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Database: UniProt
Entry: Q72DH8_DESVH
LinkDB: Q72DH8_DESVH
Original site: Q72DH8_DESVH 
ID   Q72DH8_DESVH            Unreviewed;       445 AA.
AC   Q72DH8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=DVU_0951 {ECO:0000313|EMBL:AAS95431.1};
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882 {ECO:0000313|EMBL:AAS95431.1, ECO:0000313|Proteomes:UP000002194};
RN   [1] {ECO:0000313|EMBL:AAS95431.1, ECO:0000313|Proteomes:UP000002194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC   {ECO:0000313|Proteomes:UP000002194};
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA   Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA   Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA   Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA   Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA   Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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   -!- 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; AE017285; AAS95431.1; -; Genomic_DNA.
DR   RefSeq; WP_010938250.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_010172.1; NC_002937.3.
DR   AlphaFoldDB; Q72DH8; -.
DR   SMR; Q72DH8; -.
DR   IntAct; Q72DH8; 4.
DR   STRING; 882.DVU_0951; -.
DR   PaxDb; 882-DVU_0951; -.
DR   EnsemblBacteria; AAS95431; AAS95431; DVU_0951.
DR   KEGG; dvu:DVU_0951; -.
DR   PATRIC; fig|882.5.peg.895; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_2_7; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 9804758at2; -.
DR   PhylomeDB; Q72DH8; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002194; 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   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
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   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 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.
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:UP000002194};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          215..354
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   445 AA;  46854 MW;  661E339642967956 CRC64;
     MQQRFFRVLT VSELVALLRT CAPLGAECPT AGRSDSLPIE DAASLDSSDA PTSLESSGSL
     DSLDGRVLAK AVVARENLPA THRAAMDGYA VRAADLFGAS EGSPAYLDVV GHSAIDARPD
     VTLGPGQCLG IVTGGTLPEG ADAVLMVEYA HDLGGGAIEA HRPVAPWENV MLRAEDAEEG
     RVVLPAGTLL RPQEVGLLAA LGETAPLVHR RPRVAVISTG DELVPADATP RDGQIRDVNT
     HTLACLVRRA GAVPRCMGLV PDVLPALEAA LRQGLETADV VLLSGGSSVG VRDLTVAALE
     RIEGAELLCH GVAISPGKPL IVARVGEKLV WGLPGQVTSA QVVMHVLGMP FLRHLAGWQD
     AFDMSRWPSR RAVLARNTAT RQGREDYIRV RLDPRPDDLP EAVPLFGKSG LLKTLVGSDG
     VVRIPAEVEG LERGALVDVL LFGER
//
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