Reviewed, UniProtKB/Swiss-Prot Q54J08 (ACAC_DICDI)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA carboxylase
    EC=6.4.1.2
Alternative name(s):
    ACC-alpha
Including the following 1 domains:
    1- Recommended name:
            Biotin carboxylase
              EC=6.3.4.14

Gene names

Name:	accA
ORF Names:	DDB_G0288387

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	2282 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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.
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
Cofactor	Biotin By similarity. Binds 2 manganese ions per subunit By similarity.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Biotin Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: EC biotin binding Inferred from electronic annotation. Source: InterPro biotin carboxylase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2282	2282	Acetyl-CoA carboxylase		PRO_0000328220
Regions
	Domain	16 – 515	500	Biotin carboxylation
	Domain	647 – 719	73	Biotinyl-binding
	Domain	1639 – 2138	500	Carboxyltransferase
	Nucleotide binding	196 – 253	58	ATP By similarity
	Compositional bias	82 – 85	4	Poly-Asn
	Compositional bias	210 – 215	6	Poly-Gly
	Compositional bias	825 – 831	7	Poly-Asp
	Compositional bias	943 – 946	4	Poly-Leu
	Compositional bias	1012 – 1015	4	Poly-Gln
Sites
	Active site	335	1	By similarity
	Metal binding	319	1	Manganese 1 By similarity
	Metal binding	331	1	Manganese 1 By similarity
	Metal binding	331	1	Manganese 2 By similarity
	Metal binding	333	1	Manganese 2 By similarity
	Binding site	1761	1	Coenzyme A By similarity
	Binding site	2068	1	Coenzyme A By similarity
	Binding site	2070	1	Coenzyme A By similarity
Amino acid modifications
	Modified residue	687	1	N6-biotinyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54J08-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: BDBEA99629EE1B2B	FASTA	2,282	256,735
	10 20 30 40 50 60 MIEINEYIKK LGGDKNIEKI LIANNGIAAV KAIRSVRKWA YTNFGNERAI KFVVMATPED 70 80 90 100 110 120 MKANAEYIRM ADQILQVPGG SNNNNYANVD IIVDFAERAG VQAVWAGWGH ASENPRLPDL 130 140 150 160 170 180 LSKTETGIVF IGPPAKAMAD LGDKIASTIV AQSARVACVP WSGSGLKVDY SECNGVPSEI 190 200 210 220 230 240 YGRACINSVE EARECAQRVG FPAMIKASEG GGGKGIRKVT SMEDLESSFR QVQNEVPGSP 250 260 270 280 290 300 IFFMKLVSNA RHLEVQIVAD RHGEAISLNG RDCSVQRRHQ KIIEEGPAIA PTPQVWEEME 310 320 330 340 350 360 RAAVRLVKEV GYVGAGTVEY LFAEGEYYFL ELNPRLQVEH PVTEQITGVN LPATQLQIAM 370 380 390 400 410 420 GIPLHRIPDI RKLYGRTGDD LYGDSMIDLH DFTKRNPPAG HCIAVRITGE NPDEGFKPTS 430 440 450 460 470 480 GQIHELTFRS TPNIWGYFSV GAKGGLHEYA DSQFGHIFAN GATREEARKT IILGLKEISI 490 500 510 520 530 540 RGDIRTPVEY IIHLLESKDF KENHIHTGWL DQLISEKIQT KKPETMIVVL CGAIYKASTI 550 560 570 580 590 600 FSTKIQEFSN QLSNGQLPSL ELLNNSLPIE LIYNNVKYQF EVSRTGINNY SVCLKNDKSA 610 620 630 640 650 660 VSIDSSVIML SDSGLLILLN GSTHVCYGRE DVIGLSLMID SKTCVFSQEY DPSILRTSSP 670 680 690 700 710 720 GKLVRYLVDD GSLVVKGTPF AEIEVMKMYM PLLVPEKGII KFVLTEGSVM APGAIIANLE 730 740 750 760 770 780 LSDQSSIQKS TVFTGSLTKM SPPTLIGNKP HQLLNYTLGK ISNVLCGYES NDLNQLLNDT 790 800 810 820 830 840 IKQLSNQKLP LFEFKEQLSI VQSRIPQSLF KLINDELNKF EFNNDDDDED DSELFNSKNL 850 860 870 880 890 900 QLSISLYLNK LLLENEQLSI AIQLLIKPII LLAEKYNDGV SFAAINIFKN YLEEFIQIET 910 920 930 940 950 960 NLQNKNIQTV LKSIRPTYKD NISKVVDIAQ SLHPQSKKYK FILLLLNKIQ EQGLVCDFVE 970 980 990 1000 1010 1020 QFKKLSSLGG NCMEISLKAK HIMVHSQLPS NKQRSNDLIN SLKSILNVNN EQQQQVDEKV 1030 1040 1050 1060 1070 1080 QDNKDEKISK LSKQTNEISD ILIPMFFNES NNDDDIRKLA MEVYVRHSYR SYYVEDTKVT 1090 1100 1110 1120 1130 1140 LSNDEGSSGF SFIEWHFYIN LPQQSNLGGS NSGSPTYGSP LIRSISSSGG SSGGSGFQIS 1150 1160 1170 1180 1190 1200 PRPSMSIFNG LSMLRTDSTD SLTAMEDQTK LRYGMMVFFE NEKKFEEKLP LILTRYNEEN 1210 1220 1230 1240 1250 1260 NKKSQLSLSP NESTDILSVI ISIYPESISQ ENQAISSFQS ILKGYIKELS IARIRRITFI 1270 1280 1290 1300 1310 1320 CCGGDEGKPL KYFTFRERHM YMEDPIFRHI EPAMAYHLEV RKLSNFDITH VPTTSQRIHL 1330 1340 1350 1360 1370 1380 YYAQEKGKKE TDPDADRSFF VRSVIRYSDL YGHSNEIKVD ILLSQIETLL SESIESLEIA 1390 1400 1410 1420 1430 1440 MSNKKYEKAQ NHSIFLNVMP EVMFDEKMIG YVVQEIGDRL GKRLWKLRVG RVEVRGRIRK 1450 1460 1470 1480 1490 1500 GDGLIPVRFF VQNPTGYAFQ VQCYYEQQNS IGQMVFAVVP GSSKGSWEGL PVDTPYPIMD 1510 1520 1530 1540 1550 1560 AVQRNRFKAQ RLDTTYCYDY PDLFREAMQN IWMEFMESNK TNPVKVYPSS RGVLESVELI 1570 1580 1590 1600 1610 1620 LPSTINTDFP PSIPLDQLPE ESKPKLEETY RPIGYNDIGM VAWRMTFYTP EYPLGRQAIV 1630 1640 1650 1660 1670 1680 IANDITHQIG SFGPQEDMLF KLASELARKE KIPRIYLSSN SGARIGLADE IKSKFKVTWN 1690 1700 1710 1720 1730 1740 VPSDPTKGIK NLYLTNNDYQ ALKDSVIAYQ DTTDKDKWII HDIIGQKNGI GVENLSWSGL 1750 1760 1770 1780 1790 1800 IAGETSQAYN EIFTITLVSG RSVGIGAYLV RLGQRTIQND APIILTGASA LNKVLGKEVY 1810 1820 1830 1840 1850 1860 ESNQQLGGSQ IMYPNGVSHI IVNDELRGIT NVLQWLSFVP KSGGEMVPII SPIDSPHRDI 1870 1880 1890 1900 1910 1920 EFDPSNSING KCDTRHLIAG LQSELDPNYW ISGMFDKDSF METLAGWANT VITGRARLGG 1930 1940 1950 1960 1970 1980 IPVGIIAVET KSVEKIIPAD PANPLSYEQV NTQAGQVWYP DSSFKTAQAI ADFNNGEELP 1990 2000 2010 2020 2030 2040 LMILANWRGF SGGMRDMFDE ILKFGSMIVD NLRNYKQPVM VYIPPFAELR GGAWVVLDST 2050 2060 2070 2080 2090 2100 INLDMMEMYC SEEGRGGVLE PNGIAEIKYR DPELIKTMHR LDPKLIEWDK SIPIGVSVNG 2110 2120 2130 2140 2150 2160 LDQSQKTIKS QIQQREKELL GIYQQIAIKF ADLHDTPGRM KAKGVIKQMV PWKSARSFFY 2170 2180 2190 2200 2210 2220 DRIKRRLFEE DKLKLIDKSH PGLNRQSKLN LLETWIKQIL GNNQSVDYHQ NDKLISSTIE 2230 2240 2250 2260 2270 2280 SNSHIINDKI IDLSKQYAIN QILNFVQSDS ESIVDGFQNL LPFISTQQKE FLFESLKKDL NK

References

[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: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000111 Genomic DNA. Translation: EAL63219.1.
RefSeq	XP_636722.1.
3D structure databases
HSSP	HSSP built from PDB template 1W96 based on UniProtKB Q00955.
SMR	Q54J08. Positions 4-497, 640-735, 1493-2243.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54J08.
Genome annotation databases
GeneID	8626599.
KEGG	ddi:DDB_0230067.
Organism-specific databases
dictyBase	DDB_G0288387. accA.
Phylogenomic databases
eggNOG	KOG0368.
HOGENOM	HBG320067.
OMA	LRNYKQP.
PhylomeDB	Q54J08.
Enzyme and pathway databases
BRENDA	6.3.4.14. 424. 6.4.1.2. 424.
Family and domain databases
InterPro	IPR013537. AcCoA_COase_cen. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR001882. Biotin_BS. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR000022. Carboxyl_trans. IPR011763. COA_CT_C. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	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]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS50989. COA_CT_CTER. 1 hit. PS50980. COA_CT_NTER. False negative. PS00866. CPSASE_1. False negative. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACAC_DICDI

Accession

Primary (citable) accession number: Q54J08

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)