(data stored in SCRATCH zone)

SWISSPROT: Q13EF4_RHOPS

ID   Q13EF4_RHOPS            Unreviewed;       324 AA.
AC   Q13EF4;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS00176990};
DE            Short=ACCase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE            EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS01087405};
GN   Name=accA {ECO:0000256|HAMAP-Rule:MF_00823};
GN   OrderedLocusNames=RPD_0297 {ECO:0000313|EMBL:ABE37535.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37535.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37535.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37535.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
CC       complex. First, biotin carboxylase catalyzes the carboxylation of
CC       biotin on its carrier protein (BCCP) and then the CO(2) group is
CC       transferred by the carboxyltransferase to acetyl-CoA to form
CC       malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00177034}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] =
CC         malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:54728, Rhea:RHEA-COMP:10505, Rhea:RHEA-
CC         COMP:10506, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00823,
CC         ECO:0000256|SAAS:SAAS01122170};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00057363}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
CC       biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC)
CC       and two subunits each of ACCase subunit alpha (AccA) and ACCase
CC       subunit beta (AccD). {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00176983}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00231887}.
CC   -!- SIMILARITY: Belongs to the AccA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00823, ECO:0000256|SAAS:SAAS00588190}.
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DR   EMBL; CP000283; ABE37535.1; -; Genomic_DNA.
DR   STRING; 316057.RPD_0297; -.
DR   EnsemblBacteria; ABE37535; ABE37535; RPD_0297.
DR   KEGG; rpd:RPD_0297; -.
DR   eggNOG; ENOG4107QM9; Bacteria.
DR   eggNOG; COG0825; LUCA.
DR   HOGENOM; HOG000273832; -.
DR   KO; K01962; -.
DR   OMA; MFEHSVY; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001818; 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   3: Inferred from homology;
DR   PRODOM; Q13EF4.
DR   SWISS-2DPAGE; Q13EF4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00127049};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00177046};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00126967};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00127008};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00127050};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00126977};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00057352};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS01087435, ECO:0000313|EMBL:ABE37535.1}.
FT   DOMAIN       45    299       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000259|PROSITE:PS50989}.
SQ   SEQUENCE   324 AA;  34924 MW;  11ABDE5C85CC5828 CRC64;
     MSLVMSEPMR SYLDFEKPVA ELDSKIDELR TLAASGSDIH EEVSRIEEKA AQALNELYAA
     LTPWQKTQVA RHPQRPHCVD YIQGLITEFT PLAGDRKFGE DEALIGGFGR FRGESICVLG
     QEKGSSTETR LKHNFGMARP EGYRKAVRLM EMADRFGIPV LSLVDTAGAY PGIGAEERGQ
     AEAIARSTDA CLQLGVPNVA VVIGEGGSGG AIAIATANKV LMLEHAIYSV ISPEAASSIL
     WRDGTKAQEA ANSMKITAQD LLRFGVIDQI LAEPKGGAHR DPEAMIATTG DAIAAAFAEL
     NGLDSSTVRN KRRQKFLEIG RKLG
//

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