ID A0A0M9GS20_9BACI Unreviewed; 447 AA.
AC A0A0M9GS20;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:KPB04423.1};
GN ORFNames=AAV98_11905 {ECO:0000313|EMBL:KPB04423.1};
OS Bacillus sp. CHD6a.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB04423.1, ECO:0000313|Proteomes:UP000037908};
RN [1] {ECO:0000313|EMBL:KPB04423.1, ECO:0000313|Proteomes:UP000037908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHD6a {ECO:0000313|EMBL:KPB04423.1,
RC ECO:0000313|Proteomes:UP000037908};
RA Lin W., Liu Y., Zheng Q., Jiao N.;
RT "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT hydrothermal environment.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPB04423.1}.
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DR EMBL; LBMD01000013; KPB04423.1; -; Genomic_DNA.
DR RefSeq; WP_060665793.1; NZ_LBMD01000013.1.
DR AlphaFoldDB; A0A0M9GS20; -.
DR STRING; 1643452.AAV98_11905; -.
DR PATRIC; fig|1643452.3.peg.1229; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000037908; 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 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 447 AA; 49724 MW; 68D13E48BD78C5AD CRC64;
MQKILIANRG EIAERIIRTC QRLGVETVAI YSDADKDLPY VQQATVARHV GEAPPQKSYL
NVERILEIAK EENVDAVHPG YGFLSENGEF AQALHDAGLT FIGPNVDVIK LMGDKLSSRR
AMIKAGVPVV PGSEQPVESL EEALVLAEKI GFPVMLKASG GGGGIGMHRC ENKQDIENTF
EQTKKRAKAY FKNEDMFIEK YVGNAKHIEV QIFGDAHGNV VHMFERNCSV QRRNQKVIEE
AQSPAMSEEA RIKICEAAVL AAKEVGYKNA GTVEFIMDEE ENFYFLEMNT RLQVEHPITE
CITGLDLVEW QLNVAAGEKL PLQQEEITST GHAIEFRLYA EDPVKFFPSP GLITKWLLPS
EKGVRVDSGY GPDLKVTPFY DPMIAKIIVS GETREATIER AKEYLRAASV EGIKTNLPFL
IHALEADDFV SGHYHTGFIQ SMKPITT
//
