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Database: UniProt
Entry: A0A0F5ZUY7_9GAMM
LinkDB: A0A0F5ZUY7_9GAMM
Original site: A0A0F5ZUY7_9GAMM 
ID   A0A0F5ZUY7_9GAMM        Unreviewed;       588 AA.
AC   A0A0F5ZUY7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=RN22_16185 {ECO:0000313|EMBL:KKD59454.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD59454.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD59454.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD59454.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) 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   -!- 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}.
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:KKD59454.1}.
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DR   EMBL; LASY01000070; KKD59454.1; -; Genomic_DNA.
DR   RefSeq; WP_046305756.1; NZ_LASY01000070.1.
DR   AlphaFoldDB; A0A0F5ZUY7; -.
DR   PATRIC; fig|1581149.3.peg.4154; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000033732; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
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; cd03116; MobB; 1.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR004435; MobB_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; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00176; mobB; 1.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF03205; MobB; 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.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}.
FT   DOMAIN          362..499
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   588 AA;  63746 MW;  EEBF59FEEB78AAF5 CRC64;
     MSLSNCSLPV LGFAAFSGTG KTTLLEKLIP QLVESGVRIA MVKHAHHEFD VDKPGKDSYR
     LRKAGASQML ISSRNRNALM TETPEEEHTL NQLLSRLDQN RADLVLVEGF KHESFPKIEL
     RRDELAKQWL HKEDKNIIAI ACDSHPDSDL PTLDINDVSA ICGFILRWME GHKAQTATCD
     SLSPTMLSVD AGRAKILTAI DEPTSSEVHP LESLSGRVLS EDVIAPVNVP SSTNSAMDGF
     AIRSDDLERD SYQIVGEIYA GHGLGIPLQK GECVRIMTGA PVPEGADTVV MREQAAMDGD
     LVMFDTRKGA IRPGQNVRQA GEDLKKGAAV FNAGTRLNAA SVGMMASLGF NQAKCYKPLT
     AALFSTGDEV QAPGTLAKES CIYDANRFTV RSMLENLGCR ILDLGIIEDS EQALTNTLAT
     AMEKADVVIS SGGVSVGDAD YIKNVLDALG DINFWRVNMR PGRPLAFGKL GNTPFFGLPG
     NPVAVMVTFL QFVEPAIRKM QGDANWQPQL FSAVTQEKIR SRLGRTEYTR GIYSISANGQ
     IEVRSTGSQG SGILRSMHEA NCLIEVSPEV ESAEVGDRVS IIPLVSRL
//
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