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Database: UniProt
Entry: C5AFF9_BURGB
LinkDB: C5AFF9_BURGB
Original site: C5AFF9_BURGB 
ID   C5AFF9_BURGB            Unreviewed;       423 AA.
AC   C5AFF9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=bglu_1g14170 {ECO:0000313|EMBL:ACR28566.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR28566.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR28566.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR28566.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
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; CP001503; ACR28566.1; -; Genomic_DNA.
DR   RefSeq; WP_015875459.1; NC_012724.2.
DR   AlphaFoldDB; C5AFF9; -.
DR   STRING; 626418.bglu_1g14170; -.
DR   KEGG; bgl:bglu_1g14170; -.
DR   PATRIC; fig|626418.3.peg.4199; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_4; -.
DR   OMA; GKPLMHG; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002187; Chromosome 1.
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|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002187};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..423
FT                   /note="Molybdopterin molybdenumtransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002947709"
FT   DOMAIN          187..338
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   423 AA;  43763 MW;  C106CAB3BCB0F508 CRC64;
     MSTPASQAPR APLLSTAEAL AALLGAAAPL AQTETVPTLD ALGRVLAVDV VSPLDVPPMA
     ISAMDGYAVR VADLTQGTRR LPVSQRIPAG HAAAPLAAGT AARIFTGAPL PPGADAVVMQ
     EQAEAAGEAV DILHTPKAGE WITAQGADIR RGTVILPAGT RLAPQALGLA ASVGCAHLTV
     RRRVKVAVFF TGDELTMPGE PLAPGAIYNS NRFTLRGLLE RFGCEVSDFG IVPDSLDATR
     ATLREAARDH DLIVTSGGVS VGEEDHVKPA VEAEGRLTLW QIAMKPGKPL AHGAVRRGAG
     NGADGGGSAG EAHFIGLPGN PVSSFVTFLL FVRPFLLRLA GAAQVAPRAL SLRADFTLAK
     GDRRNEFLRA RVNEAGGLDL YPNQSSAVLT STVWGDGLID NPPNHAISAG ETVRFLPFSD
     LLG
//
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