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B3LM95

- HFA1_YEAS1

UniProt

B3LM95 - HFA1_YEAS1

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Protein
Acetyl-CoA carboxylase, mitochondrial
Gene
HFA1, SCRG_02101
Organism
Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 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

Biotin By similarity.

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi332 – 3376ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  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

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
ORF Names:SCRG_02101
OrganismiSaccharomyces cerevisiae (strain RM11-1a) (Baker's yeast)
Taxonomic identifieri285006 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000008335: Unassembled WGS sequence

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 104104Mitochondrion Reviewed prediction
Add
BLAST
Chaini105 – 22732169Acetyl-CoA carboxylase, mitochondrial
PRO_0000392099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei804 – 8041N6-biotinyllysine By similarity

Structurei

3D structure databases

ProteinModelPortaliB3LM95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 635502Biotin carboxylation
Add
BLAST
Domaini292 – 484193ATP-grasp
Add
BLAST
Domaini770 – 83667Biotinyl-binding
Add
BLAST
Domaini1648 – 2147500Carboxyltransferase
Add
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

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.

B3LM95-1 [UniParc]FASTAAdd to Basket

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KGKTITHGQS WGARRIHSHF YITIFTITCI RIGQYKLALY LDPYRFYNIT     50
GSQIVRLKGQ RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK 100
HTRLPPQFIG LNTVESAQPS ILRDFVDLRG GHTVISKILI ANNGIAAVKE 150
MRSIRKWAYE TFNDEKIIQF VVMATPDDLH ANSEYIRMAD QYVQVPGGTN 200
NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA SSQRKILFIG 250
PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD 300
DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNQDDFIAL 350
YRQAVNETPG SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR 400
HQKIIEEAPV TITKPETFQR MERAAIRLGE LVGYVSAGTV EYLYSPKDDK 450
FYFLELNPRL QVEHPTTEMI SGVNLPATQL QIAMGIPMHM ISDIRKLYGL 500
DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST GKIHELNFRS 550
SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI 600
RGEFKTPIEY LTELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI 650
ICGAAMKAYV FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNKYL 700
FNVAQSSEEQ FILSINKSQC EVNVQKLSSD CLLISVDGKC HTVYWKDDIR 750
GTRLSIDSNT IFLEAELNPT QVISPTPGKL VKYLVRSGDH VFAGQQYAEI 800
EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS PSKANESSLY 850
RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK 900
ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM 950
KRYLEENTND HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE 1000
KIFENHDIHE ERNLLNLRRK DLTNLKEILC ISLSHANIVA KNKLVTAILH 1050
EYEPLCQDSS KMSLKFRAVI HDLASLESKW AKEVAVKARS VLLRGIFPPI 1100
KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH SNLIQLQDLF 1150
FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR 1200
NYLVNPDGES DGFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV 1250
YEQIHIPEER LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS 1300
KLKVNRITFA FIAANAPAVK FYSFDGTTYD EIPQIRNMDP SYEAPLELGK 1350
MSNYKIRSLP TYDSSIRIFE GISKFTPLDK RFFVRKIINS FMYNDQKTTE 1400
ENLKAEINAQ VVYMLEHLGA VDISNSDLNH IFLSFNTVLN IPVHRLEEIV 1450
STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI 1500
ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG 1550
TTYVYDFPGL FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR 1600
EPGLNNIGMV AFEIMVQTPE YPEGRNMIVI SNDITYNIGS FGPREDLFFD 1650
RVTNYARERG IPRIYLAANS GAKLGIAEEL IPLFRVAWND PSDPTKGFQY 1700
LYLAPKDMQL LKDSGKGNSV VVEHKMVYGE ERYIIKAIVG FEEGLGVECL 1750
QGSGLIAGAT SKAYREIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII 1800
LTGASAINKV LGTDIYISNL QIGGTQIMYK NGIAHLTASN DMKAIEKIMT 1850
WLSYVPAKRD MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN 1900
NFQSGLFDKD SFFETLSGWA KGVIVGRARL GGIPVGVIAV ETKTIEEIIP 1950
ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ TINDFNYGEQ LPLIILANWR 2000
GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE LRGGSWVVID 2050
PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL 2100
RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML 2150
VKGVIRNELE WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD 2200
LLKIVQSWYN DLDVNDDRAV VEFIERNSKK IDKNIEEFEI SLLIDELKKK 2250
FEDRRGNIVL EELTRLVDSK RKR 2273
Length:2,273
Mass (Da):259,111
Last modified:March 2, 2010 - v2
Checksum:i724744FD30ABA505
GO

Sequence cautioni

The sequence EDV11698.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH408047 Genomic DNA. Translation: EDV11698.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH408047 Genomic DNA. Translation: EDV11698.1 . Different initiation.

3D structure databases

ProteinModelPortali B3LM95.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OrthoDBi EOG74J9H5.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RM11-1a.

Entry informationi

Entry nameiHFA1_YEAS1
AccessioniPrimary (citable) accession number: B3LM95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 2, 2010
Last modified: June 11, 2014
This is version 24 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi