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Database: UniProt
Entry: A0A1H6KHM3_9MYCO
LinkDB: A0A1H6KHM3_9MYCO
Original site: A0A1H6KHM3_9MYCO 
ID   A0A1H6KHM3_9MYCO        Unreviewed;       662 AA.
AC   A0A1H6KHM3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-FEB-2019, entry version 16.
DE   SubName: Full=Acetyl-CoA/propionyl-CoA carboxylase, biotin carboxylase, biotin carboxyl carrier protein {ECO:0000313|EMBL:SEH72801.1};
GN   ORFNames=SAMN04489835_3359 {ECO:0000313|EMBL:SEH72801.1};
OS   Mycolicibacterium rutilum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=370526 {ECO:0000313|EMBL:SEH72801.1, ECO:0000313|Proteomes:UP000182915};
RN   [1] {ECO:0000313|EMBL:SEH72801.1, ECO:0000313|Proteomes:UP000182915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45405 {ECO:0000313|EMBL:SEH72801.1,
RC   ECO:0000313|Proteomes:UP000182915};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT629971; SEH72801.1; -; Genomic_DNA.
DR   BioCyc; GCF_900108565:BLW81_RS16570-MONOMER; -.
DR   Proteomes; UP000182915; Chromosome i.
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:UP000182915};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN        2    447       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      121    320       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      582    652       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   662 AA;  69458 MW;  B7923665328320E7 CRC64;
     MTFDTVLVAN RGEIAVRVIR TLRQMGVRSV AVFSTADAGA RHVAEADVAV HIGPAAARES
     YLNIDAVLSA ARRTGAQAVH PGYGFLSENA QFAAALEAAG ITFIGPPVGA IETMGDKIAA
     KAAVSAFGVP VVPGISRPGL TDDDLIAGAA EVGFPVLVKP SAGGGGKGMR VVHDAAELPA
     ALVSARREAG AAFGDDTLFL ERFVLNPRHI EVQVLADAHG NVVHLGEREC SLQRRHQKVI
     EEAPSPLLDA ATRARIGAAA CDTARSVDYT GAGTVEFIVS ADRPDEFFFM EMNTRLQVEH
     PVTEMVTGID LVEQQVRIAA GEKLCVAQDD VTLTGHAVEA RVYAEDPARG FLPTGGPVLD
     LAEPADVRVD SGLARGSVIG SDYDPMLSKV IAYADDRAGA LRALDRALAG TAVLGVTTNV
     EFLRFLLADP DVVAGRLDTG LLDRRSPDFE SAPATDAELV AAAAYKWLSA WPVPASDLWA
     TPSGWRMGRH APTTYRLRSG ERTDHVHLSG TPQHATAVIE DGESRSLSAV LTGNRLSVVY
     DEVQVDYLVA ADDGRIWLAG GGRTVAVEEV REAPVRPDDA HSGDAELTSP MPGSVVALGV
     ADGQRVAAGT VVVTVEAMKM EHALAAPVDG VVELLVAEGD QVKVGQPLAK VIADLTVEKE
     ES
//
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