ID A0A1W2AF20_9PSEU Unreviewed; 1807 AA.
AC A0A1W2AF20;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=SAMN05660733_00645 {ECO:0000313|EMBL:SMC59266.1};
OS Lentzea albidocapillata.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=40571 {ECO:0000313|EMBL:SMC59266.1, ECO:0000313|Proteomes:UP000192840};
RN [1] {ECO:0000313|Proteomes:UP000192840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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; FWYC01000003; SMC59266.1; -; Genomic_DNA.
DR STRING; 40571.SAMN05660733_00645; -.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR Proteomes; UP000192840; 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; 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}.
FT DOMAIN 1..438
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 111..309
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 560..643
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1527..1803
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1807 AA; 195370 MW; F115F04301ABB417 CRC64;
MRLIHAVREL AAESGERIET VALYTDVDKS APFVREADLA YNLGLAADRP YLNLQVLEKA
LVETKADAAW VGWGFVAEIP EFAELCEKVG VTFVGPSAEA MRKLGDKIGS KLIAEEVGVP
VAPWSRGAVE NLEHALKVAD EVTYPLMLKA TAGGGGRGIR KITSPAEMEE NFDRTSMEAE
RAFGSGVMFL ERLVTGARHV EVQVISDGQG TAWALGVRDC SVQRRNQKII EESASCVLEP
HQVDELKTSA ERLANAVGYR GACTVEFLYH PGEKLFAFLE VNTRLQVEHP ITEITTSFDL
VKAQLHVAGG GRLEGEKPVE LGHAVEARLN AEDPDRDFAP CPGRIVRLEL PAGPGIRVDT
GVAEGSQIPA DFDSMIAKII AYGRNRDEAL GKLRRAMAET TVIIEGGTTN KSFVLDLLDE
PAVIDGSADT SWIDRVRAEG GLISHRHSAI ALAAAGIEVY EDEEQINRTA LLASARGGQP
RTNHEGAVKL EFVLRGQPYI VTVARVGATS YRVGVAAADS ETVLTGDVDV ERFDHHVGQI
TVNGARFRVV TGTHGPVHQV EVDGVTHRVT RDEGGVLRSP MPALVVATPL AVGAEVEAGA
PVLVLEAMKM ETVLRAPFRA RLRELNVVVG TQVPAGGALL KLEEIEDEAG AVEEQRSESA
VELELPAPRT DVRPEELVAS GIDDLRNLLL GFDTTAADTE RVLKNYMDAR HDLPERPLVL
EAELLGIFAD LCDLSRNRPA GEESKPENHI HSPREHFHTY LKTLDADRAA LPEGFRARLQ
NVIGHYGITE LDRTPELEQA VFRIFVALRR GVFDAAVATT LLRQWVQEAP PVESEQVRIG
LVLEHIVAAT QVRYPAVADL ARSVVFTWFA QPLVRRNRAR VHSEVRKHLI HLDAQPQAAD
REERIVAMVA SAEPLVRLLG QRIGKPGADN TPLLEVLARR YYTKKALENP RVHGAFFIAE
NEPEQTRLVS TAVEFPSLTD AIGDVVKHGT GSAVVADLYV NWPGGPSDQD EMAAGLGAAL
AAHQLPPTIT RITTTVAGRR GESMHHHFTF RPSSHGFAEE RLVRGLHPRI AERMQLERLR
EFDLTRLSSV DEDVYLFRAV AKANKSDERL VALGQVRDLT PLRDDEGRIV ALPAAEDVLA
TCLDGIRRAR AQAGGRTRLA TNRVVLYAWP PTELGSKDLD AVGQRVLPTT AGLDLEEVLF
LARRRDPVSG DVSDIGVRIA NDAGSGVRFS FVQPPTDPIQ PLDDYRQNVL RAQSRGTIYP
YELVEMLVGD GGSFVEHDLV DGALVPVDRP RGGNKAGIVV GVVTTPTPAY PEGMKRVVLL
GDPTKSLGAL AEPECSRVIH ALDLAEELSV PLEWFSLSSG AKISMSSGVE NMDWVAAALK
RIVEFTQDGG EINVVVNGIN VGAQPYWNAE ATMLMHTKGI LVMTPDSAMV LTGKQALDFS
GGVSAEDNYG IGGYDRVMGP NGQAQYWAPN LRSAFDVLLG HYEHSYIAPG ETGPRRVSTS
DPVGRDVSSY PHVVGDSPFA TVGEIFSVES NPDRKKPFDI RTVMRALSDQ DHEVLERWAG
MADADTAVVQ DVHLGGIPVT LLGVESRGVA RTGFPPTDGP DTYTAGTLFP KSSKKAARAI
NAASGNRPLV VLANLSGFDG SPESMRELQL EYGAEIGRAI VNFRGPIVFT VISRYHGGAF
VVFSKALNPS MTVLAVEGSF ASVIGGAPAA AVVFAREVDG RTANDPRVKK LESAVAEASG
AERSALTAEL TSTRQSVRTE KLNEMAAEFD RVHSVQRAVE VGAVDAIISA AQLRPAIIKA
IEDGLAG
//
