ID K8EBX0_9FIRM Unreviewed; 339 AA.
AC K8EBX0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=DESHY_60370 {ECO:0000313|EMBL:CCO09198.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO09198.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO09198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
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:CCO09198.1}.
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DR EMBL; CAOS01000013; CCO09198.1; -; Genomic_DNA.
DR RefSeq; WP_008413076.1; NZ_FQXF01000012.1.
DR AlphaFoldDB; K8EBX0; -.
DR STRING; 1121428.DESHY_60370; -.
DR eggNOG; COG0303; Bacteria.
DR OrthoDB; 9767940at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000009315; 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:UP000009315};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 174..306
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 339 AA; 37222 MW; 5BD387B4FF204A89 CRC64;
MKMVPVQEAV GMVLCHDITQ IIPGKFKGRA FKKGHIVKFE DIPRLLDLGK QNLYVWEINK
DLLHEDDAAL RIARAAAGHG ITLTEPKEGK VNLVAKEKGL LKVNSDALYS INELEDVMFA
TLHTNQIVEK DKVLAGTRII PLVIKDDKIR NIENICRINY PLIEVKPFRS LKVGVVTTGS
EVYHGRIQDE FGPVVTKKIA SWGSYVFRQI FVSDSTEMIV NAINQLLREG AEMITATGGM
SVDPDDLTPA GIRAAGGRIV TYGAPTLPGA MFMVAYMGKV PVLGLPGCVM YSRSSIFDLV
VPRILAGEEI TRRDIVALGH GGLCVNCKEC RYPDCGFGK
//
