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Database: UniProt
Entry: A0A1W7CVD4_9ACTN
LinkDB: A0A1W7CVD4_9ACTN
Original site: A0A1W7CVD4_9ACTN 
ID   A0A1W7CVD4_9ACTN        Unreviewed;       677 AA.
AC   A0A1W7CVD4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-FEB-2019, entry version 8.
DE   SubName: Full=Acetyl/propionyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:ARQ68702.1};
GN   ORFNames=CAG99_07410 {ECO:0000313|EMBL:ARQ68702.1};
OS   Streptomyces sp. SCSIO 03032.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1109743 {ECO:0000313|EMBL:ARQ68702.1, ECO:0000313|Proteomes:UP000194218};
RN   [1] {ECO:0000313|EMBL:ARQ68702.1, ECO:0000313|Proteomes:UP000194218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ68702.1,
RC   ECO:0000313|Proteomes:UP000194218};
RA   Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT   "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT   diverse biosynthetic pathways for its bioactive secondary
RT   metabolites.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP021121; ARQ68702.1; -; Genomic_DNA.
DR   BioCyc; GCF_002128305:CAG99_RS07405-MONOMER; -.
DR   Proteomes; UP000194218; Chromosome.
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; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000194218};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194218}.
FT   DOMAIN        1    452       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    314       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      593    671       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   677 AA;  70163 MW;  9E80B9BE6F29044C CRC64;
     MFDTVLVANR GEIAVRVIRT LRRLGIASAA VYSDADAGAR HVAEADMAVR IGPERAAHSY
     LSVPALLRAA ERTGADAVHP GYGFLAENAD FARAVTAAGL TFIGPPADAI ETMGDKIRAK
     ETVRAAGVPV VPGAHGEGLA DAVRAMGPPV LLKPSAGGGG KGMRLVRDPA RLDDEIEAAR
     REAKAAFDDD TLLAERWIDR PRHIEIQVLA DRHGTVVHLG ERECSLQRRH QKIVEEAPSP
     LLDPATRAAM GEAAVRAARA CGYVGAGTVE FIVPAGDRAA YCFMEMNTRL QVEHPVTELI
     TGLDLVEWQV RVAAGEPLPF GQDGVPAARG HAVEARVCAE TATPAPGGGG AVAFLPSAGT
     VRLLREPSGE GVRVDSGLAE GTEVGTAYDP MLAKVVAHGP DRATALRRLR AALARTTVLG
     VDTNTGFLRR LLAHPAVLAG DFDTGLVAEA AAGLLAGPVP DEVYAAVALL RQEALRPAPD
     ATGWVDPFAV PSGWRLGEPP AWTTHRLRVA GQEPVAVAVR PGEVRVGTGP PLPARLLGTG
     ADAGADATGE RATVRVACAG AVHTFAHAVD SGGHWLGRDG DAWHVRGHDP VAAARAGAAT
     GRDELSAPMP GTVTVVKAAV GDAVRAGQGL LVVEAMKMEH VIAAPHDGTV TELKVTAGTA
     VAIDQVLVRV APGEEAR
//
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