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Database: UniProt
Entry: F3Z0M1_DESAF
LinkDB: F3Z0M1_DESAF
Original site: F3Z0M1_DESAF 
ID   F3Z0M1_DESAF            Unreviewed;       646 AA.
AC   F3Z0M1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=Desaf_1508 {ECO:0000313|EMBL:EGJ49845.1};
OS   Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfocurvibacter.
OX   NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49845.1, ECO:0000313|Proteomes:UP000007844};
RN   [1] {ECO:0000313|EMBL:EGJ49845.1, ECO:0000313|Proteomes:UP000007844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49845.1,
RC   ECO:0000313|Proteomes:UP000007844};
RX   PubMed=21642452; DOI=10.1128/JB.05223-11;
RA   Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA   Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA   Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA   Elias D.A.;
RT   "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT   africanus Strain Walvis Bay.";
RL   J. Bacteriol. 193:4037-4038(2011).
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; CP003221; EGJ49845.1; -; Genomic_DNA.
DR   RefSeq; WP_014259629.1; NC_016629.1.
DR   AlphaFoldDB; F3Z0M1; -.
DR   STRING; 690850.Desaf_1508; -.
DR   KEGG; daf:Desaf_1508; -.
DR   eggNOG; COG0303; Bacteria.
DR   eggNOG; COG1910; Bacteria.
DR   HOGENOM; CLU_010186_3_0_7; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007844; 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   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.
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:UP000007844};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          176..317
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   646 AA;  69373 MW;  641886E4A89F1DAA CRC64;
     MERNIYLHTV PLTQAVETLK AALDREALVG REDVDTQDAA GRVLAGPVFA RYSSPTFHSA
     AMDGIAVRAK ETFAAREGSP VRLRLGQGYA PVNTGHPLPA GFDAVVMIEN VVQEGEDTVA
     LEAPAFPMQH VRRIGEDIVA TELLMPQGRR ISAYDLGALL SAGIWQVEAF EPVRLAFIPT
     GDEVLDFMQR PEPKAGQVVE SNSVMLCALA RFWGLEARRV PPVPDNLEAL EAAARQALDS
     DAHIVVIGAG SSAGSKDYTR TVMERVGRVL VHGVAAMPGK PSLLGVAQNG KLLVGAPGYP
     VSAVICFEEL VRPLAAWLGR FDAPERAGLD VELTRKVPSK LGTEEFVRLA VGRVGQRWVA
     TPLARGAGMI TTLTRAQAMT RVPEQLEGLE AGATVRAELL SPMAELDRTL VIVGSHDNTL
     DLLANELMGL AEPVRMSSTH VGSMGGINAL KGGLALCAGA HLFDPETGDF NFPFLAKYVP
     DQDITTVNLA IRHQGLILAK GNPKCIKGVA DLAREDVRFI NRQRGAGTRI LLDHHLKTAG
     IKPEQVRGYD KEEFTHMAVA VNVLTGAADC GLGIYAAAKA LGLDFVELAR ERYDLLIPTR
     FLDDPRIAAL LAMVRSPEFQ AKIRGQGGYE TNLTGQIMRP GMGLEG
//
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