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P32874

- HFA1_YEAST

UniProt

P32874 - HFA1_YEAST

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Protein

Acetyl-CoA carboxylase, mitochondrial

Gene

HFA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

biotinBy similarityNote: Biotin.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei459 – 4591By similarity
Binding sitei1776 – 17761Coenzyme ABy similarity
Binding sitei2080 – 20801Coenzyme ABy similarity
Binding sitei2082 – 20821Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi332 – 3376ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid biosynthetic process Source: SGD
  2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
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, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YMR207C-MONOMER.
YEAST:YMR207C-MONOMER.
ReactomeiREACT_188404. Defective HLCS causes multiple carboxylase deficiency.
REACT_188774. Biotin transport and metabolism.
REACT_241476. ChREBP activates metabolic gene expression.
REACT_258513. Fatty Acyl-CoA Biosynthesis.
REACT_260529. Import of palmitoyl-CoA into the mitochondrial matrix.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase, mitochondrial (EC:6.4.1.2)
Short name:
ACC
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:HFA1
Ordered Locus Names:YMR207C
ORF Names:YM8261.01C, YM8325.08C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

SGDiS000004820. HFA1.

Subcellular locationi

Mitochondrion 3 Publications

GO - Cellular componenti

  1. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 104104MitochondrionSequence AnalysisAdd
BLAST
Chaini105 – 22732169Acetyl-CoA carboxylase, mitochondrialPRO_0000146771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei804 – 8041N6-biotinyllysineBy similarityPROSITE-ProRule annotation

Proteomic databases

MaxQBiP32874.
PaxDbiP32874.

Expressioni

Gene expression databases

GenevestigatoriP32874.

Interactioni

Protein-protein interaction databases

BioGridi35385. 82 interactions.
DIPiDIP-2568N.
IntActiP32874. 2 interactions.
MINTiMINT-423824.

Structurei

3D structure databases

ProteinModelPortaliP32874.
SMRiP32874. Positions 90-634, 1538-2236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 635502Biotin carboxylationAdd
BLAST
Domaini292 – 484193ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini763 – 83775Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1648 – 2147500CarboxyltransferaseAdd
BLAST

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0511.
HOGENOMiHOG000214115.
InParanoidiP32874.
KOiK11262.
OrthoDBiEOG74J9H5.

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.
IPR011762. COA_CT_N.
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.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32874-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
KGKTITHGQS WGARRIHSHF YITIFTITCI RIGQYKLALY LDPYRFYNIT
60 70 80 90 100
GSQIVRLKGQ RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK
110 120 130 140 150
HTRLPPQFIG LNTVESAQPS ILRDFVDLRG GHTVISKILI ANNGIAAVKE
160 170 180 190 200
MRSIRKWAYE TFNDEKIIQF VVMATPDDLH ANSEYIRMAD QYVQVPGGTN
210 220 230 240 250
NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA SSQRKILFIG
260 270 280 290 300
PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD
310 320 330 340 350
DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNEDDFIAL
360 370 380 390 400
YRQAVNETPG SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR
410 420 430 440 450
HQKIIEEAPV TITKPETFQR MERAAIRLGE LVGYVSAGTV EYLYSPKDDK
460 470 480 490 500
FYFLELNPRL QVEHPTTEMI SGVNLPATQL QIAMGIPMHM ISDIRKLYGL
510 520 530 540 550
DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST GKIHELNFRS
560 570 580 590 600
SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI
610 620 630 640 650
RGEFKTPIEY LIELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI
660 670 680 690 700
ICGAAMKAYV FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNRYL
710 720 730 740 750
FNVAQSSEEQ FILSINKSQC EVNVQKLSSD CLLISVDGKC HTVYWKDDIR
760 770 780 790 800
GTRLSIDSNT IFLEAELNPT QVISPTPGKL VKYLVRSGDH VFAGQQYAEI
810 820 830 840 850
EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS PSKANESSLY
860 870 880 890 900
RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK
910 920 930 940 950
ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM
960 970 980 990 1000
KRYLEENTND HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE
1010 1020 1030 1040 1050
KIFENHDIHE ERNLLNLRRK DLTNLKKILC ISLSHANVVA KNKLVTAILH
1060 1070 1080 1090 1100
EYEPLCQDSS KMSLKFRAVI HDLASLESKW AKEVAVKARS VLLRGIFPPI
1110 1120 1130 1140 1150
KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH SNLIQLQDLF
1160 1170 1180 1190 1200
FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR
1210 1220 1230 1240 1250
NYLVNSDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV
1260 1270 1280 1290 1300
YEQIHIPEER LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS
1310 1320 1330 1340 1350
KLKVNRITFA FIAANAPAVK FYSFDGTTYD EISQIRNMDP SYEAPLELGK
1360 1370 1380 1390 1400
MSNYKIRSLP TYDSSIRIFE GISKFTPLDK RFFVRKIINS FMYNDQKTTE
1410 1420 1430 1440 1450
ENLKAEINAQ VVYMLEHLGA VDISNSDLNH IFLSFNTVLN IPVHRLEEIV
1460 1470 1480 1490 1500
STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI
1510 1520 1530 1540 1550
ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG
1560 1570 1580 1590 1600
TTYVYDFPGL FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR
1610 1620 1630 1640 1650
EPGLNNIGMV AFEIMVQTPE YPEGRNMIVI SNDITYNIGS FGPREDLFFD
1660 1670 1680 1690 1700
RVTNYARERG IPRIYLAANS GAKLGIAEEL IPLFRVAWND PSDPTKGFQY
1710 1720 1730 1740 1750
LYLAPKDMQL LKDSGKGNSV VVEHKMVYGE ERYIIKAIVG FEEGLGVECL
1760 1770 1780 1790 1800
QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII
1810 1820 1830 1840 1850
LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTASN DMKAIEKIMT
1860 1870 1880 1890 1900
WLSYVPAKRD MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN
1910 1920 1930 1940 1950
NFQSGLFDKD SFFETLSGWA KGVIVGRARL GGIPVGVIAV ETKTIEEIIP
1960 1970 1980 1990 2000
ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ TINDFNYGEQ LPLIILANWR
2010 2020 2030 2040 2050
GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE LRGGSWVVID
2060 2070 2080 2090 2100
PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL
2110 2120 2130 2140 2150
RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML
2160 2170 2180 2190 2200
VKGVIRNELE WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD
2210 2220 2230 2240 2250
LLKIVQSWYN DLDVNDDRAV VEFIERNSKK IDKNIEEFEI SLLIDELKKK
2260 2270
FEDRRGNIVL EELTRLVDSK RKR
Length:2,273
Mass (Da):259,163
Last modified:October 1, 1996 - v2
Checksum:i08727A301549DA92
GO

Sequence cautioni

The sequence DAA10106.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti661 – 6611F → L in CAA80280. (PubMed:7906156)Curated
Sequence conflicti1027 – 10271K → E in BAA24410. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78165 Genomic DNA. Translation: BAA24410.1.
Z49809 Genomic DNA. Translation: CAA89922.1.
Z48755 Genomic DNA. Translation: CAA88647.1.
Z22558 Genomic DNA. Translation: CAA80280.1.
BK006946 Genomic DNA. Translation: DAA10106.1. Different initiation.
PIRiS55089.
RefSeqiNP_013934.1. NM_001182714.1.

Genome annotation databases

GeneIDi855247.
KEGGisce:YMR207C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78165 Genomic DNA. Translation: BAA24410.1 .
Z49809 Genomic DNA. Translation: CAA89922.1 .
Z48755 Genomic DNA. Translation: CAA88647.1 .
Z22558 Genomic DNA. Translation: CAA80280.1 .
BK006946 Genomic DNA. Translation: DAA10106.1 . Different initiation.
PIRi S55089.
RefSeqi NP_013934.1. NM_001182714.1.

3D structure databases

ProteinModelPortali P32874.
SMRi P32874. Positions 90-634, 1538-2236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35385. 82 interactions.
DIPi DIP-2568N.
IntActi P32874. 2 interactions.
MINTi MINT-423824.

Proteomic databases

MaxQBi P32874.
PaxDbi P32874.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 855247.
KEGGi sce:YMR207C.

Organism-specific databases

SGDi S000004820. HFA1.

Phylogenomic databases

eggNOGi COG0511.
HOGENOMi HOG000214115.
InParanoidi P32874.
KOi K11262.
OrthoDBi EOG74J9H5.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BioCyci MetaCyc:YMR207C-MONOMER.
YEAST:YMR207C-MONOMER.
Reactomei REACT_188404. Defective HLCS causes multiple carboxylase deficiency.
REACT_188774. Biotin transport and metabolism.
REACT_241476. ChREBP activates metabolic gene expression.
REACT_258513. Fatty Acyl-CoA Biosynthesis.
REACT_260529. Import of palmitoyl-CoA into the mitochondrial matrix.

Miscellaneous databases

NextBioi 978813.

Gene expression databases

Genevestigatori P32874.

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.
IPR011762. COA_CT_N.
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.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Identification of a Saccharomyces cerevisiae gene closely related to FAS3 (acetyl-CoA carboxylase)."
    Kearsey S.E.
    DNA Seq. 4:69-70(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-949.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiHFA1_YEAST
AccessioniPrimary (citable) accession number: P32874
Secondary accession number(s): D6W032, O42823
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 396 molecules/cell in log phase SD medium.1 Publication

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 (PubMed:14761959) 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.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3