ID   E6Q0Z3_9ZZZZ            Unreviewed;       517 AA.
AC   E6Q0Z3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Putative acyl-CoA carboxylase {ECO:0000313|EMBL:CBI00853.1};
GN   Name=yqjD {ECO:0000313|EMBL:CBI00853.1};
GN   ORFNames=CARN4_0200 {ECO:0000313|EMBL:CBI00853.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI00853.1};
RN   [1] {ECO:0000313|EMBL:CBI00853.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) 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:CBI00853.1}.
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DR   EMBL; CABO01000006; CBI00853.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6Q0Z3; -.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR   PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
FT   DOMAIN          1..260
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          258..510
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          13..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  56294 MW;  46B90DDBE938068B CRC64;
     MKTTQEKYAD LAHRRALARK PTGDEGIERQ HARGKRSARE RVEALVDPES FHELDAFVTH
     RTTAFGLDER EFLGDGVITG HATIAGRPVF LFSQDFSVLG GSLGEAFAEK ICKVMDLAVR
     TGAPMIGIND SGGARIQEGV VSLGGYAEIF WRNVQASGVI PQLSLIAGPC AGGAVYSPAI
     TDFTIMTQDI SQMFITGPEI IKTVTGEEVT FEELGGARTH AQKSGVAHLV AHDEEDLVAQ
     THELLSFLPQ NNLEDPPRFD SDDDAQREAP ELDALIPDSP NKPYDMHDVL RAVLDDGNFF
     EIHPEYARNI IVGFGRIDGR SIGIVANQPS VLAGVLDIKS SIKAARFVRT CDAFNIPLLT
     FEDVPGFLPG TEQEYGGIIL HGAKLLYAYA EATVPKITII TRKAYGGAYD VMASKHIRAD
     INLAWPSAEI AVMGAEGAVK TIFRREIAAA SDPAAKMAEL IDEYTDRFAN PYIAAQRGYI
     DDVIEARSTR RAVAAALAML ENKRVERPKR KHGNIPL
//