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ACCA_STAA8
ID   ACCA_STAA8              Reviewed;         314 AA.
AC   Q2FXM7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=SAOUHSC_01808;
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       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; CP000253; ABD30876.1; -; Genomic_DNA.
DR   RefSeq; WP_000883645.1; NZ_LS483365.1.
DR   RefSeq; YP_500313.1; NC_007795.1.
DR   PDB; 5KDR; X-ray; 2.60 A; A=1-314.
DR   PDBsum; 5KDR; -.
DR   AlphaFoldDB; Q2FXM7; -.
DR   SMR; Q2FXM7; -.
DR   STRING; 1280.SAXN108_1728; -.
DR   EnsemblBacteria; ABD30876; ABD30876; SAOUHSC_01808.
DR   GeneID; 3919278; -.
DR   KEGG; sao:SAOUHSC_01808; -.
DR   PATRIC; fig|93061.5.peg.1648; -.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_0_2_9; -.
DR   OMA; TPWQRVQ; -.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:Q2FXM7; -.
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: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; Reference proteome; Transferase.
FT   CHAIN           1..314
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT                   /id="PRO_1000062679"
FT   DOMAIN          32..289
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   HELIX           6..15
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           32..49
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           53..60
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           68..75
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          104..111
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           117..123
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           130..146
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          150..159
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           163..167
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           170..182
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          188..197
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           198..202
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          208..213
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          219..221
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           223..229
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           248..253
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   STRAND          256..261
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           272..289
FT                   /evidence="ECO:0007829|PDB:5KDR"
FT   HELIX           295..307
FT                   /evidence="ECO:0007829|PDB:5KDR"
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
 
 
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