ACCA_STAA3
ID ACCA_STAA3 Reviewed; 314 AA.
AC Q2FG38;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_00823};
GN Name=accA {ECO:0000255|HAMAP-Rule:MF_00823};
GN OrderedLocusNames=SAUSA300_1646;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC carboxyltransferase to acetyl-CoA to form malonyl-CoA.
CC {ECO:0000255|HAMAP-Rule:MF_00823}.
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_00823};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}.
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_00823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00823}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
CC Rule:MF_00823}.
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DR EMBL; CP000255; ABD21607.1; -; Genomic_DNA.
DR RefSeq; WP_000883645.1; NZ_CP027476.1.
DR PDB; 2F9I; X-ray; 1.98 A; A/C=1-314.
DR PDBsum; 2F9I; -.
DR AlphaFoldDB; Q2FG38; -.
DR SMR; Q2FG38; -.
DR PRIDE; Q2FG38; -.
DR EnsemblBacteria; ABD21607; ABD21607; SAUSA300_1646.
DR KEGG; saa:SAUSA300_1646; -.
DR HOGENOM; CLU_015486_0_2_9; -.
DR OMA; TPWQRVQ; -.
DR UniPathway; UPA00655; UER00711.
DR EvolutionaryTrace; Q2FG38; -.
DR Proteomes; UP000001939; 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: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 InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR PANTHER; PTHR42853; PTHR42853; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00513; accA; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..314
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /id="PRO_1000062678"
FT DOMAIN 32..289
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:2F9I"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 272..288
FT /evidence="ECO:0007829|PDB:2F9I"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:2F9I"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:2F9I"
SQ SEQUENCE 314 AA; 35070 MW; EC1C58F163948B0F CRC64;
MLDFEKPLFE IRNKIESLKE SQDKNDVDLQ EEIDMLEASL ERETKKIYTN LKPWDRVQIA
RLQERPTTLD YIPYIFDSFM ELHGDRNFRD DPAMIGGIGF LNGRAVTVIG QQRGKDTKDN
IYRNFGMAHP EGYRKALRLM KQAEKFNRPI FTFIDTKGAY PGKAAEERGQ SESIATNLIE
MASLKVPVIA IVIGEGGSGG ALGIGIANKV LMLENSTYSV ISPEGAAALL WKDSNLAKIA
AETMKITAHD IKQLGIIDDV ISEPLGGAHK DIEQQALAIK SAFVAQLDSL ESLSRDEIAN
DRFEKFRNIG SYIE
