ACCDA_NATTJ
ID ACCDA_NATTJ Reviewed; 605 AA.
AC B2A865;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Nther_0846;
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001034; ACB84431.1; -; Genomic_DNA.
DR RefSeq; WP_012447309.1; NC_010718.1.
DR AlphaFoldDB; B2A865; -.
DR SMR; B2A865; -.
DR STRING; 457570.Nther_0846; -.
DR PRIDE; B2A865; -.
DR EnsemblBacteria; ACB84431; ACB84431; Nther_0846.
DR KEGG; nth:Nther_0846; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_3_1_9; -.
DR OMA; RNPTMGG; -.
DR OrthoDB; 504557at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001683; 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..605
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunits beta/alpha"
FT /id="PRO_0000359115"
FT DOMAIN 40..306
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 317..570
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT ZN_FING 44..66
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..269
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /evidence="ECO:0000250"
FT REGION 40..570
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 270..593
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 605 AA; 67608 MW; E146C7C08BE9153C CRC64;
MFKGLFKKTK YISLNPERKT ELRSDQNDNK SNKPHIPDGL WEKCDSCKSI IYAEDLKKNY
HICHECGHHF RIGAQERINQ IIDEDTWVEL DQNIISENPL EFEGYSEKVD KLQKKTELKE
AILTGLGKIN GQQAVIGAMD SRFLMGSMGS VVGEKVTRAI ETGIDENLPV IMFTASGGAR
MQEGIYSLMQ MAKTSAAISK LKDKGLPYIV VLTDPTTGGV TASFAMLGDI ILAEPNALIG
FAGKRVIEQT IKQKLPKEFQ RAEFLLKHGF VDKVINRKEM RNKLSHILKL HKTKQPSRML
DGNDCSYYSS KDASKKASAK SVEEIRQQGK KLTPYDKVKL VRSKERPTSL DYIDNIFEGF
IEFHGDRYFA DDTSIVGGLA FLNGLPVTVI GQQKGRDLQE NIYRNFGMPN PEGYRKAVRL
MQQAEKFNRP IINFVDTSGA GCGKGAEERG QGEAIAQNLY TMSSLKVPII SLVIGEGGSG
GALALTVADE VWMLENSVYS IVSPEGFASI LWKDSSKAKE AADVMKITAQ DLQELQIIDK
ILEEPYQDAS KDGQAMSEII KNNLLKTLDN LSKKETNDLL TKRYEKFRSI GRFIEKSNLD
SSINQ
