ACCD_STAAC
ID ACCD_STAAC Reviewed; 285 AA.
AC Q5HF73;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=SACOL1748;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS), AND ZINC-BINDING.
RX PubMed=16460018; DOI=10.1021/bi0520479;
RA Bilder P., Lightle S., Bainbridge G., Ohren J., Finzel B., Sun F.,
RA Holley S., Al-Kassim L., Spessard C., Melnick M., Newcomer M.,
RA Waldrop G.L.;
RT "The structure of the carboxyltransferase component of acetyl-coA
RT carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.";
RL Biochemistry 45:1712-1722(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:0000305}.
CC -!- MISCELLANEOUS: It is not known from which strain the crystal structure
CC is derived.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; CP000046; AAW36851.1; -; Genomic_DNA.
DR RefSeq; WP_000471571.1; NC_002951.2.
DR PDB; 2F9I; X-ray; 1.98 A; B/D=1-285.
DR PDBsum; 2F9I; -.
DR AlphaFoldDB; Q5HF73; -.
DR SMR; Q5HF73; -.
DR EnsemblBacteria; AAW36851; AAW36851; SACOL1748.
DR KEGG; sac:SACOL1748; -.
DR HOGENOM; CLU_015486_1_0_9; -.
DR OMA; PEGLWIK; -.
DR UniPathway; UPA00655; UER00711.
DR EvolutionaryTrace; Q5HF73; -.
DR Proteomes; UP000000530; 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; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..285
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /id="PRO_0000389848"
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 28..32
FT /evidence="ECO:0007829|PDB:2F9I"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:2F9I"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2F9I"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:2F9I"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 173..192
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:2F9I"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:2F9I"
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
