ID A0A1H9W3S4_9ACTN Unreviewed; 462 AA.
AC A0A1H9W3S4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=SAMN04487983_104029 {ECO:0000313|EMBL:SES28337.1};
OS Streptomyces sp. yr375.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761906 {ECO:0000313|EMBL:SES28337.1, ECO:0000313|Proteomes:UP000198568};
RN [1] {ECO:0000313|EMBL:SES28337.1, ECO:0000313|Proteomes:UP000198568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR375 {ECO:0000313|EMBL:SES28337.1,
RC ECO:0000313|Proteomes:UP000198568};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOFF01000040; SES28337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9W3S4; -.
DR STRING; 1761906.SAMN04487983_104029; -.
DR OrthoDB; 3196725at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000198568; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000198568};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:SES28337.1}.
FT DOMAIN 238..374
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 22..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 47996 MW; 82D7A980AB5AF924 CRC64;
MTPHGTRQGL DAEDLDVEEA LALVKDGNGP ARPTGDHGPA QREGSADGTP SSETSPAPEH
RHRAISWPEA RTIAARAARS GAARRPPVSV TLGDALGLVL AAPLTALTDL PSFDTSAMDG
WAVAGPGPWH VRDEGVLAGS AAPASLGDGE AVRIATGARI PADTTAVLRS EHGRTDDSGR
LHPTREMQHG QDIRPRGQEC RSGDQLLLAG AVVTPAVLGL AAAAGYDTLT AVPRPRVEVL
VLGDELLTEG RPHEGLIRDA LGPMLPPWLR ALGAEVIAVR RLRDDAKVLH KAVTASGADL
IVTTGGTAAG PVDHVHPTLR RLDAELLVDS VKVRPGHPML LARLKDDQHL VGLPGNPLAA
VSGLITLAEP LLRTLAARSA PEPYTLPLRE TVHGHPYDTR LVPVVLRGDH VVPLHYNGPA
MLRGIAVADA LAVVPPGGAG AGQEAELLDL PWATAGIGAC FT
//
