ID C7RE47_ANAPD Unreviewed; 324 AA.
AC C7RE47;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN OrderedLocusNames=Apre_1437 {ECO:0000313|EMBL:ACV29460.1};
OS Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806
OS / PC1) (Peptostreptococcus prevotii) (Peptococcus prevotii).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525919 {ECO:0000313|EMBL:ACV29460.1, ECO:0000313|Proteomes:UP000002294};
RN [1] {ECO:0000313|EMBL:ACV29460.1, ECO:0000313|Proteomes:UP000002294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1
RC {ECO:0000313|Proteomes:UP000002294};
RX PubMed=21304652; DOI=10.4056/sigs.24194;
RA Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Detter J.C., Han C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Anaerococcus prevotii type strain (PC1).";
RL Stand. Genomic Sci. 1:159-165(2009).
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; CP001708; ACV29460.1; -; Genomic_DNA.
DR RefSeq; WP_015778358.1; NC_013171.1.
DR AlphaFoldDB; C7RE47; -.
DR STRING; 525919.Apre_1437; -.
DR KEGG; apr:Apre_1437; -.
DR eggNOG; COG0303; Bacteria.
DR HOGENOM; CLU_068847_1_0_9; -.
DR OrthoDB; 9767940at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002294; 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 174..306
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 324 AA; 36299 MW; 856D86C092B837EE CRC64;
MIEKIRVEDA VGLPLLHDFT AIMEDGFKGV LFKKGHVVEE SDIEVLKDIG KDHIYVGELE
EDQVHEEDAI DEISDNLFGA NIEASDVSEG KINLTSKVKG LFVIDRTLLR KINEIGDYTI
TCKKSYTKVE EGDRLAGARI VPLWTERRQV ERAKEILEAG PIFEVKEFKK LKVGCIITGD
EVYYGRIKDA FRPVLREKLA EFGAEVLGYE FLPDDEDRLV ATFEKFKEEG ADLVIFTGGM
SVDPDDITPR AIRETHAEVI VQGIPMQPGN MLMVARLGDT YLMGVPGASI HSKVTSFDFF
LPRVFAGIDL KREDFLEIAE GGLL
//
