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Database: UniProt
Entry: J7IVP1_DESMD
LinkDB: J7IVP1_DESMD
Original site: J7IVP1_DESMD 
ID   J7IVP1_DESMD            Unreviewed;       635 AA.
AC   J7IVP1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   OrderedLocusNames=Desmer_1186 {ECO:0000313|EMBL:AFQ43203.1};
OS   Desulfosporosinus meridiei (strain ATCC BAA-275 / DSM 13257 / KCTC 12902 /
OS   NCIMB 13706 / S10).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768704 {ECO:0000313|EMBL:AFQ43203.1, ECO:0000313|Proteomes:UP000005262};
RN   [1] {ECO:0000313|EMBL:AFQ43203.1, ECO:0000313|Proteomes:UP000005262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC   {ECO:0000313|Proteomes:UP000005262};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
RN   [2] {ECO:0000313|Proteomes:UP000005262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC   {ECO:0000313|Proteomes:UP000005262};
RA   Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Tapia R., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Pester M., Spring S., Ollivier B.,
RA   Rattei T., Klenk H.-P., Wagner M., Loy A.;
RT   "Finished genome of Desulfosporosinus meridiei DSM 13257.";
RL   Submitted (AUG-2012) 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; CP003629; AFQ43203.1; -; Genomic_DNA.
DR   RefSeq; WP_014902122.1; NC_018515.1.
DR   AlphaFoldDB; J7IVP1; -.
DR   STRING; 768704.Desmer_1186; -.
DR   KEGG; dmi:Desmer_1186; -.
DR   eggNOG; COG0303; Bacteria.
DR   eggNOG; COG1910; Bacteria.
DR   HOGENOM; CLU_010186_3_0_9; -.
DR   OMA; IEAKTHS; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000005262; 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   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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   InterPro; IPR024370; PBP_domain.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF16; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   Pfam; PF12727; PBP_like; 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   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AFQ43203.1}.
FT   DOMAIN          176..313
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   635 AA;  69605 MW;  B4B1E1B19EA4F993 CRC64;
     MERQIYLENT AWQDGLKLMM DKLAVRCIPK NEFIDVRSAL HRITGAIVRA KKSSPHFAAS
     AMDGYALRAR DTHGISEREP RWLKLGIQAI QVDTGDPLPE GMDAVVMLED VLELGEQGIL
     LQAPIVPWNH VRPVGEDMVE GEVLLPIHHR IRPQDQGALL AAGVLEVEVR RKPRVGILPT
     GDEIRPVEAN LQVGDIVDSN STVLASLVEE WGGSATIWPI TPDKPELLEA AILEMAATQD
     ILVIIAGSSQ GRDDYTSHLV SKHGNLYLHG VAIKPGKPVV LGEVQEKPTI GIPGYPVSAY
     LTAHLFLEPW VKHYQGLSKD FQSSLDAVIS KKVFSSLGSE EFVRVKVGKV GERWVAAPLS
     RGAGVTMSLV RADGILRVPR LQEGFHEGET VPIELLRPVS ELEETLVCIG SHDLTLDVLS
     SHMKARGGFG GVASAHVGSL AGILSLRKEE AHFAGIHLLD PETGEYNHSY LKRFLPGRDM
     ALMNLVYRTQ VLIVPKGNPL NIKTLADFTK PGVRFVNRQG GSGTRVLFDY LLQQQGLSKE
     QILGYEREEF THLAVAIAVA SGAADVGLGI QSAAEALGLD YIFIGEERYD LAIPREYLEE
     PRMKAMISVI QSKEFQDEVL ALGGYDVRET GVFYI
//
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