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Database: UniProt
Entry: A0A087BND2_9BIFI
LinkDB: A0A087BND2_9BIFI
Original site: A0A087BND2_9BIFI 
ID   A0A087BND2_9BIFI        Unreviewed;       581 AA.
AC   A0A087BND2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   05-JUN-2019, entry version 19.
DE   SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:KFI72532.1};
DE            EC=6.3.4.14 {ECO:0000313|EMBL:KFI72532.1};
GN   ORFNames=BMIN_0428 {ECO:0000313|EMBL:KFI72532.1};
OS   Bifidobacterium minimum.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI72532.1, ECO:0000313|Proteomes:UP000029014};
RN   [1] {ECO:0000313|EMBL:KFI72532.1, ECO:0000313|Proteomes:UP000029014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI72532.1,
RC   ECO:0000313|Proteomes:UP000029014};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFI72532.1}.
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DR   EMBL; JGZD01000009; KFI72532.1; -; Genomic_DNA.
DR   RefSeq; WP_026647305.1; NZ_JGZD01000009.1.
DR   STRING; 1693.BMIN_0428; -.
DR   EnsemblBacteria; KFI72532; KFI72532; BMIN_0428.
DR   OrthoDB; 361205at2; -.
DR   Proteomes; UP000029014; 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:0046872; F:metal ion binding; IEA:InterPro.
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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029014};
KW   Ligase {ECO:0000313|EMBL:KFI72532.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029014}.
FT   DOMAIN        1    443       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      119    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      507    581       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   REGION      448    470       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A087BND2}.
SQ   SEQUENCE   581 AA;  62179 MW;  410291E607B22BD9 CRC64;
     MTRVLIANRG EIAVRVIHAC HENGWTALAV YADSDADALF VHLADEAYAL GADSPKDTYL
     DAARIIEVAV RSDADAIHPG YGFLSENADF AQAVIDAGLV WIGPSPDSIR LLGDKVAARR
     IAAEVGAPMA PGTTEPVRDP AEVVGFVREH GLPVAIKAVH GGGGKGLKVV RRLEDVREAF
     LSATREAEES FGNGDCFIER FLSRPRHVEV QVLGDGDGHV IAVGTRDCSL QRRNQKLIEE
     APAPFLGTDV VTRLCDSAVA ICSRAGYVGA GTVEFLVDPD GTISFMEVNT RIQVEHAVTE
     EVTGVDLVKA QFSIAQGACV SDMDIHIHGH AMEFRINAED PAHGFVPFPG RIRSLRVPSG
     PGIRFDTGIE AGSVVPGRFD SMLAKLIVTA PDRASCLARA RRALAELRIE GVPTVIPFDR
     LVLRDPDFTG DDRLNIYTRW IEESFLPRTD PKDLSGPRPS RDQGGDPVTR SWIEIDGRRM
     ELGIPSGLLP AMTGAIADGG DAAPDDSTTT ASPGDVLAPL TGTVTSWLVD EGDRVERGTP
     VATLEAMKME TQVMAPVSGV IHRTASIGDL VDYGEPMGRV E
//
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