GenomeNet

Database: UniProt
Entry: A0A0T5ZLF4_9CHLR
LinkDB: A0A0T5ZLF4_9CHLR
Original site: A0A0T5ZLF4_9CHLR 
ID   A0A0T5ZLF4_9CHLR        Unreviewed;       528 AA.
AC   A0A0T5ZLF4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   31-JUL-2019, entry version 12.
DE   SubName: Full=Acetyl-CoA carboxylase alpha subunit acca {ECO:0000313|EMBL:KRT63594.1};
DE            EC=6.3.4.14 {ECO:0000313|EMBL:KRT63594.1};
GN   Name=accA {ECO:0000313|EMBL:KRT63594.1};
GN   ORFNames=XU10_C0009G0041 {ECO:0000313|EMBL:KRT63594.1};
OS   Chloroflexi bacterium CSP1-4.
OC   Bacteria; Chloroflexi.
OX   NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63594.1, ECO:0000313|Proteomes:UP000051896};
RN   [1] {ECO:0000313|EMBL:KRT63594.1, ECO:0000313|Proteomes:UP000051896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63594.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated
RT   with bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) 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:KRT63594.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LDXM01000009; KRT63594.1; -; Genomic_DNA.
DR   PATRIC; fig|1640513.3.peg.1050; -.
DR   Proteomes; UP000051896; 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; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 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:UP000051896};
KW   Ligase {ECO:0000313|EMBL:KRT63594.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN        7    462       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      126    328       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      493    514       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   528 AA;  55961 MW;  5D80A3F87E91C4A6 CRC64;
     MRKDGRPFRR ILIANRGEIA LRLIRACREM GIESVAVFSD VDAGMRHVRA ADQAVRIGPA
     PAAESYLVVE RIVEAALSTG AEAIHPGYGF LSERPALAEA CVAAGIVFIG PEPATLHGLG
     DKLNARRAAS AVGVPVVPGT LEPAPVDRPD AAASIVAEAE RIGFPVLVKA AAGGGGRGMR
     LVERAADLPA ALVAASHEAE AAFGDGSVYL ERRIDRARHV EVQLLGDAHG AVVALGERDC
     SVQRRHQKLV EEAPAPGFDE ARRRELHALG VSVARAVGLR NAATAEFLVA PDGAAWFLEV
     NARLQVEHGV TELVSGLDLV HEQLRIAAGE PLRDRVLAAA EAAATPDRHA IEVRLSAEDP
     ARGFAPVPGT VGRWRPPGGP GVRMDDWIED GTRVGGDYDP LLAKLLVVAE DRDMALARLA
     RALDELVVTG IQTTVPFDRW LVDEPHFRAG DLSTDFVPDH WDPAPVRTEA AHRAARLAAE
     AWAAGLAAPS RPTLAGTSPA VGVPADDADG RSGWLASGRR EVVDRWPR
//
DBGET integrated database retrieval system