ID Q6HIH2_BACHK Unreviewed; 445 AA.
AC Q6HIH2;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Propionyl-CoA carboxylase {ECO:0000313|EMBL:AAT60497.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:AAT60497.1};
GN Name=pcc {ECO:0000313|EMBL:AAT60497.1};
GN OrderedLocusNames=BT9727_2328 {ECO:0000313|EMBL:AAT60497.1};
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT60497.1, ECO:0000313|Proteomes:UP000001301};
RN [1] {ECO:0000313|EMBL:AAT60497.1, ECO:0000313|Proteomes:UP000001301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27 {ECO:0000313|EMBL:AAT60497.1,
RC ECO:0000313|Proteomes:UP000001301};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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DR EMBL; AE017355; AAT60497.1; -; Genomic_DNA.
DR RefSeq; WP_000486737.1; NC_005957.1.
DR RefSeq; YP_036654.1; NC_005957.1.
DR AlphaFoldDB; Q6HIH2; -.
DR KEGG; btk:BT9727_2328; -.
DR PATRIC; fig|281309.8.peg.2465; -.
DR HOGENOM; CLU_000395_3_2_9; -.
DR Proteomes; UP000001301; 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:AAT60497.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
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; 49642 MW; 1D454C498D788728 CRC64;
MFQKILIANR GEIAVRIMKT CQKLGIRTVA IYSEADENAL HVKMANEAYL VGGPRVQESY
LNLEKIIEIA KKTNAEAIHP GYGLLSENPS FPVRCKEEGI VFIGPSEEII TKMGSKIESR
IAMQAADVPV VPGITTNIET AEEAIEIAKQ IGYPLMLKAS AGGGGIGMQL METEQTLTKA
FESNKTRAQN FFGNGEMYLE RYIADAHHIE IQLLADTHGN TVYLWERECS VQRRNQKVIE
EAPSPFLDEG TRKAMGEIAV QAAKALGYTN AGTVEFLVDD QKNFYFLEMN TRLQVEHPVT
EEITGLDLVE QQLLIAYGEK LSFTQDDIKR SGHAIEARIY AEDPKTFFPS PGKITDLTLP
TNVRIDHFLE NQVTITPFYD PMIAKVIAHG ETREEAISKL HDALEELKVE GIKTNTPMLL
QVLEDDVFKS GIYTTGFVTK QLVKK
//
