ID A0A0K1EDH6_CHOCO Unreviewed; 474 AA.
AC A0A0K1EDH6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE SubName: Full=Acetyl-CoA carboxylase biotin carboxylase {ECO:0000313|EMBL:AKT38930.1};
GN ORFNames=CMC5_030770 {ECO:0000313|EMBL:AKT38930.1};
OS Chondromyces crocatus.
OC Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
OC Polyangiaceae; Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT38930.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT38930.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT38930.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012159; AKT38930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K1EDH6; -.
DR STRING; 52.CMC5_030770; -.
DR KEGG; ccro:CMC5_030770; -.
DR PATRIC; fig|52.7.peg.3380; -.
DR Proteomes; UP000067626; Chromosome.
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 FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
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; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CPAse_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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000067626}.
FT DOMAIN 13..473
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 132..337
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 474 AA; 50365 MW; 8D5200F36CB36100 CRC64;
MTTPRCPSYA SSVLRKILVA NRGEIACRIL RTCKRLGIAT VAVYSDADAQ APHVAMADEA
VRIGPAPVKD SYLNIEAILD AARTTGADGV HPGYGLLSEK RAFADAVAAA GITFIGPPPE
VLDAFGDKIR AREVARKVGV LPPPGTDGPL DPADTEAVAR EAERIGFPLL VKAAGGGGGI
GMQIVPDAAK LARAVQACSD RGRQAFADPR VYLERYIEKP RHIEVQVLCD GKGGAVALGE
RECSVQRRHQ KIIEETPSPA AFFQGSEGEA RRQKLLSDAL RVVTSVGYVG AGTVELVASQ
SGEIWFLEVN ARLQVEHCVT EMVTGIDLVE QQIRVASGEA LAPEILANER RGSSIEARVY
AEDPAKKFAP QPGRVTRLAW PEAGEDLRIE TGITEGLDVT PFYDPMLAKV VAFGETRADA
IQRLDAALGA TTLELTGPAG PAASNLTFLR KVLASEEFAG GQYDTSLAEA LVKR
//
