ID G8SKX0_ACTS5 Unreviewed; 1159 AA.
AC G8SKX0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=lamA {ECO:0000313|EMBL:AEV86995.1};
GN OrderedLocusNames=ACPL_6108 {ECO:0000313|EMBL:AEV86995.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV86995.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) 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; CP003170; AEV86995.1; -; Genomic_DNA.
DR RefSeq; WP_014693064.1; NZ_LT827010.1.
DR AlphaFoldDB; G8SKX0; -.
DR STRING; 134676.ACPL_6108; -.
DR KEGG; ase:ACPL_6108; -.
DR PATRIC; fig|134676.3.peg.5997; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR HOGENOM; CLU_002162_3_0_11; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000005440; Chromosome.
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 NCBIfam; TIGR00724; urea_amlyse_rel; 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:AEV86995.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000005440}.
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 1081..1159
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1159 AA; 123159 MW; E42F7B375B14BD58 CRC64;
MFDTLLVANR GEIACRIIRT AARLGLKTVA VFSEPDRAAP HVRMADQAVL LGPAPARESY
LVVDRVLAAA LSTGAGAVHP GYGFLSEDAA FATAVEAAGL AFVGPTPAQL TAFGAKHTAR
QLASAAGVPM IQGTGLLSGL DEALTAAAAI GYPVMLKATG GGGGIGMQAC FGPDQLARAY
DRVERLAVAN FGSGGVFLER FVPRARHVEV QVFGDGAGRV VALGDRDCSL QRRHQKVVEE
APAPGLPAAV RDRLHESAAA LCASVGYRSA GTVEFVYDAA REEASFLEVN TRLQVEHPVT
EEIFGIDLVA WMLRLARGDA GMLDEPRRAA GVAVEARVYA EDPTQDHRPG AGLITDAVFP
GDVRVDGWVA AGTEVGTAYD PMLAKVIVTG ATRGEAFANL RTALAGTRID GIETNLGLLR
AAAAHEDVLA ARHSTATLAG VHDTEPRVVV QRPGTLTTVQ DWPGRIGLWE VGVPPSGPMD
DLSFRLGNRA LGNPEGAPGL ECTVDGPALR FTAETTVCVT GAPVPVSVDG RPVPQWEPVV
VPAGAVLDVG TATEGGLRAY VLFAGGLDVP RYLGSAATFT LGQFGGHGGR ALRVGDVLRS
AVGAIGAGRP VAAPPHIGHD WRIRVTEGPH AAPEFFTRED IDAFYAAEWQ VHFNSARTGV
RLVGPKPRWA RTDGGEAGLH PSNIHDTPYS VGAVDFTGDV PILLGPDGPS LGGFVCPATV
ITSERWKLGQ LSPRDTVRFV PVDDLDFTPL IRTRDDGVLA RTDDATYRRS GDDNLLVEYG
PMTLDLGLRM RGHALMDRLR AEGLPGVVDL TPGIRSLQIH IDPAVLPVRK LLDVVRSIEL
PAVRDLEVPS RTVHLPLSWD DPATREAIAR YMNGVRDDAP WCPWNIEFIR RVNGLDAVED
VYRTVYDASY LVLGLGDVYL GAPVATPLDP RHRLVTTKYN PARTWTPENA VGIGGAYLCI
YGMEGPGGYQ FVGRTVQVWS RWQREAGDPW LLRHFDRIRW YPVGAEELLD LRADMAAGRH
RLRIDDGTFR LADHEDFLAA NADSIAAFRA TQAAAFGAER DAWAAAGEFD PRPEPEAAPA
AGQVTVPDGG ALVEAPFVSS VWRVDVRPGD RVAAGQPLLA LEAMKLETVV TAPRAATVTD
ILVTPGAQVA PGSPLVVLA
//
