ID A0A0B1Y410_9RALS Unreviewed; 676 AA.
AC A0A0B1Y410;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:KHK52132.1};
GN ORFNames=PI87_19645 {ECO:0000313|EMBL:KHK52132.1};
OS Ralstonia sp. A12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1217052 {ECO:0000313|EMBL:KHK52132.1, ECO:0000313|Proteomes:UP000030970};
RN [1] {ECO:0000313|EMBL:KHK52132.1, ECO:0000313|Proteomes:UP000030970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A12 {ECO:0000313|EMBL:KHK52132.1,
RC ECO:0000313|Proteomes:UP000030970};
RA Chen J.W., Yin W.F., Chan K.G.;
RT "Draft Genome of Ralstonia A12.";
RL Submitted (NOV-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:KHK52132.1}.
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DR EMBL; JSZO01000017; KHK52132.1; -; Genomic_DNA.
DR RefSeq; WP_039599417.1; NZ_JSZO01000017.1.
DR AlphaFoldDB; A0A0B1Y410; -.
DR STRING; 1217052.PI87_19645; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000030970; 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 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; 3.30.470.20; 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; IPR048429; MCC_alpha_BT.
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 Pfam; PF21139; MCC_alpha_BT; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 1..459
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 592..671
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 676 AA; 72194 MW; 68E5E6837FB79A04 CRC64;
MITKLLIANR GEIACRVAAT CRKLGIRTVA VYSDADANAR HVAACDEAIH IGEPAARDSY
LRADRILEAA RATGAQAVHP GYGFLSENEA FAKACADAGI IFVGPPASAI EAMGSKSAAK
ALMEKAGVPL VPGYHGDNQD AAFLRTQADR IGYPVLIKAS AGGGGKGMRV VESGDAFEAS
LASVKREASS SFGDDRVLIE KYLTRPRHIE IQVFADGFGD AVYLFERDCS VQRRHQKVLE
EAPAPGMTLD RRRAMGEAAV AAARAVGYVG AGTVEFIVDE DGTFYFMEMN TRLQVEHPVT
EMITGEDLVE WQLRVASGEP LPRTQDELHI HGHALEARIY AENPDRDFLP SIGTLKVLRT
PVAVEFTVGA QANGEPAAVR IDAGVREGDA ISPYYDPMIA KLIVWGRDRE EALARMLQAL
GSFHLVGLSS NVAFLRRLVA SKPFATADLD TGLIARNHDT LFPAAPEVPQ DAIALAVAAL
LAREARSLRT DTRDPHSPWA RGSGWRLNGA AERMLRFTHG DQSIDATLVY GRDGSRLKAN
GADAPFTTQR HGETFTVALG SHKAAGQVHA DGDVFHVFTG GAHWTLERHD PLAHAGDAED
EGGKLTAPMP GKVIAVLATP GQTVTKGAPL VVMEAMKMEH TLTAPADGVV ESVLYSVGDQ
VTEGVQLLAF KPAEGA
//
