ID A0A068LP54_BACMM Unreviewed; 459 AA.
AC A0A068LP54;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Biotin carboxylase 2 {ECO:0000313|EMBL:AIE59546.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:AIE59546.1};
GN Name=accC2 {ECO:0000313|EMBL:AIE59546.1};
GN ORFNames=BMMGA3_05590 {ECO:0000313|EMBL:AIE59546.1};
OS Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE59546.1, ECO:0000313|Proteomes:UP000027602};
RN [1] {ECO:0000313|EMBL:AIE59546.1, ECO:0000313|Proteomes:UP000027602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGA3 / ATCC 53907 {ECO:0000313|Proteomes:UP000027602};
RX PubMed=25758049;
RA Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT previously uncharted transcriptional landscape.";
RL BMC Genomics 16:73-73(2015).
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DR EMBL; CP007739; AIE59546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068LP54; -.
DR STRING; 796606.BMMGA3_05590; -.
DR KEGG; bmet:BMMGA3_05590; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_9; -.
DR Proteomes; UP000027602; Chromosome.
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 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AIE59546.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000027602}.
FT DOMAIN 8..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 459 AA; 52067 MW; 976C399A3577CDD5 CRC64;
MEAERGTRVQ KIIIANRGEI ASRIIRTCHA LGIETIAVYS DADRDMPYVK EAKYAFRIGE
PLVQKSYLNS DLLLKIAKSE KADGIHPGYG FLSENADFAR KVRKEGLTFI GPSPETIERM
GDKITARNTM EKAGIPVIPG SREGLTTLEE ACDFAESIGY PVMLKASGGG GGIGMVHCEN
QKELTKFFES TKARAKAYFG SEKIFIEKYI QNARHIEVQI FGDAYGNIVH LFERDCSVQR
RHQKVIEETP SPFLSEHTRK QMYAAALKAA EVVHYVNAGT IEFIVDEEEN FYFLEMNTRL
QVEHPITEQI TGLDLVKWQI LVAKGERLPL LQNEINRSGH AMEFRLYAED PNTFMPSPGK
ITGFKWKEFE GVRIDHGYLE GCFVTTFYDP MVAKCIFYSK AREDVLKTAK EFFQNIKIEG
IKTNIPLFIN IIDDSDFQNG TYTTKFLIEK TLQWSRGSL
//
