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
//