ID A0L2M9_SHESA Unreviewed; 599 AA.
AC A0L2M9;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN OrderedLocusNames=Shewana3_4081 {ECO:0000313|EMBL:ABK50298.1};
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK50298.1, ECO:0000313|Proteomes:UP000002589};
RN [1] {ECO:0000313|Proteomes:UP000002589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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}.
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DR EMBL; CP000469; ABK50298.1; -; Genomic_DNA.
DR RefSeq; WP_011718791.1; NC_008577.1.
DR AlphaFoldDB; A0L2M9; -.
DR STRING; 94122.Shewana3_4081; -.
DR KEGG; shn:Shewana3_4081; -.
DR eggNOG; COG0303; Bacteria.
DR eggNOG; COG1763; Bacteria.
DR HOGENOM; CLU_010186_5_0_6; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002589; Chromosome.
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; IPR012182; MobB_MoeA.
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 PIRSF; PIRSF036618; MobB_MoeA; 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 373..510
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 599 AA; 64490 MW; D2CA6127823F0D17 CRC64;
MSTPFVNPLS IPVLGFCAYS GTGKTTLLKQ LIPELNQRGL RLAVIKHAHH NFDVDIPGKD
SYEMRKAGAR QMLVASHVRW ALMTEDARDG DPELVHLLKQ IEADKVDIVL VEGFKKLSLP
KIELHRAAHG KPFIYTQDDN ILAIACCDDT ELPSELRRLD LNNVAQIADF VMEYANSWQA
PNPALPIATV DACTLGSDKN LSVSQGLAQI LSHVAPVSEV EEVGLDALDN RVLARDSISP
VDVPQQTNSA MDGYAFVYQD PLPASFNLVG EVLAGHQYSG TLKVGETVRI MTGAPVPAGA
DTVQPRELAN EANAKVSFDG RIQQGQHVRL AGEDIGQGQV ALTQATRLSA AEQGLLASLG
LDRVTVYRRP TVAVFSTGDE VSQPGEALNP NCIYDSNRYT IKAMAKRLGC EVIDLGIIED
SESALEATLT KAAAQADVVI SSGGVSVGDA DYIKAVLARL GNIDFWRINM RPGRPLAFGK
VGDSLFFGLP GNPVAVMVSF LQFVQPALRK LGGETNWQAP LFPAITDETL RSRTGRTEFI
RGIYRLGNDG RLHVTSTGNQ GSGMLSSMVK GNCLIIIGDD AEAVNAGETV FIQPFADLL
//
