ID A0A0E3GSP9_CLOSL Unreviewed; 340 AA.
AC A0A0E3GSP9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=CSCA_5326 {ECO:0000313|EMBL:AKA72451.1};
OS Clostridium scatologenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1548 {ECO:0000313|EMBL:AKA72451.1, ECO:0000313|Proteomes:UP000033115};
RN [1] {ECO:0000313|Proteomes:UP000033115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25775 {ECO:0000313|Proteomes:UP000033115};
RA Xie J., Zhu Z., Guo T., Song T.;
RT "Complete Genome Sequence of the Malodorant-Producing Specialist,
RT Clostridium scatologenes ATCC 25775.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKA72451.1, ECO:0000313|Proteomes:UP000033115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25775 {ECO:0000313|EMBL:AKA72451.1,
RC ECO:0000313|Proteomes:UP000033115};
RX PubMed=26210291; DOI=10.1016/j.jbiotec.2015.07.013;
RA Zhu Z., Guo T., Zheng H., Song T., Ouyang P., Xie J.;
RT "Complete genome sequence of a malodorant-producing acetogen, Clostridium
RT scatologenes ATCC 25775(T).";
RL J. Biotechnol. 212:19-20(2015).
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; CP009933; AKA72451.1; -; Genomic_DNA.
DR RefSeq; WP_029162706.1; NZ_CP009933.1.
DR AlphaFoldDB; A0A0E3GSP9; -.
DR STRING; 1548.CSCA_5326; -.
DR KEGG; csq:CSCA_5326; -.
DR HOGENOM; CLU_068847_1_0_9; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000033115; 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; 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 Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 173..305
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 340 AA; 37090 MW; 48B01499ABBEF45E CRC64;
MKKIPTKEAV GSILCHDITQ IIPGKIKGRA FEKGHIITEE DIPVLLSLGK DNLYVWEKKE
GYLHENEAAE RLKNLSAGEG LTFSEVNEGK INFISDKDGI LKIDIDLLTQ LNSIDEIMLA
TIHNNTPVKK GDKVAGTRVI PLVIDEKKIL EAEHLSEGRK IVSVKPYKKF KAAIVTTGNE
VYYERIKDAF GPVVRKKLSQ FDCEIIGSTI VPDNIETITA AIEDFINKGA EMVICTGGMS
VDPDDSTPAA IKNTGAQIVT YGAPVLPGAM FLISYKGDIP ILGLPGCVMY AKTTIFDLVL
PRIFAGEKIK KEDVVILGHG GLCLECNVCT YPHCSFGKGC
//