ID A0A1A8ZRU9_9ACTN Unreviewed; 1826 AA.
AC A0A1A8ZRU9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=GA0070621_2665 {ECO:0000313|EMBL:SBT46613.1};
OS Micromonospora narathiwatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=299146 {ECO:0000313|EMBL:SBT46613.1, ECO:0000313|Proteomes:UP000198765};
RN [1] {ECO:0000313|EMBL:SBT46613.1, ECO:0000313|Proteomes:UP000198765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45248 {ECO:0000313|EMBL:SBT46613.1,
RC ECO:0000313|Proteomes:UP000198765};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; LT594324; SBT46613.1; -; Genomic_DNA.
DR PATRIC; fig|299146.4.peg.2763; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000198765; Chromosome i.
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; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198765}.
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 1543..1825
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1826 AA; 198276 MW; 01E70D699DFDE683 CRC64;
MFSRIAIVNR GEAAMRLIHA VRELNAESGA PPIETIALYT EAERGATFVR EADDSYCLGP
ASARPYLDHR VLERALVETR ADAAWVGWGF VAEDPAFAEL CEKTGVTFIG PSAEAMRELG
DKIGAKLIAE EVGVPVAPWS RGAVESLDAA KRAAAEIGYP LMLKATAGGG GRGIRVVRSD
EELAEAYERT SLEAQRAFGS GVVFLERLVT GARHVEVQVI ADGQGTAWAL GVRDCSVQRR
NQKVIEESAS PVLAPEQTRE LKAAAERLAL AVNYRGAGTV EFLYHPGERL FAFLEVNTRL
QVEHPITEAT TDFDLVKAQI HVAAGGRLGD RVPAEAGHAV EARLNAEDPD RDFAPSPGRI
VRLALPSGPG IRVDTGVSEG DVIPADFDSM IAKIIAYGRT RDEALGRLRR AVAETTVIIE
GGATNKSFLL DLLDQPEVID ASADTGWIDR VRTQGRLVST KHSGIALAAA AIEAYEDEAL
VERQRLLSTA HGGRPQVQHE SGRPIDLKLR GASYRVTVAQ TGPRQFRVGI GEVSTVDVEA
ERFDEHTGRI LVNGRRFRLV TDTHGPIHLV EVDGITHRVS RDEGGVLRSP APALVVATPL
EVGDEIEAGA PVLVLESMKM ETVLRAPFKA KLRECLVTVG SQVETGAPLM RLEPVGDETA
GEAAETEAVD LELPPERTGL SAEARVARGI ADLRSLLLGY DLDPRDERRA LSNYLAARAE
LSHRPLEEEV GLLQVFADLS ELSRNRPVGE ETRADTRVHS PREYFHAYLQ CLDVERAALP
DTFRNRLARV LAHYGVNDFE RTPALEEAVF RIFLAQRRVS ADVSVIVTFL QQWLTEPLPG
DGLRELVGQA LEHLILATQL RFPVVADLAR SIVFRWAAQP MLRRKRAEVY AGVRGHLRHL
DRNPDAADRA ERIAKMVASP EPLVRLLGQR IGKPDADHSP MLEVLSRRYY GNRGASDART
VEVAGHSFFT AAYDRDGERF RLIAAATDFA ELPAALERVA GLVNQDSGPA RRDPAASVAD
VYLTWADQPD TDAMAATLRE ILDRAGLLDV LQRVTMSVAG RTGTAMHHQF TFRPGMGEDR
VIRGLHPLIA QRLQLPRLRN FDLTRLPSVD EEVYLFHCVA PNNPADERLT AMAQVRDLTP
LRDADGRILA LPAVEGALDA CLDAIRKVQA QRPAKKRFDT NRITIYVWPP NDLTIDELNT
VAQRVLPITA GAGLEEVLFL GRQRDAATGE LTDIAVQISY DAGMRVSVTE PTTEPIQPLD
DYRQKVLSAR RRGTTYPYEL TEMLAGQRGS FTEYDLDDTG ELAPVERPKG QNRAGIVAGV
VSTPTERYPE GVTRVVLLGD PTKALGALAE PECARVIAAL DLAERMRVPL DWFALSAGAR
ISMGSGTENM DWVAAALKRI VEFTQQGGEI NIVVAGITVG AQPYWNAEAT MLMHTKGILV
MTPDSAMVLT GKQSLDFSGG VSAEDNFGIG GYDRVMGPNG QAQYWAPDLR AARNVLMAHY
DHTYIAPGET RPRRAVTTDP VDRDISGYPH AVPDSDFATV GEIFSRERNP DRKKAFDIRT
LMRALADQDH AVLERWAGMA DAETAVVQDV HLGGIPVCLL GIESRSVPRR GFPPTDGPDT
YTAGTLFPRS SKKAARAINA ASGNRPLVVL ANLSGFDGSP ESMRQLQLEY GAEIGRAIVN
FEGPIVFCVI SRYHGGAFVV FSKALNPNMT VLAVEGSFAS VIGGAPAAAV VFASDVNART
AKDPRVAELE ARVAAAAGGE RAALVTQLMD VRATVRAEKL GEVAAEFDGV HSIQRAVEVG
SVDAIIRPEE LRPQIVAAVE RGLAGA
//
