ID A0A0T5ZLF4_9CHLR Unreviewed; 528 AA.
AC A0A0T5ZLF4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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; Chloroflexota.
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 with
RT 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 EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {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 AlphaFoldDB; A0A0T5ZLF4; -.
DR STRING; 1640513.XU10_C0009G0041; -.
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 Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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 PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRT63594.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 7..462
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 493..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-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
//
