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ACCA_ACIF5
ID   ACCA_ACIF5              Reviewed;         316 AA.
AC   B5EQR6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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}; OrderedLocusNames=Lferr_1178;
OS   Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS   (Leptospirillum ferrooxidans (ATCC 53993)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53993 / BNL-5-31;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Borole A.P.;
RT   "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001132; ACH83416.1; -; Genomic_DNA.
DR   RefSeq; WP_012536536.1; NC_011206.1.
DR   AlphaFoldDB; B5EQR6; -.
DR   SMR; B5EQR6; -.
DR   GeneID; 66432451; -.
DR   KEGG; afe:Lferr_1178; -.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_0_2_6; -.
DR   OMA; TPWQRVQ; -.
DR   UniPathway; UPA00655; UER00711.
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;
KW   ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Transferase.
FT   CHAIN           1..316
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT                   /id="PRO_1000148727"
FT   DOMAIN          40..290
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   316 AA;  34693 MW;  F9007B3A4B0A7D70 CRC64;
     MKISYLDFEQ SVAELDAKVE ELHALNQPGI ADDISRLEVK ARKELQRIYS KLGAWQTVQV
     ARHPQRPYTM DYVQALFTEV QVLAGDRAFA DDQAIIGGLA RFNGQPIVWM GHQKGRDTKE
     KIQRNFGMPR PEGYRKALRL LRLAERFALP VFTFIDTPGA YPGIGAEERG QSEAIARNLA
     VMSDLAVPII CTVIGEGGSG GALAIGVGDR MLMLEYGVYS VISPEGCASI LWKNAAMAAE
     AAETLGITAR RLQGMGLVDE VLAEPLGGAH RDPEAVFALA RERFAHHLQE LQAMDTSKLL
     TTRYERLMHY GVVGAA
 
 
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