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Database: UniProt
Entry: A0A239L0U8_9ACTN
LinkDB: A0A239L0U8_9ACTN
Original site: A0A239L0U8_9ACTN 
ID   A0A239L0U8_9ACTN        Unreviewed;      1817 AA.
AC   A0A239L0U8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 6.
DE   SubName: Full=Acetyl/propionyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:SNT24207.1};
GN   ORFNames=SAMN05443665_102093 {ECO:0000313|EMBL:SNT24207.1};
OS   Actinomadura meyerae.
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Actinomadura.
OX   NCBI_TaxID=240840 {ECO:0000313|EMBL:SNT24207.1, ECO:0000313|Proteomes:UP000198318};
RN   [1] {ECO:0000313|EMBL:SNT24207.1, ECO:0000313|Proteomes:UP000198318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44715 {ECO:0000313|EMBL:SNT24207.1,
RC   ECO:0000313|Proteomes:UP000198318};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZOR01000020; SNT24207.1; -; Genomic_DNA.
DR   BioCyc; GCF_900188445:CHF16_RS21105-MONOMER; -.
DR   Proteomes; UP000198318; Unassembled WGS sequence.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 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; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 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:UP000198318};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198318}.
FT   DOMAIN        1    451       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      125    322       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      571    654       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN     1535   1817       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000259|PROSITE:PS50989}.
SQ   SEQUENCE   1817 AA;  195332 MW;  F6785CA4F71F1970 CRC64;
     MFSRVAIVNR GEAAMRLIHA VRALAAETGA GIETVALHTD VDRTATFVRE ADLAYDLGPA
     AERPYLNPEV LERALVETGA DAAWVGWGFV AEDPAFAELC ERTGVTFVGP SAEAMRRLGD
     KIGAKLIAEE VGVPVAPWSR GAVETLDAAR EAAAGIGYPL MLKATAGGGG RGIRVINDEA
     ELADAYERTS QEAARAFGSG VVFLERLVTG ARHVEVQVIA DGETAWALGV RDCSVQRRNQ
     KVIEESASPV LRAEQAAELK ASAERLAVAV GYRGAATVEF LYHPGDELFA FLEVNTRLQV
     EHPITEAVTG FDLVRAQLHV AAGGRLEGPR PVERGHAVEA RLNAEDPDRD FAPAPGRIAR
     LDLPAGPGVR VDTGVREGDT IPADFDSMIA KIIAYGRDRD EALGRLRRAM AQTTVIIEGG
     ATNKSFVLDL LDRPEVVAAS ADTGWIDRER AAGGLVTSRH SAVALAAAAI EAYEEDERAA
     RRRLLSTASG GRPQVRHESG RPLDLKLRGA AYRVRVARVG ADRFRVAVEA GDDVRTADVE
     LDRFDRHTAQ ITVNGARYRL LTGTHGPVHL VEVDGVTHRV SRDEGGVVRS PAPALVVATP
     LEPGAEVEAG APVLVLESMK METVLRAPFK ARLKECVVSV GSQVETGAPL LRLEPLADAE
     AGDGAAAAAA ELDLPAAPAA VPAPERAARG REELRGLLLG FDVDPHDERR ALAGYLAARQ
     AAAAEGHRPL AEEIALLDVF ADLAELTRDR PAGGDGADGH VHSAREYFHT YLQSLDVERA
     GLPAAFQDRL AKALGHYGVT SLDRSPELEA AVFRIFLSRQ RASADAAVVS ALLRAWLREP
     PPVEALREPA GLALQRLINA AQVRFPVVYD LACGVVFAWY AQPMLRRDRA RVYADVRRHL
     RHLDAHPDSP DRADRIAEMV RSTEPLVRLL GRRLRRGDRD NAVMLEVLTR RYYGNKGLTG
     VRTAEAGGCS FVVAEREGSR LVSAAVSFDA LGGALAGLAG LATGGEVVDA DIYLSWENQP
     EDFEAMAEAL SGVLAEHPMP GGVRRITATV AGSSGAVMHH HFTFRPYGDG MAEERLIRGL
     HPHIAQRMRM ERLSGFDLTR LPSSDEEVYL FQCVARDNPS DDRLVAFAQV RDLTGLRDHD
     GRLLSLPTAE FIIATCLDSI RRAQERRPSK NRLPTNRIVI YVWPPSDLAR AELEMLVDRM
     LPTAAGAGLE EIEIIGRRRD PETGELLKRT VRIAFDAAGG TSLTVGEPSD DPVEPVDGYR
     QKVLRARSRN TVYPYELTAM LGDFTEHDLD AAHALVPVDR PAGRNTAAIV AGVVTTPTPR
     HPEGVTRVVL LGDPTKALGA LSEPECRRVI AALDLAERMR VPVEWYALSA GARISMESGT
     ENMDWVAAAL KRIVEFTQDG GEINVVVAGI NVGAQPYWNA EATMLMHTKG VLVMTPESAM
     VLTGKQALDF SGGVSAEDNL GIGGYDRVMG PNGQAQYWAP NLVAARDVLM AHYDHTYVVP
     GEDAPRRAAT TDPADRDVSD FPHIVEGSDF TTVGEIFSAA ANPDRKKPFD IRTVMRALSD
     QDHPVLERWA GMADADTAVV QDVHLGGIPV CLLGIESHAV PRRGFPPTDG PDSYTAGTLF
     PQSSKKAARA INAASGNRPL VVLANLSGFD GSPESLRKLQ LEYGAEIGRA IVNFRGPIVF
     CVISRYHGGA FVVFSKALNP NMTVLALEGS FASVLGGAPA AAAVFSRDVD ARTAADPRVR
     ALEPRVAAAT GADRAALIAE LDELRASVRA EKLGEVAAEF DRVHDIRRAV EVGSVDAVIP
     AAELRPRIIE AIESRLK
//
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