ACCD_STAA8
ID ACCD_STAA8 Reviewed; 285 AA.
AC Q2FXM6;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=SAOUHSC_01809;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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:0000255|HAMAP-Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; CP000253; ABD30877.1; -; Genomic_DNA.
DR RefSeq; WP_000471571.1; NZ_LS483365.1.
DR RefSeq; YP_500314.1; NC_007795.1.
DR PDB; 5KDR; X-ray; 2.60 A; B=1-285.
DR PDBsum; 5KDR; -.
DR AlphaFoldDB; Q2FXM6; -.
DR SMR; Q2FXM6; -.
DR STRING; 1280.SAXN108_1729; -.
DR EnsemblBacteria; ABD30877; ABD30877; SAOUHSC_01809.
DR GeneID; 3919279; -.
DR KEGG; sao:SAOUHSC_01809; -.
DR PATRIC; fig|93061.5.peg.1649; -.
DR eggNOG; COG0777; Bacteria.
DR HOGENOM; CLU_015486_1_0_9; -.
DR OMA; PEGLWIK; -.
DR UniPathway; UPA00655; UER00711.
DR PRO; PR:Q2FXM6; -.
DR Proteomes; UP000008816; 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 InterPro; IPR041010; Znf-ACC.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF17848; zf-ACC; 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 3D-structure; ATP-binding; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..285
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /id="PRO_0000389857"
FT DOMAIN 29..285
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 33..55
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 52
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 STRAND 30..32
FT /evidence="ECO:0007829|PDB:5KDR"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:5KDR"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5KDR"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 139..155
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 173..192
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:5KDR"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5KDR"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5KDR"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:5KDR"
SQ SEQUENCE 285 AA; 31872 MW; 57E99BA3BF626CC5 CRC64;
MFKDFFNRTK KKKYLTVQDS KNNDVPAGIM TKCPKCKKIM YTKELAENLN VCFNCDHHIA
LTAYKRIEAI SDEGSFTEFD KGMTSANPLD FPSYLEKIEK DQQKTGLKEA VVTGTAQLDG
MKFGVAVMDS RFRMGSMGSV IGEKICRIID YCTENRLPFI LFSASGGARM QEGIISLMQM
GKTSVSLKRH SDAGLLYISY LTHPTTGGVS ASFASVGDIN LSEPKALIGF AGRRVIEQTI
NEKLPDDFQT AEFLLEHGQL DKVVHRNDMR QTLSEILKIH QEVTK
