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Reviewed, UniProtKB/Swiss-Prot O00763 (ACACB_HUMAN)

Last modified October 14, 2008. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Acetyl-CoA carboxylase 2
    EC=6.4.1.2
Alternative name(s):
    ACC-beta
Including the following 1 domains:
    1- Recommended name:
            Biotin carboxylase
              EC=6.3.4.14
Gene names
Name: ACACB
Synonyms: ACC2, ACCB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.

Catalytic activity

ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.

ATP + biotin-carboxyl-carrier protein + CO(2) = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.

Cofactor

Biotin By similarity.

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

Activated by citrate. Inhibited by malonyl-CoA.

Pathway

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

Subcellular location

Intracytoplasmic membrane. Note= May associate with membranes.

Tissue specificity

Predominantly expressed in the heart, skeletal muscles and liver.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Biophysicochemical properties

Kinetic parameters:

KM=120 µM for ATP

KM=58 µM for Acetyl-CoA

KM=3.0 mM for NaHCO(3)

Sequence caution

The sequence AAB58382.1 differs from that shown. Reason: Frameshift at several positions.

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Ontologies

Keywords

   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Biotin
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Multifunctional enzyme

Gene Ontology (GO)

   Biological processregulation of fatty acid oxidation

Inferred from Experiment. Source: Reactome

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: O00763-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: O00763-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1118-1187: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 24582458Acetyl-CoA carboxylase 2

Regions

Domain259 – 761503Biotin carboxylation
Domain414 – 609196ATP-grasp
Domain895 – 96167Biotinyl-binding
Domain1809 – 2305497Carboxyltransferase
Nucleotide binding458 – 4636ATP Potential

Sites

Active site5841 By similarity
Metal binding5671Manganese 1 By similarity
Metal binding5801Manganese 1 By similarity
Metal binding5801Manganese 2 By similarity
Metal binding5821Manganese 2 By similarity
Binding site9291Biotin (covalent) By similarity
Binding site19341Coenzyme A By similarity
Binding site22381Coenzyme A By similarity
Binding site22401Coenzyme A By similarity

Amino acid modifications

Modified residue2201Phosphoserine By similarity
Modified residue2221Phosphoserine By similarity

Natural variations

Alternative sequence1118 – 118770Missing in isoform Short.
Natural variant5521I → V: dbSNP rs16940029.
Natural variant6511A → T: dbSNP rs2300455.
Natural variant21411I → V: dbSNP rs2075260.

Experimental info

Sequence conflict91C → R in ABF48723. Ref.2
Sequence conflict1201T → I in AAR37018. Ref.4
Sequence conflict4221I → T in AAR37018. Ref.4
Sequence conflict13401S → N in AAC50571. Ref.6
Sequence conflict13831D → G in AAC50571. Ref.6
Sequence conflict14251V → M in AAC50571. Ref.6
Sequence conflict1819 – 18213AEG → PEA in AAC50571. Ref.6
Sequence conflict1892 – 18932MI → IM in AAC50571. Ref.6

Secondary structure

1 ...................................................................................... 2458
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: E9E072A910B490A5

FASTA2,458276,555
        10         20         30         40         50         60 
MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR 

        70         80         90        100        110        120 
NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT 

       130        140        150        160        170        180 
GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV 

       190        200        210        220        230        240 
AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR 

       250        260        270        280        290        300 
DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT 

       310        320        330        340        350        360 
PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL 

       370        380        390        400        410        420 
PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK 

       430        440        450        460        470        480 
RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV 

       490        500        510        520        530        540 
QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP 

       550        560        570        580        590        600 
LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL 

       610        620        630        640        650        660 
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE 

       670        680        690        700        710        720 
GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA 

       730        740        750        760        770        780 
LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL 

       790        800        810        820        830        840 
NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM 

       850        860        870        880        890        900 
NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP 

       910        920        930        940        950        960 
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR 

       970        980        990       1000       1010       1020 
LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK 

      1030       1040       1050       1060       1070       1080 
LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP 

      1090       1100       1110       1120       1130       1140 
SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV 

      1150       1160       1170       1180       1190       1200 
EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD 

      1210       1220       1230       1240       1250       1260 
ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP 

      1270       1280       1290       1300       1310       1320 
ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV 

      1330       1340       1350       1360       1370       1380 
VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR 

      1390       1400       1410       1420       1430       1440 
NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP 

      1450       1460       1470       1480       1490       1500 
ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFT