ID A0A541BAR4_9NOCA Unreviewed; 1203 AA.
AC A0A541BAR4;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-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:TQF69416.1};
GN ORFNames=FK531_11870 {ECO:0000313|EMBL:TQF69416.1};
OS Rhodococcus spelaei.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2546320 {ECO:0000313|EMBL:TQF69416.1, ECO:0000313|Proteomes:UP000316256};
RN [1] {ECO:0000313|EMBL:TQF69416.1, ECO:0000313|Proteomes:UP000316256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-5 {ECO:0000313|EMBL:TQF69416.1,
RC ECO:0000313|Proteomes:UP000316256};
RA Lee S.D.;
RT "Rhodococcus spaelei sp. nov., isolated from a cave.";
RL Submitted (JUN-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:TQF69416.1}.
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DR EMBL; VIGH01000004; TQF69416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A541BAR4; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000316256; 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; 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; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:TQF69416.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000316256}.
FT DOMAIN 5..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1122..1200
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1203 AA; 126711 MW; 67A708FCBC0882C3 CRC64;
MTNASFDTLL VANRGEIACR IMRSAHLLGL KTVAVYSDAD AAAAHVEMAD VAVRLGPAPA
SQSYLRADAV VAAALASGAG AIHPGYGFLS ENDEFAAAVE SAGIAFVGPT PEQLRVFGNK
HTAREAARAV GVPLVPGSGM LESLESALAA AAEIGYPVML KAVGGGGGIG MQACFDAADL
HGAYERVQRL AQANFSSSGV FLERFVANAR HVEVQVFGDG AGRTLSLGTR DCSLQRRNQK
VVEEAPAPGL TDELVERLLS SSRALASSVH YRSAGTVEFV YDVDRGEASF LEMNTRLQVE
HPVTEEVTGV DLVGWMLRLA GGDSSMLDGL PDSGPEITGH AVEARVYAED PGREYRPGAG
LLTSVEFPAH TRVETWVDTG TEVSAHYDPM LAKVIATGVT RAGAFAALGA ALDETRLYGI
ATNLTQLRHI CAMPDVLAAD HTTASLADQR GVGARMDVLR AGTMTTVQDH PGRLGYWEVG
IPPSGPMDDL SFTLVNAAVG NPAGAAGLEC TLQGPQLEFS VTTLVCVGGA PVDLTLDGVA
VPMWEPVTVP AGGVLDIGTP AGEGLRTYLA IRGGIDAPRY LGSASTFTLG GFGGLTGKAV
ATGDVLTLLG AEEGLGAPAS VPVGDRPVLE GTWHLAVTEG PQPAPSYFTA ADMAQFYDTT
WKVQAHANRT GIRLDGPKPT WSRTDGGEAG LHPSNLHDNP YSVGALNVSG DTPILLGPDG
PSLGGFACPL TVARAHRWKL GQIRPGDEVR FVPVTEAGAD ALRGSNAVRA AMLPPSAAHA
TSSDGGVLGR LEPAVDRPEV TYLRGGDDNI LVEYGAMELD LGLRMRVHAL SEALAQWAPR
GLIDVTPGVR SLHLHFDPDV LPSRTLLGLL TEIEESLPAT GDLVVPSRTV RLPLSFDDPS
IAEAIDRYRN GVRDQAPWLP SNTEFIRRIN GLDSVDEVRD AVFDAEYLVL GLGDVYLGAP
LAVPLDPRHR LVTTKYNPAR TWTPSDAVGI GGKYLCVYGM ESPGGYQLIG RTVPIWSGYR
QQGPFVEGKP WLFRFFDRIV WEPVTPEQLS EFRAEARAGR FNAEISDGTF ALADHLAFLD
RNAASIAEFN ARQSEAFEAE KDAWRAAGEF DRIVVAAAEP LAAAVDVPPG AVAVEAPMVG
TVWRVEVEPG AVVEPGQPAV VLEAMKLEMP VAFTTAGTVL EVLVEPGAKV EPGTPLVVIG
AVK
//
