Reviewed, UniProtKB/Swiss-Prot P32874 (HFA1_YEAST)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA carboxylase, mitochondrial
      Short name=ACC
    EC=6.4.1.2
Including the following 1 domains:
    1- Recommended name:
            Biotin carboxylase
              EC=6.3.4.14

Gene names

Name:	HFA1
Ordered Locus Names:	YMR207C
ORF Names:	YM8261.01C, YM8325.08C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the rate-limiting reaction in the mitochondrial fatty acid synthesis (FAS) type II pathway. Responsible for the production of the mitochondrial malonyl-CoA, used for the biosynthesis of the cofactor lipoic acid. This protein carries three functions: biotin carboxyl carrier protein, biotin carboxylase, and carboxyltransferase. Ref.7
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.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular location	Mitochondrion. Ref.7 Ref.4 Ref.6
Miscellaneous	Present with 396 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.
Caution	The reading frame from which this protein is translated has no Met initiation codon near to the 5'-end. However, it is not a pseudogene. It has been shown (Ref.7) that at least 72 residues upstream of the first in-frame start codon (Met-151) are required for function and proper subcellular location. May be translated by means of alternative initiation codon usage, programmed translational frame shifting, or mRNA editing.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Ref.7 Inferred from genetic interaction. Source: SGD
Cellular component	mitochondrion Ref.4 Ref.6 Ref.7 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Ref.7 Inferred from genetic interaction. Source: SGD biotin binding Inferred from electronic annotation. Source: InterPro biotin carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 104	104	Mitochondrion Potential
	Chain	105 – 2273	2169	Acetyl-CoA carboxylase, mitochondrial		PRO_0000146771
Regions
	Domain	134 – 635	502	Biotin carboxylation
	Domain	292 – 484	193	ATP-grasp
	Domain	770 – 836	67	Biotinyl-binding
	Domain	1648 – 2147	500	Carboxyltransferase
	Nucleotide binding	332 – 337	6	ATP By similarity
Sites
	Active site	459	1	By similarity
	Binding site	1776	1	Coenzyme A By similarity
	Binding site	2080	1	Coenzyme A By similarity
	Binding site	2082	1	Coenzyme A By similarity
Amino acid modifications
	Modified residue	804	1	N6-biotinyllysine By similarity
Experimental info
	Sequence conflict	661	1	F → L in CAA80280. Ref.3
	Sequence conflict	1027	1	K → E in BAA24410. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32874-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 08727A301549DA92	FASTA	2,273	259,163
	10 20 30 40 50 60 KGKTITHGQS WGARRIHSHF YITIFTITCI RIGQYKLALY LDPYRFYNIT GSQIVRLKGQ 70 80 90 100 110 120 RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK HTRLPPQFIG LNTVESAQPS 130 140 150 160 170 180 ILRDFVDLRG GHTVISKILI ANNGIAAVKE MRSIRKWAYE TFNDEKIIQF VVMATPDDLH 190 200 210 220 230 240 ANSEYIRMAD QYVQVPGGTN NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA 250 260 270 280 290 300 SSQRKILFIG PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD 310 320 330 340 350 360 DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNEDDFIAL YRQAVNETPG 370 380 390 400 410 420 SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR HQKIIEEAPV TITKPETFQR 430 440 450 460 470 480 MERAAIRLGE LVGYVSAGTV EYLYSPKDDK FYFLELNPRL QVEHPTTEMI SGVNLPATQL 490 500 510 520 530 540 QIAMGIPMHM ISDIRKLYGL DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST 550 560 570 580 590 600 GKIHELNFRS SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI 610 620 630 640 650 660 RGEFKTPIEY LIELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI ICGAAMKAYV 670 680 690 700 710 720 FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNRYL FNVAQSSEEQ FILSINKSQC 730 740 750 760 770 780 EVNVQKLSSD CLLISVDGKC HTVYWKDDIR GTRLSIDSNT IFLEAELNPT QVISPTPGKL 790 800 810 820 830 840 VKYLVRSGDH VFAGQQYAEI EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS 850 860 870 880 890 900 PSKANESSLY RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK 910 920 930 940 950 960 ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM KRYLEENTND 970 980 990 1000 1010 1020 HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE KIFENHDIHE ERNLLNLRRK 1030 1040 1050 1060 1070 1080 DLTNLKKILC ISLSHANVVA KNKLVTAILH EYEPLCQDSS KMSLKFRAVI HDLASLESKW 1090 1100 1110 1120 1130 1140 AKEVAVKARS VLLRGIFPPI KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH 1150 1160 1170 1180 1190 1200 SNLIQLQDLF FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR 1210 1220 1230 1240 1250 1260 NYLVNSDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV YEQIHIPEER 1270 1280 1290 1300 1310 1320 LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS KLKVNRITFA FIAANAPAVK 1330 1340 1350 1360 1370 1380 FYSFDGTTYD EISQIRNMDP SYEAPLELGK MSNYKIRSLP TYDSSIRIFE GISKFTPLDK 1390 1400 1410 1420 1430 1440 RFFVRKIINS FMYNDQKTTE ENLKAEINAQ VVYMLEHLGA VDISNSDLNH IFLSFNTVLN 1450 1460 1470 1480 1490 1500 IPVHRLEEIV STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI 1510 1520 1530 1540 1550 1560 ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG TTYVYDFPGL 1570 1580 1590 1600 1610 1620 FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR EPGLNNIGMV AFEIMVQTPE 1630 1640 1650 1660 1670 1680 YPEGRNMIVI SNDITYNIGS FGPREDLFFD RVTNYARERG IPRIYLAANS GAKLGIAEEL 1690 1700 1710 1720 1730 1740 IPLFRVAWND PSDPTKGFQY LYLAPKDMQL LKDSGKGNSV VVEHKMVYGE ERYIIKAIVG 1750 1760 1770 1780 1790 1800 FEEGLGVECL QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII 1810 1820 1830 1840 1850 1860 LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTASN DMKAIEKIMT WLSYVPAKRD 1870 1880 1890 1900 1910 1920 MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN NFQSGLFDKD SFFETLSGWA 1930 1940 1950 1960 1970 1980 KGVIVGRARL GGIPVGVIAV ETKTIEEIIP ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ 1990 2000 2010 2020 2030 2040 TINDFNYGEQ LPLIILANWR GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE 2050 2060 2070 2080 2090 2100 LRGGSWVVID PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL 2110 2120 2130 2140 2150 2160 RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML VKGVIRNELE 2170 2180 2190 2200 2210 2220 WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD LLKIVQSWYN DLDVNDDRAV 2230 2240 2250 2260 2270 VEFIERNSKK IDKNIEEFEI SLLIDELKKK FEDRRGNIVL EELTRLVDSK RKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Occurrence of an acetyl-CoA carboxylase-like gene in Saccharomyces serevisiae." Saito A., Kazuta Y., Kondo H., Tanabe T. Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SP1.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Identification of a Saccharomyces cerevisiae gene closely related to FAS3 (acetyl-CoA carboxylase)." Kearsey S.E. DNA Seq. 4:69-70(1993) [PubMed: 7906156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-949.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"HFA1 encoding an organelle-specific acetyl-CoA carboxylase controls mitochondrial fatty acid synthesis in Saccharomyces cerevisiae." Hoja U., Marthol S., Hofmann J., Stegner S., Schulz R., Meier S., Greiner E., Schweizer E. J. Biol. Chem. 279:21779-21786(2004) [PubMed: 14761959] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D78165 Genomic DNA. Translation: BAA24410.1. Z49809 Genomic DNA. Translation: CAA89922.1. Z48755 Genomic DNA. Translation: CAA88647.1. Z22558 Genomic DNA. Translation: CAA80280.1.
PIR	S55089.
3D structure databases
HSSP	HSSP built from PDB template 1OD4 based on UniProtKB Q00955.
SMR	P32874. Positions 90-634.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2568N.
STRING	P32874.
Proteomic databases
PRIDE	P32874.
Genome annotation databases
Ensembl	YMR207C; YMR207C; YMR207C; Saccharomyces cerevisiae. [Genome view]
GenomeReviews	Gene locus YMR207C in contig Z71257_GR.
NMPDR	fig|4932.3.peg.4987.
Organism-specific databases
CYGD	YMR207c.
SGD	S000004820. HFA1.
Phylogenomic databases
HOGENOM	P32874.
Enzyme and pathway databases
BRENDA	6.3.4.14. 250. 6.4.1.2. 250.
Gene expression databases
ArrayExpress	P32874.
Genevestigator	P32874.
GermOnline	YMR207C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013537. AcCoA_COase_cen. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR011764. BC. IPR001882. Biotin_BS. 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. IPR011762. COA_CT_N. IPR013817. Pre-ATP_grasp. [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]
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. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HFA1_YEAST

Accession

Primary (citable) accession number: P32874
Secondary accession number(s): O42823

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1996
Last modified:	October 13, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)