ID A0A4R4LE25_9ACTN Unreviewed; 1188 AA.
AC A0A4R4LE25;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=uca {ECO:0000313|EMBL:TDB77571.1};
GN ORFNames=E1165_03605 {ECO:0000313|EMBL:TDB77571.1};
OS Micromonospora sp. KC723.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2530381 {ECO:0000313|EMBL:TDB77571.1, ECO:0000313|Proteomes:UP000295555};
RN [1] {ECO:0000313|EMBL:TDB77571.1, ECO:0000313|Proteomes:UP000295555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC723 {ECO:0000313|EMBL:TDB77571.1,
RC ECO:0000313|Proteomes:UP000295555};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequences of novel Actinobacteria.";
RL Submitted (FEB-2019) 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:TDB77571.1}.
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DR EMBL; SMKD01000007; TDB77571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R4LE25; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000295555; Unassembled WGS sequence.
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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:TDB77571.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000295555}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1105..1183
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1188 AA; 126623 MW; 9892B3BAC2A87274 CRC64;
MFDTLLVANR GEIASRIIRT AARMGLKTVA VFSDPDRAAP HVRAADLAVR LGPAPARDSY
LRIDRVLDAA RSTGAGAVHP GYGFLSEDAG FATAVEQAGL AFVGPTPAQL TAFGAKHTAR
DLARAAGVPM IEGTGLLSGL DEALDAAERI GYPVMVKATG GGGGIGMQAC HTPEELTAAY
DRVERLAVAN FGSGGVFLER FVQRARHVEV QVFGDGRGRV VALGDRDCSL QRRNQKVIEE
APAPGLPDAV REQLHRSAAA LCASVRYRSA GTVEFVYDAE REQASFLEVN ARLQVEHPVT
EETLGIDLVE WMLRLAQGDD TVLDTPRRAG GAAVEARLYA EDPTQGHRPS AGLVTDVSFP
AGVRVDGWVA AGTEVTTSYD PMLAKVVVSA ATREEAYAKL RDALAGTRVD GIETNLGLLR
AAAADPTVLA ARHSTATLAG VRDDEPRIVV ERPGTLTTVQ DWPGRTGLWE VGVPPSGPMD
DLSFRLGNRA LGNPEGAPGL ECTVDGPALR FTAPATVCVT GAAAPVTVDG VPVPRWEPVQ
VPAGSVLDVG RATDGGLRSY VLVSGGIDVP RYLGSAATFT LGQFGGHGGR ALRVGDVLRP
GSPTGPVAGP VPLGERPAIR RDWQIAVTEG PHAAPEFFLR EDIDAFYAAQ WQVHFNSART
GVRLVGPKPR WARTDGGEAG LHPSNIHDTP YSVGAVDFTG DVPILLGPDG PSLGGFVCPA
TVVTAERWKL GQLSPGDTVR FVPVSDDTAA ALRARSLTPV TPLVTGDDGV LARREATDAA
PAVTYRRCGD DNLLVEYGPM TLDLGLRMRG HALMDRLRAE GLTGVVDLTP GIRSVQIHVD
PDRLPVRRLL DVVREVEDDL PATRDLAVSS RVVHLPLSWD DPATREAIAR YMAGVRDDAP
WCPWNIEFIR RVNGLDSVDD VHRTVYDASY LVLGLGDVYL GAPVATPLDP RHRLVTTKYN
PARTWTPENA VGIGGAYLCV YGMEGPGGYQ FVGRTVQVWS RWRQAGGFEP GSPWLLRHFD
RISWYPVGAE ELLDLRADVA AGRHRLRIED GTFRLADHED FLAENAASIA DFRRRQAAAF
GRERDAWAAA GEFDPRPEPE APPPAGEVTV PEGGALVEAP FVSSVWRVDV RPGDRVVAGQ
PLLALEAMKL ETVITAPRDG EVADILVTPG SQVAPGSPLL VLAGRTIA
//
