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UniProtKB/Swiss-Prot entry P24182


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACCC_ECOLI
Primary accession number P24182
Secondary accession number Q2M8V9
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on February 1, 1994 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 97)
Name and origin of the protein
Protein name Biotin carboxylase
Synonyms EC 6.3.4.14
Acetyl-CoA carboxylase subunit A
ACC
EC 6.4.1.2
Gene name
Name: accC
Synonyms: fabG
OrderedLocusNames: b3256, JW3224
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=K12;
PubMed=1682920 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A., Tsuru D., Anai M., Sekiguchi M., Tanabe T.;
"Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit.";
Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1370469 [NCBI, ExPASy, EBI, Israel, Japan]
Li S.-J., Cronan J.E. Jr.;
"The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase.";
J. Biol. Chem. 267:855-863(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Best E.A., Knauf V.C.;
"Cloning and characterization of the E. coli fabEG operon encoding subunits of acetyl-CoA carboxylase.";
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.
PubMed=2575489 [NCBI, ExPASy, EBI, Israel, Japan]
Alix J.-H.;
"A rapid procedure for cloning genes from lambda libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome.";
DNA 8:779-789(1989).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1021/bi00200a004; PubMed=7915138 [NCBI, ExPASy, EBI, Israel, Japan]
Waldrop G.L., Rayment I., Holden H.M.;
"Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase.";
Biochemistry 33:10249-10256(1994).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.
DOI=10.1074/jbc.275.21.16183; PubMed=10821865 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L.;
"Movement of the biotin carboxylase B-domain as a result of ATP binding.";
J. Biol. Chem. 275:16183-16190(2000).
[10]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF ARG-19; GLU-23; PHE-363 AND ARG-366.
DOI=10.1016/j.molcel.2006.04.026; PubMed=16793549 [NCBI, ExPASy, EBI, Israel, Japan]
Shen Y., Chou C.-Y., Chang G.-G., Tong L.;
"Is dimerization required for the catalytic activity of bacterial biotin carboxylase?";
Mol. Cell 22:807-818(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M79446; AAA23748.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M80458; AAA23409.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M83198; AAA23746.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58059.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76288.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77297.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32214; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR JS0632; JS0632.
RefSeq AP_003796.1; -.
NP_417722.1; -.
3D structure databases
PDB
1BNC; X-ray; 2.40 A; A/B=1-449.[ExPASy / RCSB / EBI]
1DV1; X-ray; 1.90 A; A/B=1-449.[ExPASy / RCSB / EBI]
1DV2; X-ray; 2.50 A; A/B=1-449.[ExPASy / RCSB / EBI]
1K69; Model; -; A=1-447.[ExPASy / RCSB / EBI]
2GPS; X-ray; 2.80 A; A/B=1-449.[ExPASy / RCSB / EBI]
2GPW; X-ray; 2.20 A; A/B/C/D=1-449.[ExPASy / RCSB / EBI]
2J9G; X-ray; 2.05 A; A/B=1-449.[ExPASy / RCSB / EBI]
2VR1; X-ray; 2.60 A; A/B=1-449.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BNC; -.
1DV1; -.
1DV2; -.
1K69; -.
2GPS; -.
2GPW; -.
2J9G; -.
2VR1; -.
ModBase P24182.
Protein-protein interaction databases
DIP DIP:9035N; -.
Enzyme and pathway databases
BioCyc EcoCyc:BIOTIN-CARBOXYL-MON; -.
MetaCyc:BIOTIN-CARBOXYL-MON; -.
Organism-specific databases
EchoBASE EB0272; -.
EcoGene EG10276; accC.
Ontologies
GO
GO:0003989; Molecular function: acetyl-CoA carboxylase activity (inferred from electronic annotation from EC).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0009374; Molecular function: biotin binding (inferred from electronic annotation from InterPro).
GO:0004075; Molecular function: biotin carboxylase activity (inferred from electronic annotation from EC).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004549; Acetyl_CoA_COase_biotin_COase.
IPR011761; ATP-grasp.
IPR013816; ATP_grasp_subdomain_2.
IPR011764; BC.
IPR005482; Biotin_COase_C.
IPR005479; CarbamoylP_synth_lsu_ATP-bd.
IPR005481; CarbamoylP_synth_lsu_N.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.
Gene3D G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
Pfam PF02785; Biotin_carb_C; 1.
PF00289; CPSase_L_chain; 1.
PF02786; CPSase_L_D2; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00514; accC; 1.
PROSITE PS50975; ATP_GRASP; 1.
PS50979; BC; 1.
PS00866; CPSASE_1; 1.
PS00867; CPSASE_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P24182.
Genome annotation databases
GeneID 947761; -.
GenomeReviews U00096_GR; b3256.
AP009048_GR; JW3224.
KEGG ecj:JW3224; -.
eco:b3256; -.
Phylogenomic databases
HOGENOM P24182; -.
Other
LinkHub P24182; -.
Genome annotation databases
CMR P24182; b3256.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Biotin; Complete proteome; Direct protein sequencing; Fatty acid biosynthesis; Ligase; Lipid synthesis; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   449  449     Biotin carboxylase. PRO_0000146791
DOMAIN   1   445  445     Biotin carboxylation. 
DOMAIN   120   317  198     ATP-grasp. 
ACT_SITE   292   292        Potential. 
BINDING   116   116        ATP. 
BINDING   201   201        ATP. 
BINDING   236   236        ATP. 
MUTAGEN   19    19        R->E: Loss of homodimerization. No effect on ATP binding. 
MUTAGEN   23    23        E->R: Loss of homodimerization. No effect on ATP binding. 
MUTAGEN   363   363        F->A: Loss of homodimerization. No effect on ATP binding. 
MUTAGEN   366   366        R->E: Loss of homodimerization. No effect on ATP binding. 
CONFLICT   136   136        G -> A (in Ref. 7). 
CONFLICT   160   160        A -> P (in Ref. 7). 
CONFLICT   260   261        CA -> SR (in Ref. 2). 
CONFLICT   313   313        L -> M (in Ref. 1; AAA23748). 
STRAND   4     7  4      
HELIX   11    23  13      
STRAND   27    33  7      
HELIX   34    36  3      
HELIX   40    44  5      
STRAND   46    52  7      
HELIX   56    58  3      
TURN   59    61  3      
HELIX   63    73  11      
STRAND   77    79  3      
STRAND   82    85  4      
HELIX   89    97  9      
STRAND   101   105  5      
HELIX   107   114  8      
HELIX   116   126  11      
HELIX   142   152  11      
STRAND   154   159  6      
HELIX   175   186  12      
TURN   187   189  3      
STRAND   198   202  5      
STRAND   208   220  13      
STRAND   222   229  8      
STRAND   233   236  4      
STRAND   240   244  5      
HELIX   250   266  17      
STRAND   270   280  11      
STRAND   283   292  10      
HELIX   297   304  8      
HELIX   308   316  9      
HELIX   325   327  3      
STRAND   332   342  11      
TURN   344   346  3      
STRAND   356   358  3      
STRAND   365   369  5      
STRAND   383   394  12      
HELIX   395   408  14      
STRAND   410   414  5      
HELIX   418   426  9      
HELIX   428   432  5      
HELIX   439   444  6      
Sequence information
Length: 449 AA [This is the length of the unprocessed precursor] Molecular weight: 49321 Da [This is the MW of the unprocessed precursor] CRC64: 68C55F10ACB4F170 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY 

        70         80         90        100        110        120 
LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI 

       130        140        150        160        170        180 
AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ 

       190        200        210        220        230        240 
SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV 

       250        260        270        280        290        300 
EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 

       310        320        330        340        350        360 
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP 

       370        380        390        400        410        420 
GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL 

       430        440 
QIRIMNDENF QHGGTNIHYL EKKLGLQEK 

P24182 in FASTA format

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