ID A0A221P1V9_9ACTN Unreviewed; 591 AA.
AC A0A221P1V9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=LK07_21920 {ECO:0000313|EMBL:ASN26229.1};
OS Streptomyces pluripotens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1355015 {ECO:0000313|EMBL:ASN26229.1, ECO:0000313|Proteomes:UP000031501};
RN [1] {ECO:0000313|EMBL:ASN26229.1, ECO:0000313|Proteomes:UP000031501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 137 {ECO:0000313|EMBL:ASN26229.1,
RC ECO:0000313|Proteomes:UP000031501};
RA Ser H.-L., Lee L.-H.;
RT "Genome sequence of Streptomyces pluripotens MUSC 137T.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP022433; ASN26229.1; -; Genomic_DNA.
DR RefSeq; WP_039652976.1; NZ_CP022433.1.
DR AlphaFoldDB; A0A221P1V9; -.
DR STRING; 1355015.LK06_020765; -.
DR KEGG; splu:LK06_020765; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000031501; 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:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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; 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 SMART; SM00878; Biotin_carb_C; 1.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000031501}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 517..590
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 591 AA; 62909 MW; 0E5D881417BEF474 CRC64;
MRKVLIANRG EIAVRVARAC RDAGIASVAV YADPDRDALH VRAADEAFAL GGDTPATSYL
DIDKVLNAAR ESGADAVHPG YGFLSENADF AQAVLDADLI WIGPPPHAIR DLGDKVAARH
IAQRAGAPLV AGTPDPVSGA DEVVAFAEQH GLPIAIKAAF GGGGRGLKVA RTLEEVPELY
ESAVREAVAA FGRGECFVER YLDRPRHVET QCLADKHGNV VVVSTRDCSL QRRHQKLVEE
APAPFLTGEQ TAELYRASKA ILKEARYEGA GTCEFLVGQD GTISFLEVNT RLQVEHPVTE
EVAGIDLVRE MFRIADGEEL GYDDPPLRGH SFEFRINGED PGRNFLPAPG TVTTFHAPSG
PGIRLDAGVE SGSVIGPAWD SLLAKLIVTG RTREEALQRA ARALNEFHVE GMATAIPFHR
AVVKDPAFAP ELTGTSDPFT VHTRWIETEF TNDIKPFTAP ADTEAEEDAT SRETVVVEVG
GKRLEVSLPA SLGMSLARTG LAAGAKPKRR AAKKSGPVAS GDTLASPMQG TIVKIAVEEG
QEVKEGDLVV VLEAMKMEQP LNAHKAGTIK GLNTEVGASI TSGAAICEIK D
//
