ID Q81D92_BACCR Unreviewed; 445 AA.
AC Q81D92;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=Propionyl-CoA carboxylase biotin-containing subunit {ECO:0000313|EMBL:AAP09444.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:AAP09444.1};
GN OrderedLocusNames=BC_2484 {ECO:0000313|EMBL:AAP09444.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP09444.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP09444.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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DR EMBL; AE016877; AAP09444.1; -; Genomic_DNA.
DR RefSeq; NP_832243.1; NC_004722.1.
DR RefSeq; WP_000486761.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81D92; -.
DR KEGG; bce:BC2484; -.
DR PATRIC; fig|226900.8.peg.2519; -.
DR HOGENOM; CLU_000395_3_2_9; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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:AAP09444.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001417}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 445 AA; 49558 MW; 003684A077E36ED3 CRC64;
MFQKILIANR GEIAVRIMKT CQKLGIRTVA IYSEADENAL HVKMANEAYL VGGPRVQESY
LNLEKIIEIA KKTNVEAIHP GYGLLSENPS FPVRCKEEGI VFIGPSEEII TKMGSKIESR
IAMQAADVPV VPGITTNIET AEEAIEIAKQ IGYPLMLKAS AGGGGIGMQL METEQTLTKA
FESNKTRAQN FFGNGEMYLE RYIADAHHIE IQLLADTHGN TVYLWERECS VQRRNQKVIE
EAPSPFLDEG TRKAMGEVAV QAAKALGYTN AGTVEFLVDN QKNFYFLEMN TRLQVEHPVT
EEITGLDLVE QQLLIASGEK LSFTQDDVKR SGHAIEARIY AEDPKTFFPS PGKITDLTLP
SNVRIDHFLE NHVTITPFYD PMIAKVIAHG ETREEAISKL HDALEELKVE GIKTNTPMLL
QVLEDEVFKA GIYTTGFVTK QLVKK
//
