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Database: UniProt
Entry: L8DLK1_9NOCA
LinkDB: L8DLK1_9NOCA
Original site: L8DLK1_9NOCA 
ID   L8DLK1_9NOCA            Unreviewed;      1825 AA.
AC   L8DLK1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=RHODMAR_2143 {ECO:0000313|EMBL:CCQ15517.1};
OS   Rhodococcus sp. AW25M09.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ15517.1, ECO:0000313|Proteomes:UP000011207};
RN   [1] {ECO:0000313|EMBL:CCQ15517.1, ECO:0000313|Proteomes:UP000011207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ15517.1,
RC   ECO:0000313|Proteomes:UP000011207};
RA   Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA   Smalaas A.O., Altermark B.;
RT   "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT   from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCQ15517.1}.
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DR   EMBL; CAPS01000058; CCQ15517.1; -; Genomic_DNA.
DR   RefSeq; WP_008714457.1; NZ_CAPS01000058.1.
DR   STRING; 1268303.RHODMAR_2143; -.
DR   eggNOG; COG4770; Bacteria.
DR   eggNOG; COG4799; Bacteria.
DR   OrthoDB; 4435847at2; -.
DR   Proteomes; UP000011207; Unassembled WGS sequence.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
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   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
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; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_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; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
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   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          1..453
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          126..324
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          570..653
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1537..1825
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   1825 AA;  197270 MW;  DE7BF1467E140D7E CRC64;
     MFKRIAVVNR GEAAVRLIRA VRELNAEHDY GIRTVALHTE AEKRAMFVRQ ADEAVTLRKP
     ATGSAYLDYD VLEAALVESG ADAVWVGWGF VAEDPAFADL VARLNITFIG PSADAMRLLG
     DKVEAKILAE KVGVPVAPWS GGPVETRADA RRHAAAIGYP LIIKARSGGG GRGIRKVFHE
     DELELSLERT QGEAERSFGD PVVFLERLVT DARHVEVQVI ADSHGNVWAP GVRDCSIQRR
     NQKVIEESSS PLLTREQADQ LRTASAELVK AAGYQGAGTV EYLYQPEQKI FTFLEVNTRL
     QVEHPITEYT TGIDLVKLQI LVADGQALPG ECPTEFGHAV EARLNAEDAD NGFAPAPGTV
     ELLKFPLGTG IRVDTGIAQG DVIPPDYDSM VAKVIAWGRD RSEALARLRN ALRETTVVID
     GGTTTKSFLL SLLDREEVIS ASADTGWLDR TEAGSQVGPT AVADIAVIAA AIDAYDAEEG
     RERTAFLSSA RGGRPRATHA IGRTVELNYQ GQAYKLEVGQ TGPHRYTIDG DGIGELQVDV
     ERLGTYESRL VIGDHRFSVV TVAGAAHFLV EVDGISHQIS QDEAGLVRAP APAVVVAVPV
     AVGDEVEAGQ TLVVLESMKM ETAVRSPYAG TVREVLASVN GQVDSGAALL RVDQAGEQKV
     SEQAPRVRFR GIDDAAQRSP QRRALDRLDE LAALITGFDV SGARARNLLS TYETLRAEVP
     RNDSELVGAE LSLLNTFADI CELSRNRPTM DEESTDERVH SPREHFHSFM QSLDADVQGL
     PESFRGKLTR ALAHYDAAID EGRTPELEEA VYRVFLALQR MENQVPVIAA LLGHWLSDCS
     AQPEATPAMA EVLERLIGAT QARYPVIGDV ARNLRFRLFD EPQINTAREK IYDGVRGSLQ
     YLAENPDAAD YSARIAALVA TPEPLIELLA QRITDPGALL EVITRQYYEI RTLEDVKAFD
     RDGTHFVTGN FELAGEQLQL ISTATDFDSL ATTLHSIDDI SGPAPENLAV DLYLSWPDAP
     ADGDALSDQL QAALAEHPGS GRWRRVTVTA FGSVTRKMTY RRTAAEGTEP LAEDTIIRDM
     HPLTGQRLDL WRLKNFDGVR LPASAGTYLF HLTSKANPSD ERLVALAEIR GITTQLDEAG
     NIVAVPEIER TVAACLDGIR RAQAGRGKKR LDANRVMLYV WPVLNVPADR IATIARHIAP
     LTIGAGLEEI TLIARLAETP GAKPREVALR LSYRSGAGIV AKVTPPPTEP MRPLDEYTQK
     VQRSQARGTV YPYELIPLLS SNGGSFTEYD FDADGVLAPV DRPYGRNTAG VIVGVATTPT
     AKYPEGITRV ALFGDPTKAL GTVAEAECSR IVAAIDLAEQ LGAPVEWFAL SSGATISMES
     GTENMDWVSR GLRRIITFTQ AGGEINIVVA GINVGAQPYW NAEATMLTHT KGILVMTPDS
     AMVLTGKQSL DYSGGVSAED NFGIGGYDRV MGPNGQAQYW APNLRAACDI LFAHYEHAYA
     APGERFPRRA ATADPTERDV RTYPHVHPSS DFTTVGDIFS SVTNPDRKKP FDIRTVMRAV
     VDQDHSVLER WADMADADTS VVFDAHLAGI PVSVIGIESR AIPRKGWFPS DGPDQWTSGT
     LFPNSSKKTA RAINAASGSR PIVVLANLSG FDGSPESLRN IQLEYGAEIG RAIVNFDGPV
     VFCVVSRYHG GAFVVFSGAL NDNMEVLAVE GSFASVLGGA PAAAVVFTRD VNARTAADPT
     VKELETALNT AEDDATRSAL RVELATVRAN ARNAKLGEVA AEFEAIHNIQ RAQNVGSVHH
     IVPAAELRPQ LVAAIERGMA RSLAT
//
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