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Database: UniProt
Entry: A0A0L0MHN7_9BURK
LinkDB: A0A0L0MHN7_9BURK
Original site: A0A0L0MHN7_9BURK 
ID   A0A0L0MHN7_9BURK        Unreviewed;       663 AA.
AC   A0A0L0MHN7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000313|EMBL:KND61810.1};
DE            EC=6.4.1.4 {ECO:0000313|EMBL:KND61810.1};
GN   ORFNames=BVER_05979 {ECO:0000313|EMBL:KND61810.1};
OS   Candidatus Burkholderia verschuerenii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=242163 {ECO:0000313|EMBL:KND61810.1, ECO:0000313|Proteomes:UP000036959};
RN   [1] {ECO:0000313|Proteomes:UP000036959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot4 {ECO:0000313|Proteomes:UP000036959};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KND61810.1}.
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DR   EMBL; LFJJ01000011; KND61810.1; -; Genomic_DNA.
DR   RefSeq; WP_050452227.1; NZ_LFJJ01000011.1.
DR   AlphaFoldDB; A0A0L0MHN7; -.
DR   PATRIC; fig|242163.4.peg.459; -.
DR   OrthoDB; 9803706at2; -.
DR   Proteomes; UP000036959; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.700.40; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SMART; SM01209; GARS_A; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KND61810.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036959}.
FT   DOMAIN          1..452
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          582..660
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   663 AA;  71642 MW;  934D2F2EBA0F4E92 CRC64;
     MFNKILIANR GEIACRVAAT AKRLNVGSVA VYSDADAKAK HVDVCDEAVH VGGSAAAESY
     LRIERIVDAA KKTGAQAVHP GYGFLSENEA FANACKQAGI TFIGPPVEAI RAMGSKAAAK
     ALMQSASVPL VPGYHGDDQD ASLLQREADR IGYPVMLKAS AGGGGKGMRV VEKSEDFAAA
     LASCKREAAS SFGNDRVLIE KYLLRPRHVE VQVFADKHGH AVYLFDRDCS VQRRHQKVLE
     EAPAPGLSDE TRRAMGEAAV AAARAVNYVG AGTVEFIMTQ DGQFYFMEMN TRLQVEHPVT
     EMVTGLDLVE WQLRVAAGEP LPLTQDQLKV HGHAIEARIY AENPSRGFLP STGTLKHLRM
     PHAVQFAIDG DVRVDSGVRQ GDAITPYYDP MIAKLIVHGR DRRNALARMS RALAECEIVG
     LHTNVEFLQR IVKSEPFSSG ELDTGLIERH HDALFAPSTV SRNKALALAC AALLTREGGE
     AHGQSPWDAL SHWRMAGGYS QDLNFRATDN DEALKVVFTK NGEKRLQLNG ESARFGWSHS
     GETSYAVQLD DALIKGHVFT DGDIFHVFYE GASFAFEWQN LMAHAGDAEH EGRLTAPMPG
     KVIAVLVQAG ATVEKGAPLM VMEAMKMEHT IVAPSAGKIG EILFDVGDQV ADGAQLLILE
     ASA
//
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