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
//