ID Q6HCF8_BACHK Unreviewed; 429 AA.
AC Q6HCF8;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 95.
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 Name=moeA {ECO:0000313|EMBL:AAT60940.1};
GN OrderedLocusNames=BT9727_4454 {ECO:0000313|EMBL:AAT60940.1};
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT60940.1, ECO:0000313|Proteomes:UP000001301};
RN [1] {ECO:0000313|EMBL:AAT60940.1, ECO:0000313|Proteomes:UP000001301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27 {ECO:0000313|EMBL:AAT60940.1,
RC ECO:0000313|Proteomes:UP000001301};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT60940.1; -; Genomic_DNA.
DR RefSeq; WP_000229672.1; NC_005957.1.
DR RefSeq; YP_038768.1; NC_005957.1.
DR AlphaFoldDB; Q6HCF8; -.
DR KEGG; btk:BT9727_4454; -.
DR PATRIC; fig|281309.8.peg.4743; -.
DR HOGENOM; CLU_010186_7_1_9; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001301; 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|ARBA:ARBA00022505, 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 189..327
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 429 AA; 46650 MW; EF02449AE71DBA84 CRC64;
MVEKRIPIQV AEAVERVMEY AKIGEVEEVS ITESYGKILG EDVVSDHDVP HFDRSPYDGF
AIRAEDTKEA NQENAIEFEV IGEIGAGSVF TEEVGSFQAV RIMTGAAIPA DCNAVVMLEL
TEGFEKNGKT YMKLKRPFHS GDNVSFKGED IKQNQVLVKK GAVINPGVAA LLATFGYSNV
KVVKQPVVGI VTTGSELLEV HESLQPGKIR NSNSYMIAAQ IMKAGGKVRY YGQLADELDA
CFTAVQSAIE EVDILITTGG VSVGDYDYLP AIYERLQANV LFNKIAMRPG SVTTVAEVDG
KLLFGLSGNP SACYVGFELF VHPVIKTYLY AKEPHVYRAD AILQKDFPKP NPFTRFVRAK
VTIVDGALHA MPVGLDKSSA VSSLADANAF IVLPGGTRGF EAGMKVSVLL LEHAEGCDWP
WAKPLRSYK
//
