ID R0KR38_NOSB1 Unreviewed; 299 AA.
AC R0KR38;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE SubName: Full=Molybdopterin biosynthesis protein moeA {ECO:0000313|EMBL:EOB13201.1};
GN Name=MOEA {ECO:0000313|EMBL:EOB13201.1};
GN ORFNames=NBO_118g0001 {ECO:0000313|EMBL:EOB13201.1};
OS Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS (Pebrine of silkworm).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB13201.1, ECO:0000313|Proteomes:UP000016927};
RN [1] {ECO:0000313|EMBL:EOB13201.1, ECO:0000313|Proteomes:UP000016927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT "Comparative genomics of parasitic silkworm microsporidia reveal an
RT association between genome expansion and host adaptation.";
RL BMC Genomics 14:186-186(2013).
CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC molybdate is inserted into adenylated molybdopterin and AMP is
CC released. {ECO:0000256|RuleBase:RU365090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC ChEBI:CHEBI:62727; Evidence={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;
CC Evidence={ECO:0000256|RuleBase:RU365090};
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.
CC {ECO:0000256|RuleBase:RU365090}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; KB909026; EOB13201.1; -; Genomic_DNA.
DR AlphaFoldDB; R0KR38; -.
DR STRING; 578461.R0KR38; -.
DR EnsemblFungi; EOB13201; EOB13201; NBO_118g0001.
DR VEuPathDB; MicrosporidiaDB:NBO_118g0001; -.
DR HOGENOM; CLU_010186_7_1_1; -.
DR OMA; YAQCSSK; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000016927; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; 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 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 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.
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:UP000016927};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 69..206
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 299 AA; 32244 MW; 35EF1F5F9B6AFF7C CRC64;
MQEQAEQTDE GIRFLAPVKN GQNIRRLGED IAHGAVVFPA GTRLTAAELP VIASLGIAEV
EVVRKVRVAV FSTGDELQLP GQPLADGQIY DTNRLAVHLM LQELGCEVIN LGIIPDDPAK
LREAFIQADQ QADVVISSGG VSVGEADYTK AILEELGEIG FWKLAIKPGK PFAFGKLNHS
WFCGLPGNPV SATLTFYQLV QPLLAKLSGN VGQAQPMRLR VRAASGLKKS PGRLDFQRGV
LQRGPDGELV VSSTGHQGSH IFSSFSLGNC FIVLERERGN VEAGEWVEVE PFNHLFGGL
//