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Database: UniProt
Entry: A0A1H8NMI8_9BURK
LinkDB: A0A1H8NMI8_9BURK
Original site: A0A1H8NMI8_9BURK 
ID   A0A1H8NMI8_9BURK        Unreviewed;       679 AA.
AC   A0A1H8NMI8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   25-APR-2018, entry version 5.
DE   SubName: Full=3-methylcrotonoyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:SEO30772.1};
GN   ORFNames=SAMN05428959_106223 {ECO:0000313|EMBL:SEO30772.1};
OS   Duganella sp. CF517.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Duganella.
OX   NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEO30772.1, ECO:0000313|Proteomes:UP000198691};
RN   [1] {ECO:0000313|EMBL:SEO30772.1, ECO:0000313|Proteomes:UP000198691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF517 {ECO:0000313|EMBL:SEO30772.1,
RC   ECO:0000313|Proteomes:UP000198691};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FODC01000006; SEO30772.1; -; Genomic_DNA.
DR   Proteomes; UP000198691; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198691};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198691}.
FT   DOMAIN        1    458       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      598    677       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   679 AA;  72030 MW;  C7B79F70CA07A536 CRC64;
     MFTKILIANR GEIACRVAAT ARRLGIKTVA VYSEADAGAK HVAVCDEAVL IGPAAAKESY
     LCGDKIIAVA RATGAQAIHP GYGFLSENAG FADACAEAGL VFIGPPASAM RAMGSKSAAK
     SLMEKANVPL VPGYHGEQQD ADFLHTQADK IGYPVLLKAS AGGGGKGMRV IENSAQFKDA
     LASCKREAIS SFGDDKVLAE KYLQRPRHIE IQVFADTLGN CIYLFERDCS VQRRHQKVLE
     EAPAPNMTAE RRAAMGEAAV AAAKAVGYVG AGTVEFIANQ DGSFYFMEMN TRLQVEHPVT
     EMITGTDLVE WQLRVAAGEP LPKQQHELVI NGHAIEARIY AENPEKGFLP SIGTLRHLAT
     PDAVSFELGG ATNLPAGVRI DSGVRAGDAI SPFYDPMIAK LIVWGADRKQ ALARMAQALS
     EYQVVGLATN IAFLKRLVEG RAFATADLDT GLIERNQDAL FPAPQAAPKA ALALAVVSLI
     ATEKQRAAAQ SRANPADPWG RALGWRMNQP YVRALSFGDE FASDEPYTAH VSYRADGWLF
     SVGAGAQPEA LGLTAEDGNG YSIKLGDQAV HGAVRRDGDV LHVFTGGAHY QLTYNDPMAH
     AGETEAEGGR LTAPMPGKVV AVLATKGQEV KKGDALVIME AMKMEHTIAA PHDGVVDDIL
     YGVGDQVADG APLLAFKTA
//
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