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Database: UniProt
Entry: C5C0Z3_BEUC1
LinkDB: C5C0Z3_BEUC1
Original site: C5C0Z3_BEUC1 
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};
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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
//
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