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Reviewed, UniProtKB/Swiss-Prot P37798 (ACCC_PSEAE)

Last modified November 3, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Biotin carboxylase
    EC=6.3.4.14
Alternative name(s):
    Acetyl-CoA carboxylase subunit A
      Short name=ACC
    EC=6.4.1.2
Gene names
Name: accC
Synonyms: fabG
Ordered Locus Names: PA4848
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA By similarity.

Catalytic activity

ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

Acetyl-CoA carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex By similarity.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Biotin carboxylase
PRO_0000146794

Regions

Domain1 – 445445Biotin carboxylation
Domain120 – 317198ATP-grasp

Sites

Active site2921 Potential
Binding site1161ATP By similarity
Binding site2011ATP By similarity
Binding site2361ATP By similarity

Secondary structure

1 ............................................................................... 449
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P37798-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 3B04C77785C73541

FASTA44948,888
        10         20         30         40         50         60 
MLEKVLIANR GEIALRILRA CKELGIKTVA VHSTADRELM HLSLADESVC IGPAPATQSY 

        70         80         90        100        110        120 
LQIPAIIAAA EVTGATAIHP GYGFLAENAD FAEQIERSGF TFVGPTAEVI RLMGDKVSAK 

       130        140        150        160        170        180 
DAMKRAGVPT VPGSDGPLPE DEETALAIAR EVGYPVIIKA AGGGGGRGMR VVYDESELIK 

       190        200        210        220        230        240 
SAKLTRTEAG AAFGNPMVYL EKFLTNPRHV EVQVLSDGQG NAIHLGDRDC SLQRRHQKVI 

       250        260        270        280        290        300 
EEAPAPGIDE KARQEVFARC VQACIEIGYR GAGTFEFLYE NGRFYFIEMN TRVQVEHPVS 

       310        320        330        340        350        360 
EMVTGVDIVK EMLRIASGEK LSIRQEDVVI RGHALECRIN AEDPKTFMPS PGKVKHFHAP 

       370        380        390        400        410        420 
GGNGVRVDSH LYSGYSVPPN YDSLVGKVIT YGADRDEALA RMRNALDELI VDGIKTNTEL 

       430        440 
HKDLVRDAAF CKGGVNIHYL EKKLGMDKH

« Hide

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References

« Hide 'large scale' references
[1]"Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase."
Best E.A., Knauf V.C.
J. Bacteriol. 175:6881-6889(1993) [PubMed: 7693652] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L14612 Unassigned DNA. Translation: AAA16041.1.
AE004091 Genomic DNA. Translation: AAG08233.1.
PIRB49342.
RefSeqNP_253535.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2C00X-ray2.50A/B1-449[»]
2VQDX-ray2.41A1-449[»]
ModBaseSearch...

Genome annotation databases

GeneID879558.
GenomeReviewsGene locus PA4848 in contig AE004091_GR.
KEGGpae:PA4848.

Organism-specific databases

PseudoCAPPA4848.
CMRSearch...

Phylogenomic databases

HOGENOMP37798.
OMAHIRLMGD.

Enzyme and pathway databases

BioCycPAER208964:PA4848-MON.
BRENDA6.3.4.14. 354.
6.4.1.2. 354.

Family and domain databases

InterProIPR004549. 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]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
PfamPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00514. accC. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameACCC_PSEAE
AccessionPrimary (citable) accession number: P37798
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 3, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents