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Database: UniProt
Entry: B2GIU6_KOCRD
LinkDB: B2GIU6_KOCRD
Original site: B2GIU6_KOCRD 
ID   B2GIU6_KOCRD            Unreviewed;       689 AA.
AC   B2GIU6;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   Name=accA {ECO:0000313|EMBL:BAG30623.1};
GN   Synonyms=accA1 {ECO:0000313|EMBL:BAG30623.1};
GN   OrderedLocusNames=KRH_22760 {ECO:0000313|EMBL:BAG30623.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30623.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG30623.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; AP009152; BAG30623.1; -; Genomic_DNA.
DR   RefSeq; WP_012399344.1; NC_010617.1.
DR   AlphaFoldDB; B2GIU6; -.
DR   STRING; 378753.KRH_22760; -.
DR   KEGG; krh:KRH_22760; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_11; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000008838; 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, ECO:0000313|EMBL:BAG30623.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000008838}.
FT   DOMAIN          1..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          602..675
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          476..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  72340 MW;  FDEB5ABC9B3FCB3C CRC64;
     MFSTVLVANR GEIAVRVMRT LRAMGIRSVA VYSDADAGAR HVKEADVAVR IGPAAAAESY
     LDIDAVVAAA RETGAEAVHP GYGFLAENVD FARACAAAGI AFIGPRECAL EIMGDKIASK
     LQVAEHGVPL VQGVSEPGLT DEQLVAAAAD MPFPVLIKPS AGGGGKGMHV VERYEDLAEA
     LPAARRVAKQ SFGDDTLLIE QLVATPRHIE VQVLADTHGH VIHLGERECS LQRRHQKVIE
     EAPSALLDAA TRARIGEAAV AAAKAVDYVG AGTVEFLVSD REPDTFYFME MNTRLQVEHP
     VTEMVTGVDL VEWQVRIADG EHLTLTQEDV HLDGHAVEAR VYAENPARGF LPTEGTVVAL
     RDASGPGVRV DSGIMAGQRV GLDYDPMLAK VIAHGPDRRT ALQRLRAALE DTVILGVGTN
     VEYLHMLLTD EDVVAGRMDT GLIERKLPQL QFAQPDAYLE ALAAHVVLGS RDDDAARAGS
     LPDAPDAGAG TDPVADPGAD GHHGAERRTA SDTAAHRDRL AARRIGGTAW RADGFSATAA
     LPGPASFEED PSRAVVTAVG AGNPDTAEGR TVHVSEGAAS FEIPVRTRTG ALQAQLAQIE
     RETTAGGPEL RSPMPGTVVA VLAESGEHVA EGRTVVSVEA MKMEHPITAT LPGTVTVLVG
     VGDRVKVDQV VATIETDDTG DADGEAPAA
//
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