ACCD_STRPN
ID ACCD_STRPN Reviewed; 288 AA.
AC P0CC08; Q7D4F5; Q9FBB8;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; OrderedLocusNames=SP_0426;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP CHARACTERIZATION OF ACTIVITY REGULATION.
RC STRAIN=G9A;
RX PubMed=15066985; DOI=10.1074/jbc.m402989200;
RA Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J., Brands M.,
RA Raabe M., Haebich D., Ziegelbauer K.;
RT "Identification and characterization of the first class of potent bacterial
RT acetyl-CoA carboxylase inhibitors with antibacterial activity.";
RL J. Biol. Chem. 279:26066-26073(2004).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01395};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD). {ECO:0000255|HAMAP-Rule:MF_01395}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; AE005672; AAK74589.1; -; Genomic_DNA.
DR PIR; B97920; B97920.
DR PIR; D95049; D95049.
DR RefSeq; WP_001173353.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0CC08; -.
DR SMR; P0CC08; -.
DR STRING; 170187.SP_0426; -.
DR EnsemblBacteria; AAK74589; AAK74589; SP_0426.
DR GeneID; 60233944; -.
DR GeneID; 66805616; -.
DR KEGG; spn:SP_0426; -.
DR eggNOG; COG0777; Bacteria.
DR OMA; PEGLWIK; -.
DR PhylomeDB; P0CC08; -.
DR BioCyc; SPNE170187:G1FZB-441-MON; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000000585; 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_01395; AcetylCoA_CT_beta; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00515; accD; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..288
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /id="PRO_0000389871"
FT DOMAIN 33..288
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 37..58
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 288 AA; 31786 MW; 42C29A8FC7BF21D5 CRC64;
MALFSKKDKY IRINPNRSVR EKPQAKPEVP DELFSQCPGC KHTIYQKDLG SERICPHCSY
TFRISAQERL ALTIDMGTFK ELFTGIESKD PLHFPGYQKK LASMREKTGL HEAVVTGTAL
IKGQTVALGI MDSNFIMASM GTVVGEKITR LFEYATVEKL PVVLFTASGG ARMQEGIMSL
MQMAKISAAV KRHSNAGLFY LTILTDPTTG GVTASFAMEG DIILAEPQSL VGFAGRRVIE
NTVRESLPED FQKAEFLLEH GFVDAIVKRR DLPDTIASLV RLHGGSPR
