ID   ACCDA_CLOTE             Reviewed;         575 AA.
AC   Q899N5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=CTC_00135;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
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DR   EMBL; AE015927; AAO34787.1; -; Genomic_DNA.
DR   RefSeq; WP_011098459.1; NC_004557.1.
DR   AlphaFoldDB; Q899N5; -.
DR   SMR; Q899N5; -.
DR   STRING; 212717.CTC_00135; -.
DR   PRIDE; Q899N5; -.
DR   EnsemblBacteria; AAO34787; AAO34787; CTC_00135.
DR   GeneID; 64180725; -.
DR   KEGG; ctc:CTC_00135; -.
DR   HOGENOM; CLU_015486_3_1_9; -.
DR   OMA; RNPTMGG; -.
DR   OrthoDB; 504557at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001412; 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   InterPro; IPR041010; Znf-ACC.
DR   PANTHER; PTHR42853; PTHR42853; 1.
DR   Pfam; PF03255; ACCA; 1.
DR   Pfam; PF17848; zf-ACC; 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..575
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunits beta/alpha"
FT                   /id="PRO_0000359113"
FT   DOMAIN          35..301
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          295..548
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   ZN_FING         39..61
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          1..264
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta"
FT   REGION          35..548
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   REGION          265..571
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   575 AA;  64630 MW;  2B90933F7C0DE945 CRC64;
     MFKRLFKKTK YITVSSHNLN EKDTTLEKPL IPDCMWSKCE KCGQIIYSKD LRKNHSICGF
     CKNHFRISAY DRVKQIIDEG TWAEMDKNLC SVNPLNFKGY NDKIEKAQEK TDLNEAVITG
     VGSIKGEKTV ICIMDSRFFM GSMGSVVGEK ITRSIEKSIE NRLPLVIFTA SGGARMQEGM
     FSLMQMAKIS AALSKLSQAG LLYITVLTDP TTGGVTASFA MLGDIILSEP GALIGFAGKR
     VIEQTINKKL PKGFQTAEFL MKHGFIDKIV NRKNLKDTLS MILKLHREKC EFKSYKDITV
     NKVNTLKNKL DAWGKLSMAR NEKRPTSLDY IDNIFENFME FHGDRYYGND SCIVGGIGIL
     DGVPVTIIAQ QKGRDLNENI ERNFGMPNPE GYRKALRLMK QAEKFNRPIV CFIDTPGAYC
     GVEAEQRGQG EAIAKNLINM ISLEVPIISI VIGEGGSGGA LALSVSDKIW MLENAVYSLL
     SPEGFASILW RDSTKAKEAA NIMKITSEDL KSYSLIDKIL YEPDRDASKN VKVMSNIIKN
     NLIKEFNNLM DLDRDELLNK RYNKFRVIGE YKNKT