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Database: UniProt
Entry: A0A157SG68_9BORD
LinkDB: A0A157SG68_9BORD
Original site: A0A157SG68_9BORD 
ID   A0A157SG68_9BORD        Unreviewed;       402 AA.
AC   A0A157SG68;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeA {ECO:0000313|EMBL:SAI69221.1};
GN   ORFNames=SAMEA3906486_02370 {ECO:0000313|EMBL:SAI69221.1};
OS   Bordetella ansorpii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI69221.1, ECO:0000313|Proteomes:UP000076848};
RN   [1] {ECO:0000313|EMBL:SAI69221.1, ECO:0000313|Proteomes:UP000076848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050680373 {ECO:0000313|EMBL:SAI69221.1,
RC   ECO:0000313|Proteomes:UP000076848};
RG   Pathogen Informatics;
RL   Submitted (APR-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; FKIF01000006; SAI69221.1; -; Genomic_DNA.
DR   RefSeq; WP_066127079.1; NZ_FKIF01000006.1.
DR   AlphaFoldDB; A0A157SG68; -.
DR   STRING; 288768.SAMEA3906486_02370; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000076848; 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; 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:UP000076848};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:SAI69221.1}.
FT   DOMAIN          175..313
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  42795 MW;  9F1B3C6C6F6E5AE6 CRC64;
     MLEFDQAQAQ LADAAPAPTR TETVSLAEAP GRVLAVPLDA TLDLPPADNS AMDGYAIRHA
     DYQPGARLPI QQRIYAGDMP RPLAPGQAAR LFTGSLIPEG ADTVIVQEDT READGHVEIT
     EAPRALGQHI RRRGEDTRAG RPLLAAGTVL QAAHVALLAS QGLADVQVYA KLRVGVLTTG
     DELVPPGAAR ATQQIYNSNA SMLGALVRGI GAELTQALHA RDEESDLQAA LQTLVDDCDL
     VLSVGGVSVG EKDLVKPAIE SLGGELTLWK VRMKPGKPVA LARIEGTPLV CLPGNPVSAY
     AVFAVLVSPM LRRMQGRTEI HPPLSRAALR IERPRQDSRE EFVRVQAHAL PDGGMELTPY
     GNQGSGVISS LPWATGLARL PADVLVQDGA QVPYYDLRHW LA
//
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