ID   ACCDA_AGARV             Reviewed;         589 AA.
AC   C4Z8P1;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha;
DE            Short=ACCase subunits beta/alpha;
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunits beta/alpha;
DE            EC=2.1.3.15;
GN   Name=accD; Synonyms=accA, accDA; OrderedLocusNames=EUBREC_3141;
OS   Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS   / VPI 0990) (Eubacterium rectale).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnospiraceae incertae sedis.
OX   NCBI_TaxID=515619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC   0990;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC       Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC       carrier protein (BCCP) and then the CO(2) group is transferred by the
CC       transcarboxylase to acetyl-CoA to form malonyl-CoA (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC         CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC         Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterotetramer composed of biotin
CC       carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC       subunits of ACCase subunit beta/alpha. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AccD/PCCB family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AccA family.
CC       {ECO:0000305}.
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; CP001107; ACR76868.1; -; Genomic_DNA.
DR   RefSeq; WP_012743895.1; NC_012781.1.
DR   AlphaFoldDB; C4Z8P1; -.
DR   SMR; C4Z8P1; -.
DR   STRING; 515619.EUBREC_3141; -.
DR   EnsemblBacteria; ACR76868; ACR76868; EUBREC_3141.
DR   KEGG; ere:EUBREC_3141; -.
DR   HOGENOM; CLU_015486_3_0_9; -.
DR   OMA; RNPTMGG; -.
DR   OrthoDB; 504557at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001477; Chromosome.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR   InterPro; IPR001095; Acetyl_CoA_COase_a_su.
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; PTHR42853; PTHR42853; 1.
DR   Pfam; PF03255; ACCA; 1.
DR   PRINTS; PR01069; ACCCTRFRASEA.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   TIGRFAMs; TIGR00513; accA; 1.
DR   TIGRFAMs; TIGR00515; accD; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..589
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunits beta/alpha"
FT                   /id="PRO_0000389900"
FT   DOMAIN          46..312
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          319..569
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   ZN_FING         50..72
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250"
FT   REGION          1..275
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta"
FT   REGION          16..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..569
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   REGION          276..589
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   589 AA;  65834 MW;  502DD49CBC0E04F6 CRC64;
     MMKLFKKKDK NIEAEETLAK NAESEKTAAD GKNAGVAQET KEDAPETIVC PKCGKTVLKS
     VVKQHKYVCY ECNYYFRVRA KNRIRMVSDK EAFEPWFTEL TTGNPLNFPE YEEKIAKTQE
     KTGLSEGIVI GKTKIYGEET VLGVIDSRFM MGSMGHVVGE KITSAFERAT EERLPVILFC
     CSGGARMQEG IISLMQMAKT SAAAKRHSEA GLLYVPVLTD PTTGGVTASF AMLGDIILAE
     PKALIGFAGP RVIEQTIGQK LPEGFQRAEF QLEHGFVDMI VEREDLKKTL YKILRAHRPT
     TGYANFDPLH SDDNYEPTEL MKEREAKAKP FKVWDKVSAA RQIKRLASVD YMDYIFDEFM
     ELHGDRYFRD DPAIVGGIAY LDGQPVTVIG VHKGKDLEDC AKRNYGMPSP EGYRKALRLM
     KQAEKFNRPI ITFVNTSGAY PGMEAEENGQ GEAIARNLYE MSGIKVPILC LMIGEGGSGG
     ALALSVGNEV WMMENATYSI LSPEGFASIL WKDGKRAKEA AEVMKITAHD LKELDVVDDI
     IPEFGGADED ALSSIGNYMK GNMKKFLEKE SKLTKDQLLE ERYKRFRKF