLGHG GLCSTCSECH YPNCGFGKG
//
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