ID Q3ADY1_CARHZ Unreviewed; 634 AA.
AC Q3ADY1;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN OrderedLocusNames=CHY_0799 {ECO:0000313|EMBL:ABB16165.1};
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194 {ECO:0000313|EMBL:ABB16165.1, ECO:0000313|Proteomes:UP000002706};
RN [1] {ECO:0000313|EMBL:ABB16165.1, ECO:0000313|Proteomes:UP000002706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901
RC {ECO:0000313|Proteomes:UP000002706};
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C.,
RA Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B.,
RA Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
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 -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC {ECO:0000256|ARBA:ARBA00003487}.
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; CP000141; ABB16165.1; -; Genomic_DNA.
DR RefSeq; WP_011343729.1; NC_007503.1.
DR AlphaFoldDB; Q3ADY1; -.
DR STRING; 246194.CHY_0799; -.
DR KEGG; chy:CHY_0799; -.
DR eggNOG; COG0303; Bacteria.
DR eggNOG; COG1910; Bacteria.
DR HOGENOM; CLU_010186_3_0_9; -.
DR InParanoid; Q3ADY1; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002706; 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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_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; IPR024370; PBP_domain.
DR NCBIfam; TIGR00177; molyb_syn; 1.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000002706};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 176..313
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 634 AA; 69847 MW; 7A316BD92BF67EAE CRC64;
MAFYLNQVPF EEAWENFESE LLNVNFFHPR EEEIETVLAV GRITCEPVLA KRSNPHFNAS
AVDGFAVKAK DTFYARETSP ILLKIGESCI RVDTGDLIPE GFDAVIMVED VLYPEPGVIS
VIKPVTPGTN IRFLGEDFNE EEVLLPAFAK VKPADIGALL AGGVKTLKVL KKLKALFIPT
GDEIIPFTET PEPGQIPDTN SSFIKAVLAE YGYETSIHPI VKDDPELLYK TVKDNLEKYD
VIIINAGSSA GRDDYAAKVI ERLGRVLVHG LATKPGKPTV LGIAGNKPVI GLPGFPLSAY
LVCEIILKPL AEKYYKNKFH DYGKIKATLT KTLISTTGVD DFVWGKVSRV AGRYCFTPLS
RGASVSSTLL KANALLRIPR FSEGYKEGME IEVTLKEPPA EVDQYLTVTG SHDLLLDLID
SFLREKYGIK LSSSHVGSLN GIVAIEKNYA KLAGVHLLDP ATGDYNQSYV EKRLKGYVLI
NLSLREQGLI VARGNPRKIS GLADLVKPGV TFVNRQKGSG TRVFLDYLLN KENINPRQIS
GYDREEYTHL AVAAKVKNGL ADCGMGIFAA AKIFDLDFIP LGEERYDLLL REDTLEDPQV
KKLLEVITSE EFKKEVERIG GYKTTLTGQI VGKG
//
