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Q54J08

- ACAC_DICDI

UniProt

Q54J08 - ACAC_DICDI

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Protein

Acetyl-CoA carboxylase

Gene

accA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (By similarity).By similarity

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactori

Protein has several cofactor binding sites:
  • biotinBy similarityNote: Biotin.By similarity
  • Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi319 – 3191Manganese 1By similarity
Metal bindingi331 – 3311Manganese 1By similarity
Metal bindingi331 – 3311Manganese 2By similarity
Metal bindingi333 – 3331Manganese 2By similarity
Active sitei335 – 3351By similarity
Binding sitei1761 – 17611Coenzyme ABy similarity
Binding sitei2068 – 20681Coenzyme ABy similarity
Binding sitei2070 – 20701Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 25358ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: dictyBase
  2. ATP binding Source: UniProtKB-KW
  3. biotin carboxylase activity Source: dictyBase
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid biosynthetic process Source: dictyBase
  2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  3. nuclear envelope organization Source: dictyBase
  4. protein import into nucleus Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase (EC:6.4.1.2)
Alternative name(s):
ACC-alpha
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:accA
ORF Names:DDB_G0288387
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 5, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0288387. accA.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: dictyBase
  2. endoplasmic reticulum membrane Source: dictyBase
  3. mitochondrion Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22822282Acetyl-CoA carboxylasePRO_0000328220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei687 – 6871N6-biotinyllysineBy similarityPROSITE-ProRule annotation

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB_0230067.

Structurei

3D structure databases

ProteinModelPortaliQ54J08.
SMRiQ54J08. Positions 4-497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 515500Biotin carboxylationAdd
BLAST
Domaini170 – 360191ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini646 – 72075Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1639 – 2138500CarboxyltransferaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi82 – 854Poly-Asn
Compositional biasi210 – 2156Poly-Gly
Compositional biasi825 – 8317Poly-Asp
Compositional biasi943 – 9464Poly-Leu
Compositional biasi1012 – 10154Poly-Gln

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.CuratedPROSITE-ProRule annotation
Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

eggNOGiCOG0511.
InParanoidiQ54J08.
KOiK11262.
OMAiCERIEEN.
PhylomeDBiQ54J08.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProiIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q54J08-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIEINEYIKK LGGDKNIEKI LIANNGIAAV KAIRSVRKWA YTNFGNERAI
60 70 80 90 100
KFVVMATPED MKANAEYIRM ADQILQVPGG SNNNNYANVD IIVDFAERAG
110 120 130 140 150
VQAVWAGWGH ASENPRLPDL LSKTETGIVF IGPPAKAMAD LGDKIASTIV
160 170 180 190 200
AQSARVACVP WSGSGLKVDY SECNGVPSEI YGRACINSVE EARECAQRVG
210 220 230 240 250
FPAMIKASEG GGGKGIRKVT SMEDLESSFR QVQNEVPGSP IFFMKLVSNA
260 270 280 290 300
RHLEVQIVAD RHGEAISLNG RDCSVQRRHQ KIIEEGPAIA PTPQVWEEME
310 320 330 340 350
RAAVRLVKEV GYVGAGTVEY LFAEGEYYFL ELNPRLQVEH PVTEQITGVN
360 370 380 390 400
LPATQLQIAM GIPLHRIPDI RKLYGRTGDD LYGDSMIDLH DFTKRNPPAG
410 420 430 440 450
HCIAVRITGE NPDEGFKPTS GQIHELTFRS TPNIWGYFSV GAKGGLHEYA
460 470 480 490 500
DSQFGHIFAN GATREEARKT IILGLKEISI RGDIRTPVEY IIHLLESKDF
510 520 530 540 550
KENHIHTGWL DQLISEKIQT KKPETMIVVL CGAIYKASTI FSTKIQEFSN
560 570 580 590 600
QLSNGQLPSL ELLNNSLPIE LIYNNVKYQF EVSRTGINNY SVCLKNDKSA
610 620 630 640 650
VSIDSSVIML SDSGLLILLN GSTHVCYGRE DVIGLSLMID SKTCVFSQEY
660 670 680 690 700
DPSILRTSSP GKLVRYLVDD GSLVVKGTPF AEIEVMKMYM PLLVPEKGII
710 720 730 740 750
KFVLTEGSVM APGAIIANLE LSDQSSIQKS TVFTGSLTKM SPPTLIGNKP
760 770 780 790 800
HQLLNYTLGK ISNVLCGYES NDLNQLLNDT IKQLSNQKLP LFEFKEQLSI
810 820 830 840 850
VQSRIPQSLF KLINDELNKF EFNNDDDDED DSELFNSKNL QLSISLYLNK
860 870 880 890 900
LLLENEQLSI AIQLLIKPII LLAEKYNDGV SFAAINIFKN YLEEFIQIET
910 920 930 940 950
NLQNKNIQTV LKSIRPTYKD NISKVVDIAQ SLHPQSKKYK FILLLLNKIQ
960 970 980 990 1000
EQGLVCDFVE QFKKLSSLGG NCMEISLKAK HIMVHSQLPS NKQRSNDLIN
1010 1020 1030 1040 1050
SLKSILNVNN EQQQQVDEKV QDNKDEKISK LSKQTNEISD ILIPMFFNES
1060 1070 1080 1090 1100
NNDDDIRKLA MEVYVRHSYR SYYVEDTKVT LSNDEGSSGF SFIEWHFYIN
1110 1120 1130 1140 1150
LPQQSNLGGS NSGSPTYGSP LIRSISSSGG SSGGSGFQIS PRPSMSIFNG
1160 1170 1180 1190 1200
LSMLRTDSTD SLTAMEDQTK LRYGMMVFFE NEKKFEEKLP LILTRYNEEN
1210 1220 1230 1240 1250
NKKSQLSLSP NESTDILSVI ISIYPESISQ ENQAISSFQS ILKGYIKELS
1260 1270 1280 1290 1300
IARIRRITFI CCGGDEGKPL KYFTFRERHM YMEDPIFRHI EPAMAYHLEV
1310 1320 1330 1340 1350
RKLSNFDITH VPTTSQRIHL YYAQEKGKKE TDPDADRSFF VRSVIRYSDL
1360 1370 1380 1390 1400
YGHSNEIKVD ILLSQIETLL SESIESLEIA MSNKKYEKAQ NHSIFLNVMP
1410 1420 1430 1440 1450
EVMFDEKMIG YVVQEIGDRL GKRLWKLRVG RVEVRGRIRK GDGLIPVRFF
1460 1470 1480 1490 1500
VQNPTGYAFQ VQCYYEQQNS IGQMVFAVVP GSSKGSWEGL PVDTPYPIMD
1510 1520 1530 1540 1550
AVQRNRFKAQ RLDTTYCYDY PDLFREAMQN IWMEFMESNK TNPVKVYPSS
1560 1570 1580 1590 1600
RGVLESVELI LPSTINTDFP PSIPLDQLPE ESKPKLEETY RPIGYNDIGM
1610 1620 1630 1640 1650
VAWRMTFYTP EYPLGRQAIV IANDITHQIG SFGPQEDMLF KLASELARKE
1660 1670 1680 1690 1700
KIPRIYLSSN SGARIGLADE IKSKFKVTWN VPSDPTKGIK NLYLTNNDYQ
1710 1720 1730 1740 1750
ALKDSVIAYQ DTTDKDKWII HDIIGQKNGI GVENLSWSGL IAGETSQAYN
1760 1770 1780 1790 1800
EIFTITLVSG RSVGIGAYLV RLGQRTIQND APIILTGASA LNKVLGKEVY
1810 1820 1830 1840 1850
ESNQQLGGSQ IMYPNGVSHI IVNDELRGIT NVLQWLSFVP KSGGEMVPII
1860 1870 1880 1890 1900
SPIDSPHRDI EFDPSNSING KCDTRHLIAG LQSELDPNYW ISGMFDKDSF
1910 1920 1930 1940 1950
METLAGWANT VITGRARLGG IPVGIIAVET KSVEKIIPAD PANPLSYEQV
1960 1970 1980 1990 2000
NTQAGQVWYP DSSFKTAQAI ADFNNGEELP LMILANWRGF SGGMRDMFDE
2010 2020 2030 2040 2050
ILKFGSMIVD NLRNYKQPVM VYIPPFAELR GGAWVVLDST INLDMMEMYC
2060 2070 2080 2090 2100
SEEGRGGVLE PNGIAEIKYR DPELIKTMHR LDPKLIEWDK SIPIGVSVNG
2110 2120 2130 2140 2150
LDQSQKTIKS QIQQREKELL GIYQQIAIKF ADLHDTPGRM KAKGVIKQMV
2160 2170 2180 2190 2200
PWKSARSFFY DRIKRRLFEE DKLKLIDKSH PGLNRQSKLN LLETWIKQIL
2210 2220 2230 2240 2250
GNNQSVDYHQ NDKLISSTIE SNSHIINDKI IDLSKQYAIN QILNFVQSDS
2260 2270 2280
ESIVDGFQNL LPFISTQQKE FLFESLKKDL NK
Length:2,282
Mass (Da):256,735
Last modified:May 24, 2005 - v1
Checksum:iBDBEA99629EE1B2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000111 Genomic DNA. Translation: EAL63219.1.
RefSeqiXP_636722.1. XM_631630.1.

Genome annotation databases

EnsemblProtistsiDDB0230067; DDB0230067; DDB_G0288387.
GeneIDi8626599.
KEGGiddi:DDB_G0288387.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000111 Genomic DNA. Translation: EAL63219.1 .
RefSeqi XP_636722.1. XM_631630.1.

3D structure databases

ProteinModelPortali Q54J08.
SMRi Q54J08. Positions 4-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 44689.DDB_0230067.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi DDB0230067 ; DDB0230067 ; DDB_G0288387 .
GeneIDi 8626599.
KEGGi ddi:DDB_G0288387.

Organism-specific databases

dictyBasei DDB_G0288387. accA.

Phylogenomic databases

eggNOGi COG0511.
InParanoidi Q54J08.
KOi K11262.
OMAi CERIEEN.
PhylomeDBi Q54J08.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .

Miscellaneous databases

PROi Q54J08.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProi IPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view ]
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.

Entry informationi

Entry nameiACAC_DICDI
AccessioniPrimary (citable) accession number: Q54J08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: November 26, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3