ID   C7QC11_CATAD            Unreviewed;      1220 AA.
AC   C7QC11;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   OrderedLocusNames=Caci_3728 {ECO:0000313|EMBL:ACU72630.1};
OS   Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS   B-24433 / ID139908).
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU72630.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU72630.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647; DOI=10.4056/sigs.17259;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP001700; ACU72630.1; -; Genomic_DNA.
DR   RefSeq; WP_015792359.1; NC_013131.1.
DR   AlphaFoldDB; C7QC11; -.
DR   STRING; 479433.Caci_3728; -.
DR   KEGG; cai:Caci_3728; -.
DR   eggNOG; COG0439; Bacteria.
DR   eggNOG; COG1984; Bacteria.
DR   eggNOG; COG2049; Bacteria.
DR   HOGENOM; CLU_002162_3_1_11; -.
DR   InParanoid; C7QC11; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000000851; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR003778; CT_A_B.
DR   InterPro; IPR003833; CT_C_D.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR014084; Urea_COase.
DR   NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR   NCBIfam; TIGR02712; urea_carbox; 1.
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; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF02626; CT_A_B; 1.
DR   Pfam; PF02682; CT_C_D; 1.
DR   SMART; SM00796; AHS1; 1.
DR   SMART; SM00797; AHS2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN          4..456
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          122..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1133..1217
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1220 AA;  129460 MW;  32CAA4EDF4BE4DD3 CRC64;
     MSARFDSVLI ANRGEIARRV IRSARALGLR TVAVYSDADR AAPHVREADE AVRLGPAPAR
     ESYLRADAVV EAALRFGAAV HPGYGFLSEN AGFARAVEAA GLVFVGPTPD QIEAFGAKHT
     ARALAAEAGV PMLAGTGLLT GEQEAVAEAL RIGLPVMLKA TGGGGGIGMA ACTSTEEVRQ
     EFARVARLAE SNFGAGGVFL ERLVHPARHV EVQLFGDGAG RVAVFGDRDC SLQRRNQKVI
     EEAPAPNLPD HVRKLLHESA RTLAEQVRYR SAGTVEFVYD PVREQASFLE VNTRLQVEHP
     VTEEVFGIDL VALMLRLARD GAAGLDEEMF GVRQPAGHCV EARVYAEDPG KGGAPSSGLV
     TSAVFPGQGT GPLAGIRVDG WVETGSEVSP YYDPMLAKVI AAGPSRDDAL DVLREGLDAS
     GVDGVVTNLG LLRALTDDPA LRAATHSTST LQSLTDPEPR IDVVVPGLQT TVQDLPGRTG
     LWSVGVPPSG PFDAVSHQEA NLAVGNPAGA PALEATAAGP TLRFSADTVV AVTGAPVQVT
     VDGEPVPMWE PVQIAPGSTL AVGTVTGPGL RVYVAVRGGI DVPRYLGSAS TFTLGGFGGH
     GGRALLAGDV LRPGSPDSAG RHRAFPAGEH LTRVGPPTPR HRRPAMTGTW EIAVTEGPHA
     APEFFTRADI DTLYQSTYTV HHNSARTGVR LIGPRPQWAR GDGGEAGLHP SNIHDTPYAV
     GALDFTGDTP IILGPDGPSL GGFVCPAVVA SGDLWKLGQL RPGDGVRFVP VRESDAAALI
     DDRASTVVLL RGGDGDDGVL GRIEAADGRP GVTYRRDGND NVLVEYGPMT LDIGLRMRVH
     ALRQRLAEHG PRTGILDVTP GIRSLQVHTD AGVLGASQTA ALLRELEETI PPTHELVVPS
     RTVRLPLSWD DPATRLAIER YMAGVRDDAP WTPWNIEFIR RINGLSDVED VRRIVYDASY
     LVLGLGDVYL GAPVATPLDP RHRLVTTKYN PARTWTAENS VGIGGAYMCI YGMEGPGGYQ
     FVGRTVQVWN RFRRGGLFRE HPWALRFFDQ IQWYPVSAEE LLELRAETDA GRGDFETVEG
     EFSIADYERF LTREASSIAE FRATQARAFD EEKERWRASG EFDRQGGEPE IAGAGVGMSD
     TPAVPEGATV VSAPFLSTVW QVLVEPGATV ATGEKVLAVE AMKMESAVLA PCSGLVLGVY
     AKPGDQVSAG QTLLMIAGAR
//