ID A0A0C2VJX2_9BACL Unreviewed; 450 AA.
AC A0A0C2VJX2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:KIL44781.1};
GN ORFNames=KP78_23250 {ECO:0000313|EMBL:KIL44781.1};
OS Jeotgalibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL44781.1, ECO:0000313|Proteomes:UP000031938};
RN [1] {ECO:0000313|EMBL:KIL44781.1, ECO:0000313|Proteomes:UP000031938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P9 {ECO:0000313|EMBL:KIL44781.1,
RC ECO:0000313|Proteomes:UP000031938};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Genome sequencing of Jeotgalibacillus soli.";
RL Submitted (JAN-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:KIL44781.1}.
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DR EMBL; JXRP01000018; KIL44781.1; -; Genomic_DNA.
DR RefSeq; WP_041088872.1; NZ_JXRP01000018.1.
DR AlphaFoldDB; A0A0C2VJX2; -.
DR STRING; 889306.KP78_23250; -.
DR PATRIC; fig|889306.3.peg.2339; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000031938; 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}; Reference proteome {ECO:0000313|Proteomes:UP000031938}.
FT DOMAIN 1..445
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 450 AA; 50388 MW; B4E2F0EB56A6E32C CRC64;
MKKLLVANRG EIALRIIRSC QKLNITTVAI YSEADAQMPY VSEADIAYEI GPAPVAKSYL
NMDAILNIAK KEQVDAIHPG YGLLSENAIF VRKIEDAGIR FVGPDASIIE RMGDKISARK
TMMEAGVAVI PGIDSEMESV KTAFQFATEV GYPIMLKASS GGGGVGMIRC DDEQALTQHF
ESTKQRSKTY FGSDRLFIEK YIPRARHIEV QIFGDYKGSI FHLWERNCSM QRRNQKIVEE
SPAPKLSNEA RTKILKTAVR AAQAVGYKNA GTIEMIVDEK ENAYFLEMNT RLQVEHPVSE
MITGVDLVEW QLLTAMEKPL PISKQQEIHV NGHAMEFRLY AEDPITFYPS PGTLSSVVFP
SGEGIRIDEG YLEGNKVTPF YDPMIAKMII HADSREKCLE KARKAVKATV IEGVKTNLLF
FIKMLDEKDF IEGSYHTQSI DQIVKGEKNL
//
