ID A0A023WZS9_9ACTN Unreviewed; 587 AA.
AC A0A023WZS9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 03-MAY-2023, entry version 37.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=RradSPS_0454 {ECO:0000313|EMBL:AHY45737.1};
OS Rubrobacter radiotolerans.
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY45737.1, ECO:0000313|Proteomes:UP000025229};
RN [1] {ECO:0000313|EMBL:AHY45737.1, ECO:0000313|Proteomes:UP000025229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY45737.1,
RC ECO:0000313|Proteomes:UP000025229};
RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA da Costa M.M.S.;
RT "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT RSPS-4.";
RL Submitted (MAR-2014) 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; CP007514; AHY45737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A023WZS9; -.
DR STRING; 42256.RradSPS_0454; -.
DR KEGG; rrd:RradSPS_0454; -.
DR PATRIC; fig|42256.3.peg.462; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_6_11; -.
DR Proteomes; UP000025229; 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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; 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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000025229}.
FT DOMAIN 4..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 511..587
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 494..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 62727 MW; A0179A208BB37E29 CRC64;
MAGIFGKVLI ANRGEIAVRI IRALREMGIE SVAVYSDADR EALHTRLADE AYHIGPTPAT
ESYLNIEKLI EVAKGSGAGA VHPGYGFLAE SAPFARAVNE AGLVWIGPHP GAIEAMGSKV
ESRRIMAKAG VPITPGTEDP VDSPEAVLDF AAEHGFPVAV KASAGGGGKG FAVAFDKTEI
EGAFSRASRE GEAYFGDGSV YCERYLPGPR HIEFQVFRDK HGGAVHLGER DCSIQRRHQK
LVEECPSPAL TPEMREEMGR AAVQAAEAVD YDSAGTCEFL VQDSEFFFLE MNTRVQVEHP
VTEEVTGVDI VKTGIRIAAG EPLPFRQEDV AWRGHAIEVR LNAEDPARDF APSPGRVTAY
REPGGPGVRV DSSLAGPGLV PESYDPLVAK LICSGSDRES ALATLRRALA ELRIEGIATT
ASFHRAILDE ESFLRGEYTT GYVAERMERL KIEPAPPAEA ASDPEREVRE VEVEVNGRRF
EVRLFGEVGT FGGSGGNGRA QAPVRRGGGE RRRASVSEGT VAAPMQGTIV KVLVEEGDSV
EADQAVCVLE AMKMESEVRS QKAGTVSEVH VGAGETVKGG APLVSVE
//
