ID B7Q7N3_IXOSC Unreviewed; 453 AA.
AC B7Q7N3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 08-NOV-2023, entry version 83.
DE RecName: Full=molybdopterin molybdotransferase {ECO:0000256|ARBA:ARBA00013269};
DE EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269};
DE Flags: Fragment;
GN ORFNames=IscW_ISCW020891 {ECO:0000313|EMBL:EEC14855.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC14855.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC14855.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW020891-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW020891-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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|RuleBase:RU365090}.
CC -!- SIMILARITY: Belongs to the MoeA family.
CC {ECO:0000256|RuleBase:RU365090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; ABJB010076603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010186115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010416772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010676371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010809982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS876681; EEC14855.1; -; Genomic_DNA.
DR RefSeq; XP_002404228.1; XM_002404184.1.
DR AlphaFoldDB; B7Q7N3; -.
DR STRING; 6945.B7Q7N3; -.
DR PaxDb; 6945-B7Q7N3; -.
DR EnsemblMetazoa; ISCW020891-RA; ISCW020891-PA; ISCW020891.
DR KEGG; isc:IscW_ISCW020891; -.
DR VEuPathDB; VectorBase:ISCI020891; -.
DR VEuPathDB; VectorBase:ISCP_018526; -.
DR VEuPathDB; VectorBase:ISCW020891; -.
DR HOGENOM; CLU_010186_2_2_1; -.
DR InParanoid; B7Q7N3; -.
DR OMA; GVIRRIN; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:GOC.
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; IBA:GO_Central.
DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IBA:GO_Central.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IBA:GO_Central.
DR GO; GO:0072579; P:glycine receptor clustering; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; IBA:GO_Central.
DR CDD; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
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 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 NCBIfam; TIGR00177; molyb_syn; 2.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 2.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:B7Q7N3};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 1..117
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 220..363
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEC14855.1"
SQ SEQUENCE 453 AA; 48549 MW; C38BE09F62E97B5A CRC64;
INGTVTIRQC TPDDAEKIKE VLVMWADVMK LDLILTTGGT GFSERDVTPE ATRAVITKEA
PGMAVAIIQK SLEVTPMAML SRLVCGIRNQ TLIINLPGSF KGSQECLQFA SPAIPHAIDQ
LRGCKEKTDK FHASLSCTAK DSPINLSSEK REPGVANRPR HSPYPLLSVK EAQDIVLREC
FKTGIEAVAF KGTKLGPAEL GLLATVGRTT VNVFCLPSVA VLSTGNELVV PGSDVQPGKI
RDSNKTTLLS LLSSNGFEAI DAGIALDSRA DLCGKLRRAF EAADVLVSSG GVSMGEKDLL
KAVLSEEFQA TVHFGRVFMK PGKPTTFATL QYLGRPKLVF GLPGNPVSAT VTCHLYVLPA
LRRMSHHINV FPTEITAKLA DDIQLDPRPE YHRAVLNWSP GSLPVATSSG NQISSRLLSF
RGVNALIVLP GSKEGAETFR AGSLVTALVT DRL
//