Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Biotin carboxylase

Gene

accC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 activityi

ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine.
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA), Biotin carboxylase (accC)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei116ATPBy similarity1
Binding sitei201ATPBy similarity1
Binding sitei236ATPBy similarity1
Active sitei292Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-4962-MONOMER
UniPathwayiUPA00655; UER00711

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A (EC:6.4.1.2)
Short name:
ACC
Gene namesi
Name:accC
Synonyms:fabG
Ordered Locus Names:PA4848
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi

Organism-specific databases

PseudoCAPiPA4848

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467941 – 449Biotin carboxylaseAdd BLAST449

Proteomic databases

PaxDbiP37798
PRIDEiP37798

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi208964.PA4848

Structurei

Secondary structure

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi11 – 23Combined sources13
Beta strandi27 – 33Combined sources7
Helixi34 – 36Combined sources3
Helixi40 – 44Combined sources5
Beta strandi45 – 52Combined sources8
Helixi56 – 58Combined sources3
Turni59 – 61Combined sources3
Helixi63 – 73Combined sources11
Beta strandi76 – 79Combined sources4
Turni84 – 87Combined sources4
Helixi89 – 97Combined sources9
Beta strandi101 – 105Combined sources5
Helixi107 – 114Combined sources8
Helixi116 – 125Combined sources10
Beta strandi135 – 137Combined sources3
Helixi142 – 152Combined sources11
Beta strandi154 – 160Combined sources7
Beta strandi168 – 174Combined sources7
Helixi175 – 177Combined sources3
Helixi178 – 193Combined sources16
Beta strandi198 – 202Combined sources5
Beta strandi208 – 220Combined sources13
Beta strandi222 – 229Combined sources8
Beta strandi240 – 244Combined sources5
Helixi250 – 267Combined sources18
Beta strandi270 – 280Combined sources11
Beta strandi283 – 290Combined sources8
Helixi297 – 304Combined sources8
Helixi308 – 316Combined sources9
Helixi325 – 327Combined sources3
Beta strandi332 – 342Combined sources11
Turni344 – 346Combined sources3
Beta strandi352 – 358Combined sources7
Beta strandi365 – 369Combined sources5
Beta strandi375 – 377Combined sources3
Beta strandi379 – 381Combined sources3
Beta strandi383 – 394Combined sources12
Helixi395 – 408Combined sources14
Beta strandi410 – 412Combined sources3
Helixi418 – 424Combined sources7
Helixi428 – 432Combined sources5
Helixi439 – 444Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C00X-ray2.50A/B1-449[»]
2VQDX-ray2.41A1-449[»]
ProteinModelPortaliP37798
SMRiP37798
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37798

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 445Biotin carboxylationAdd BLAST445
Domaini120 – 317ATP-graspPROSITE-ProRule annotationAdd BLAST198

Phylogenomic databases

eggNOGiENOG4105CER Bacteria
COG0439 LUCA
HOGENOMiHOG000008988
InParanoidiP37798
KOiK01961
OMAiDYDPMLA
PhylomeDBiP37798

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR004549 Acetyl_CoA_COase_biotin_COase
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
PfamiView protein in Pfam
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF02786 CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
TIGRFAMsiTIGR00514 accC, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

P37798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEKVLIANR GEIALRILRA CKELGIKTVA VHSTADRELM HLSLADESVC
60 70 80 90 100
IGPAPATQSY LQIPAIIAAA EVTGATAIHP GYGFLAENAD FAEQIERSGF
110 120 130 140 150
TFVGPTAEVI RLMGDKVSAK DAMKRAGVPT VPGSDGPLPE DEETALAIAR
160 170 180 190 200
EVGYPVIIKA AGGGGGRGMR VVYDESELIK SAKLTRTEAG AAFGNPMVYL
210 220 230 240 250
EKFLTNPRHV EVQVLSDGQG NAIHLGDRDC SLQRRHQKVI EEAPAPGIDE
260 270 280 290 300
KARQEVFARC VQACIEIGYR GAGTFEFLYE NGRFYFIEMN TRVQVEHPVS
310 320 330 340 350
EMVTGVDIVK EMLRIASGEK LSIRQEDVVI RGHALECRIN AEDPKTFMPS
360 370 380 390 400
PGKVKHFHAP GGNGVRVDSH LYSGYSVPPN YDSLVGKVIT YGADRDEALA
410 420 430 440
RMRNALDELI VDGIKTNTEL HKDLVRDAAF CKGGVNIHYL EKKLGMDKH
Length:449
Mass (Da):48,888
Last modified:October 1, 1994 - v1
Checksum:i3B04C77785C73541
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14612 Unassigned DNA Translation: AAA16041.1
AE004091 Genomic DNA Translation: AAG08233.1
PIRiB49342
RefSeqiNP_253535.1, NC_002516.2
WP_003095391.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG08233; AAG08233; PA4848
GeneIDi879558
KEGGipae:PA4848
PATRICifig|208964.12.peg.5080

Entry informationi

Entry nameiACCC_PSEAE
AccessioniPrimary (citable) accession number: P37798
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 25, 2018
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health