ID A0A1E4I6X0_9PSEU Unreviewed; 576 AA.
AC A0A1E4I6X0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JUN-2023, entry version 24.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=ABS81_08645 {ECO:0000313|EMBL:ODU05044.1};
OS Pseudonocardia sp. SCN 72-86.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1660131 {ECO:0000313|EMBL:ODU05044.1, ECO:0000313|Proteomes:UP000094542};
RN [1] {ECO:0000313|EMBL:ODU05044.1, ECO:0000313|Proteomes:UP000094542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU05044.1}.
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DR EMBL; MEFA01000040; ODU05044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4I6X0; -.
DR Proteomes; UP000094542; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 500..576
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 441..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 59810 MW; 74B246D1146031AE CRC64;
MRTVLVANRG EIAVRILRAC RELGLRTVAV FSDADAAAPH VAMADEAVRI GPAPARSSYL
DIDAILDAAK RTGADAVHPG YGLLSEDAAF AAAVTAAGLT FVGPSADVVA RMGDKVAARA
VAVECGVPAP PGSRPVTAAS VHEAAEGIGF PLVVKATHGG GGRGMRVVTA PEELDGAVTA
AAREAAASFG RSEVHLERYL ERPRHVEVQV VGDTHGTVVH LGDRDCSVQR RHQKLVEEAP
APDLDPALRQ ALTDAAVTLA RTVGYVGAGT VEFLVLPATG EYFFLEMNTR LQVEHGVTEL
VTGLDLVATQ LRVAAGEPLA FSQDDVVIRG HAIQARIAAE DPWEGFRPAP GRVDTLVLPQ
GPGVRNDFGL RAGANAGAVA PEYDSMFGKV LAHGSDRESA RRRLIGALDE LRVDGIPTTA
PYLRSVLDSA SFTNATHDTG SVARDWVPDP GSRPHAPAPQ DAGRRRRVRI ATDRGVVEVD
VHGAGSRAVP RAARATEVPA ASRGAGDGPA VAPMDATVVE VRVVAGQNVE AGDVVAVLEA
MKMEMEIRAG ASGEVAAVLV EAGTPVAAGT PLVDLR
//
