ID C5C0Z3_BEUC1 Unreviewed; 605 AA.
AC C5C0Z3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN OrderedLocusNames=Bcav_1137 {ECO:0000313|EMBL:ACQ79397.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ79397.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ79397.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
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; CP001618; ACQ79397.1; -; Genomic_DNA.
DR RefSeq; WP_015881637.1; NC_012669.1.
DR AlphaFoldDB; C5C0Z3; -.
DR STRING; 471853.Bcav_1137; -.
DR KEGG; bcv:Bcav_1137; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_6_11; -.
DR OMA; TRWIESD; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000007962; 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, ECO:0000313|EMBL:ACQ79397.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007962}.
FT DOMAIN 16..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 135..332
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 526..602
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 513..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 63443 MW; E9E36FB865473131 CRC64;
MATAVETDRS AVISRPVTKV LVANRGEIAV RVVRALRDAS LASVAVYSDT DRDAPFVRLA
DEAFALGGTR AAETYLDAGK VLDVARRSGA DAVHPGYGFL SEQAEFAQAV IDAGLTWIGP
SPAAIEALGD KVSARHIAQR AGAPLVAGTP DPVASADEVV AFATQHGLPV AIKAAFGGGG
RGLKVARTLE EIPELFDSAV REATASFGRG ECFVERFLDR PRHVETQCLA DAYGTVVVVS
TRDCSLQRRH QKLVEEAPAP FLTPEQDAEL RRASIAILQE ARYEGAGTCE FLVASDGTIS
FLEVNTRLQV EHCVTEEIAG IDLVREQLRI AAGEPLGYSE VTTRGHSIEF RINGEDPAAN
FLPTPGTPST VHWPGGPGVR VDAGIAAGQP VTGNFDSMLA KIVVTGATRT QAIERARRAL
AETEIAGIPT VLPFHRAVLT EPAFVASDGQ FGIWTTWIES EMVGRLVRSP AAPPATPAPS
SDADEKMERV VVEVGGKRLE VVLPAGLGIA AGGAQRRRPA RRSAARPTAS ANGKALSSPM
QGTIVKVAAA DGDVVAEGDL VVVLEAMKME QPLVAHRAGT IRALTAAVGD GVSAGTVICE
IDPTP
//