ID A0A0R3MEQ3_9BRAD Unreviewed; 668 AA.
AC A0A0R3MEQ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KRR18513.1};
GN ORFNames=CQ14_24230 {ECO:0000313|EMBL:KRR18513.1};
OS Bradyrhizobium lablabi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR18513.1, ECO:0000313|Proteomes:UP000051660};
RN [1] {ECO:0000313|EMBL:KRR18513.1, ECO:0000313|Proteomes:UP000051660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR18513.1,
RC ECO:0000313|Proteomes:UP000051660};
RA Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT Spain.";
RL Submitted (MAR-2014) 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:KRR18513.1}.
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DR EMBL; LLYB01000103; KRR18513.1; -; Genomic_DNA.
DR RefSeq; WP_057861420.1; NZ_LLYB01000103.1.
DR AlphaFoldDB; A0A0R3MEQ3; -.
DR STRING; 722472.SAMN05444321_6115; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000051660; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 9..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 588..664
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 668 AA; 72515 MW; F9D6D68B257D456E CRC64;
MDRAKLYRRF RTLLIANRGE IACRVIRSAR AMGLRTVAVY SEADRDAMHV AMADEAVLLG
PARARDSYLN IERVIEAARQ TGAEAVHPGY GFLSENAEFA DACLKAGLVF VGPTAEMMTA
MGSKSGSKAL MEKAGVPLVP GYHGEAQDEA TLAKAADAIG FPVLVKASAG GGGRGMRVVN
SAGELSAAIV SAKREAKAAF GDDRMLIEKF VQNPRHIEVQ IIGDSHGNLL SLWERECTLQ
RRHQKVIEEA PSPTLDANQR ETVCAAARKA AAAVNYVGAG TIEFVSDGKE VFFIEMNTRL
QVEHPVTELI TGVDLVEWQL RVAFGEKLPL GQNEIKLNGH AIEARVYAEN PQKNFMPSVG
RIRTWRTPDA VDGLRIDSGY RDGDAVSPYY DAMLAKVIAW APTRQAAIER LNRGLEETDV
RGIVTNIPFL SALITHPNVR ANTIDTGFIE RELKKLTEAS GAPGDLELCA AVAAIVNDEQ
KAARREAHSP WQTFGWMPVG QRQRVFSFRQ GQGAETKVTL RYGNGPSTLS IGKHQFVFAV
SPADDGSFDL TIEGMKSRVT AVIEGHELYL RTRHGRFDLH WVDPFGGETE EQVGEDKIVA
PLPGTVVALL AEEGATLEKG AAILTLEVMK MEQTLRAPFA GVLKKIRCKV GDIVGEGVEL
AEVEPAAS
//
