ID B9L5Q0_NAUPA Unreviewed; 410 AA.
AC B9L5Q0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN OrderedLocusNames=NAMH_1295 {ECO:0000313|EMBL:ACM93305.1};
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nautiliaceae; Nautilia.
OX NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM93305.1, ECO:0000313|Proteomes:UP000000448};
RN [1] {ECO:0000313|EMBL:ACM93305.1, ECO:0000313|Proteomes:UP000000448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC {ECO:0000313|Proteomes:UP000000448};
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM93305.1; -; Genomic_DNA.
DR RefSeq; WP_015902357.1; NC_012115.1.
DR AlphaFoldDB; B9L5Q0; -.
DR STRING; 598659.NAMH_1295; -.
DR KEGG; nam:NAMH_1295; -.
DR eggNOG; COG0303; Bacteria.
DR HOGENOM; CLU_010186_7_1_7; -.
DR OMA; APMPAGC; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000448; 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 Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 178..316
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 410 AA; 45757 MW; AFE22E9F00B78BFA CRC64;
MTVLDNISYS EALELCLKNA KPKKTHQNIY INEALNRVLA EDIIAKRNSP VFTNSAMDGF
AFKHSSDKKL KVIKTIYAGD KYEDFEIKEG ECVRIMTGAR VPNGLDTVIP IEKCEEVTDE
YIMIPEIKKG ANVRIKGEEI AKGDVLIKKG ERITPEIIAM LVSQGIVNVP VYTKLKIAVL
STGNELKEPW ESADEEEIYN VNSYAIEALL KKFGFSADII GLIPDSLEKT VEYIKTLKNE
YDVIITSGGI SFGDADFLFE AFKQNGLKEF FHGIMVKPGR PTMAGIMGET FVFAMPGNPL
SSYINTFALA IPTLKKLSGA DKYYFQSITA VNKSDFKVNA KKDHTILGYY ENGEWEVYNG
YKYGSGMLTP LIKSNSLMLL NKGKDLIKKG EILKIIPFDA GFGKNKFTFN
//