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A6ZMR9 (HFA1_YEAS7) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase, mitochondrial

Short name=ACC
EC=6.4.1.2

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:HFA1
ORF Names:SCY_4385
OrganismSaccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]
Taxonomic identifier307796 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length2273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactor

Biotin By similarity.

Pathway

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

Subcellular location

Mitochondrion By similarity.

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 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.

Sequence caution

The sequence EDN64143.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 104104Mitochondrion Potential
Chain105 – 22732169Acetyl-CoA carboxylase, mitochondrial
PRO_0000392101

Regions

Domain134 – 635502Biotin carboxylation
Domain292 – 484193ATP-grasp
Domain770 – 83667Biotinyl-binding
Domain1648 – 2147500Carboxyltransferase
Nucleotide binding332 – 3376ATP By similarity

Sites

Active site4591 By similarity
Binding site17761Coenzyme A By similarity
Binding site20801Coenzyme A By similarity
Binding site20821Coenzyme A By similarity

Amino acid modifications

Modified residue8041N6-biotinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6ZMR9 [UniParc].

Last modified March 2, 2010. Version 2.
Checksum: 22AE8CD3EBB50432

FASTA2,273259,162
        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 
EVNVQKLSGD 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 
DLTNLKEILC 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 
NYLVNPDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV YEQIHIPEER 

      1270       1280       1290       1300       1310       1320 
LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS KLKVNRITFA FIAANAPTVK 

      1330       1340       1350       1360       1370       1380 
FYSFDGTTYD EISQIRNMDP SYEAPLELGK MSNYKIRSLP TYDSSIRIFE GISKFTPLDK 

      1390       1400       1410       1420       1430       1440 
RFFVRKIINS SMYNDQKTTE ENLKAEINAQ VVYMLEHLGA VDTSNSDLNH 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 LKDYGKGNSV VVEHKMVYGE ERYIIKAIVG 

      1750       1760       1770       1780       1790       1800 
FEEGLGVECL QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII 

      1810       1820       1830       1840       1850       1860 
LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTAGN 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 VKGVIRKELE 

      2170       2180       2190       2200       2210       2220 
WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD LLKIVQSWYN DLDVNDDRAV 

      2230       2240       2250       2260       2270 
VEFIERNSKK IDKNIEEFEI SLLIDELKKK FEDRRGNIVL EELTRLVDSK RKR 

« Hide

References

[1]"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789."
Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. expand/collapse author list , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M.
Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YJM789.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFW02000021 Genomic DNA. Translation: EDN64143.1. Different initiation.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG74J9H5.

Enzyme and pathway databases

UniPathwayUPA00655; UER00711.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProIPR013537. 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]
PfamPF08326. 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]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. 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]
ProtoNetSearch...

Entry information

Entry nameHFA1_YEAS7
AccessionPrimary (citable) accession number: A6ZMR9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 2, 2010
Last modified: June 11, 2014
This is version 36 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways