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Q38970 (ACC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1

Short name=AtACC1
EC=6.4.1.2
Alternative name(s):
Protein EMBRYO DEFECTIVE 22
Protein GURKE
Protein PASTICCINO 3

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:ACC1
Synonyms:EMB22, GK, PAS3
Ordered Locus Names:At1g36160
ORF Names:F15C21.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length2254 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the carboxylation of acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty acid synthesis and in the cytosol in various biosynthetic pathways including fatty acid elongation. Required for very long chain fatty acids elongation. Necessary for embryo and plant development. Plays a central function in embryo morphogenesis, especially in apical meristem development. Involved in cell proliferation and tissue patterning. May act as a repressor of cytokinin response. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14

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.

Binds 2 magnesium or manganese ions per subunit By similarity.

Pathway

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

Subunit structure

Homodimer Probable.

Subcellular location

Cytoplasmcytosol Probable.

Tissue specificity

Expressed in roots, trichomes, epidermal leaf cells, siliques, petals, anthers, and seeds. Ref.1 Ref.2 Ref.9 Ref.10

Developmental stage

Expressed in flower buds at stage 6 of development in tapetal cells and at stage 10 in the epidermal cells of growing petals and ovaries. In young siliques, expressed transiently in the inner integument of the ovules just prior to testal deposition. Ref.9

Disruption phenotype

Embryo lethal with an arrest in development at the late globular stage in acc1-1 and acc1-2 null allele mutants. In the leaky pas3 and gk alleles, defect in embryo development, very short and thick hypocotyl and misshaped cotyledons that do not expand. Abnormal root development, abnormal fused leaves and compact rosettes with multiple shoots. Uncoordinated cell divisions in the apical region. Reduced levels of very long chain fatty acids in seeds. Ref.6 Ref.8 Ref.10 Ref.11 Ref.12

Miscellaneous

The acc1-1 and pas3-1 mutants can be partially complemented by exogenous supply of malonate.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence caution

The sequence AAF18638.2 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAG51250.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Biotin
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processembryo development ending in seed dormancy

Inferred from mutant phenotype Ref.6Ref.8. Source: TAIR

fatty acid elongation

Inferred from mutant phenotype Ref.10. Source: TAIR

malonyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

meristem structural organization

Inferred from mutant phenotype Ref.6. Source: TAIR

primary shoot apical meristem specification

Inferred from mutant phenotype Ref.10. Source: TAIR

response to cytokinin

Inferred from mutant phenotype Ref.8. Source: TAIR

root development

Inferred from mutant phenotype Ref.8. Source: TAIR

shoot system development

Inferred from mutant phenotype Ref.8. Source: TAIR

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 17317660. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetyl-CoA carboxylase activity

Inferred from sequence or structural similarity Ref.2. Source: TAIR

biotin carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22542254Acetyl-CoA carboxylase 1
PRO_0000412211

Regions

Domain36 – 543508Biotin carboxylation
Domain189 – 381193ATP-grasp
Domain677 – 74367Biotinyl-binding
Domain1531 – 2110580Carboxyltransferase
Nucleotide binding215 – 27258ATP Potential

Sites

Active site3561 By similarity
Metal binding3381Magnesium or manganese 1 By similarity
Metal binding3521Magnesium or manganese 1 By similarity
Metal binding3521Magnesium or manganese 2 By similarity
Metal binding3541Magnesium or manganese 2 By similarity
Binding site17401Coenzyme A By similarity
Binding site20411Coenzyme A By similarity
Binding site20431Coenzyme A By similarity

Amino acid modifications

Modified residue10311Phosphothreonine Ref.13
Modified residue11921Phosphoserine Ref.13

Experimental info

Mutagenesis15881E → K in pas3-1; developmental phenotype and reduced levels of very long chain fatty acids in seeds. Ref.11
Mutagenesis17871G → S in pas3-2; developmental phenotype and reduced levels of very long chain fatty acids in seeds. Ref.11
Sequence conflict3371V → I in AAC41645. Ref.1
Sequence conflict3371V → I in AAG40563. Ref.2
Sequence conflict1378 – 13792EQ → DE in AAC41645. Ref.1
Sequence conflict1378 – 13792EQ → DE in AAG40563. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q38970 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F00A5AE316CC5E87

FASTA2,254251,382
        10         20         30         40         50         60 
MAGSVNGNHS AVGPGINYET VSQVDEFCKA LRGKRPIHSI LIANNGMAAV KFIRSVRTWA 

        70         80         90        100        110        120 
YETFGTEKAI LLVGMATPED MRINAEHIRI ADQFVEVPGG TNNNNYANVQ LIVEMAEVTR 

       130        140        150        160        170        180 
VDAVWPGWGH ASENPELPDA LDAKGIIFLG PPASSMAALG DKIGSSLIAQ AADVPTLPWS 

       190        200        210        220        230        240 
GSHVKIPPNS NLVTIPEEIY RQACVYTTEE AIASCQVVGY PAMIKASWGG GGKGIRKVHN 

       250        260        270        280        290        300 
DDEVRALFKQ VQGEVPGSPI FIMKVASQSR HLEVQLLCDK HGNVSALHSR DCSVQRRHQK 

       310        320        330        340        350        360 
IIEEGPITVA PPETVKKLEQ AARRLAKSVN YVGAATVEYL YSMDTGEYYF LELNPRLQVE 

       370        380        390        400        410        420 
HPVTEWIAEI NLPAAQVAVG MGIPLWQIPE IRRFYGIEHG GGYDSWRKTS VVAFPFDFDK 

       430        440        450        460        470        480 
AQSIRPKGHC VAVRVTSEDP DDGFKPTSGR VQELSFKSKP NVWAYFSVKS GGGIHEFSDS 

       490        500        510        520        530        540 
QFGHVFAFGE SRALAIANMV LGLKEIQIRG EIRTNVDYTI DLLHASDYRD NKIHTGWLDS 

       550        560        570        580        590        600 
RIAMRVRAER PPWYLSVVGG ALYKASATSA AVVSDYVGYL EKGQIPPKHI SLVHSQVSLN 

       610        620        630        640        650        660 
IEGSKYTIDV VRGGSGTYRL RMNKSEVVAE IHTLRDGGLL MQLDGKSHVI YAEEEAAGTR 

       670        680        690        700        710        720 
LLIDGRTCLL QNDHDPSKLM AETPCKLMRY LISDNSNIDA DTPYAEVEVM KMCMPLLSPA 

       730        740        750        760        770        780 
SGVIHFKMSE GQAMQAGELI ANLDLDDPSA VRKAEPFHGS FPRLGLPTAI SGRVHQRCAA 

       790        800        810        820        830        840 
TLNAARMILA GYEHKVDEVV QDLLNCLDSP ELPFLQWQEC FAVLATRLPK NLRNMLESKY 

       850        860        870        880        890        900 
REFESISRNS LTTDFPAKLL KGILEAHLSS CDEKERGALE RLIEPLMSLA KSYEGGRESH 

       910        920        930        940        950        960 
ARVIVHSLFE EYLSVEELFN DNMLADVIER MRQLYKKDLL KIVDIVLSHQ GIKNKNKLVL 

       970        980        990       1000       1010       1020 
RLMEQLVYPN PAAYRDKLIR FSTLNHTNYS ELALKASQLL EQTKLSELRS NIARSLSELE 

      1030       1040       1050       1060       1070       1080 
MFTEDGENMD TPKRKSAINE RIEDLVSASL AVEDALVGLF DHSDHTLQRR VVETYIRRLY 

      1090       1100       1110       1120       1130       1140 
QPYVVKDSVR MQWHRSGLLA SWEFLEEHME RKNIGLDDPD TSEKGLVEKR SKRKWGAMVI 

      1150       1160       1170       1180       1190       1200 
IKSLQFLPSI ISAALRETKH NDYETAGAPL SGNMMHIAIV GINNQMSLLQ DSGDEDQAQE 

      1210       1220       1230       1240       1250       1260 
RVNKLAKILK EEEVSSSLCS AGVGVISCII QRDEGRTPMR HSFHWSLEKQ YYVEEPLLRH 

      1270       1280       1290       1300       1310       1320 
LEPPLSIYLE LDKLKGYSNI QYTPSRDRQW HLYTVTDKPV PIKRMFLRSL VRQATMNDGF 

      1330       1340       1350       1360       1370       1380 
ILQQGQDKQL SQTLISMAFT SKCVLRSLMD AMEELELNAH NAAMKPDHAH MFLCILREQQ 

      1390       1400       1410       1420       1430       1440 
IDDLVPFPRR VEVNAEDEET TVEMILEEAA REIHRSVGVR MHRLGVCEWE VRLWLVSSGL 

      1450       1460       1470       1480       1490       1500 
ACGAWRVVVA NVTGRTCTVH IYREVETPGR NSLIYHSITK KGPLHETPIS DQYKPLGYLD 

      1510       1520       1530       1540       1550       1560 
RQRLAARRSN TTYCYDFPLA FGTALELLWA SQHPGVKKPY KDTLINVKEL VFSKPEGSSG 

      1570       1580       1590       1600       1610       1620 
TSLDLVERPP GLNDFGMVAW CLDMSTPEFP MGRKLLVIAN DVTFKAGSFG PREDAFFLAV 

      1630       1640       1650       1660       1670       1680 
TELACAKKLP LIYLAANSGA RLGVAEEVKA CFKVGWSDEI SPENGFQYIY LSPEDHERIG 

      1690       1700       1710       1720       1730       1740 
SSVIAHEVKL SSGETRWVID TIVGKEDGIG VENLTGSGAI AGAYSKAYNE TFTLTFVSGR 

      1750       1760       1770       1780       1790       1800 
TVGIGAYLAR LGMRCIQRLD QPIILTGFST LNKLLGREVY SSHMQLGGPK IMGTNGVVHL 

      1810       1820       1830       1840       1850       1860 
TVSDDLEGVS AILNWLSYIP AYVGGPLPVL APLDPPERIV EYVPENSCDP RAAIAGVKDN 

      1870       1880       1890       1900       1910       1920 
TGKWLGGIFD KNSFIETLEG WARTVVTGRA KLGGIPVGVV AVETQTVMQI IPADPGQLDS 

      1930       1940       1950       1960       1970       1980 
HERVVPQAGQ VWFPDSAAKT AQALMDFNRE ELPLFILANW RGFSGGQRDL FEGILQAGST 

      1990       2000       2010       2020       2030       2040 
IVENLRTYRQ PVFVYIPMMG ELRGGAWVVV DSQINSDYVE MYADETARGN VLEPEGTIEI 

      2050       2060       2070       2080       2090       2100 
KFRTKELLEC MGRLDQKLIS LKAKLQDAKQ SEAYANIELL QQQIKAREKQ LLPVYIQIAT 

      2110       2120       2130       2140       2150       2160 
KFAELHDTSM RMAAKGVIKS VVEWSGSRSF FYKKLNRRIA ESSLVKNVRE ASGDNLAYKS 

      2170       2180       2190       2200       2210       2220 
SMRLIQDWFC NSDIAKGKEE AWTDDQVFFT WKDNVSNYEL KLSELRAQKL LNQLAEIGNS 

      2230       2240       2250 
SDLQALPQGL ANLLNKVEPS KREELVAAIR KVLG 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of an Arabidopsis acetyl-coenzyme A carboxylase gene."
Roesler K.R., Shorrosh B.S., Ohlrogge J.B.
Plant Physiol. 105:611-617(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Genomic organization of 251 kDa acetyl-CoA carboxylase genes in Arabidopsis: tandem gene duplication has made two differentially expressed isozymes."
Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J., Ichikawa N.
Plant Cell Physiol. 36:779-787(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1246-2254.
Strain: cv. Columbia.
[6]"The GURKE gene is required for normal organization of the apical region in the Arabidopsis embryo."
Torres-Ruiz R.A., Lohner A., Juergens G.
Plant J. 10:1005-1016(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"Targeting of the Arabidopsis homomeric acetyl-coenzyme A carboxylase to plastids of rapeseeds."
Roesler K., Shintani D., Savage L., Boddupalli S., Ohlrogge J.
Plant Physiol. 113:75-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The PASTICCINO genes of Arabidopsis thaliana are involved in the control of cell division and differentiation."
Faure J.-D., Vittorioso P., Santoni V., Fraisier V., Prinsen E., Barlier I., Van Onckelen H., Caboche M., Bellini C.
Development 125:909-918(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis."
Fatland B.L., Ke J., Anderson M.D., Mentzen W.I., Cui L.W., Allred C.C., Johnston J.L., Nikolau B.J., Wurtele E.S.
Plant Physiol. 130:740-756(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[10]"Multifunctional acetyl-CoA carboxylase 1 is essential for very long chain fatty acid elongation and embryo development in Arabidopsis."
Baud S., Guyon V., Kronenberger J., Wuilleme S., Miquel M., Caboche M., Lepiniec L., Rochat C.
Plant J. 33:75-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Strain: cv. Wassilewskija.
[11]"gurke and pasticcino3 mutants affected in embryo development are impaired in acetyl-CoA carboxylase."
Baud S., Bellec Y., Miquel M., Bellini C., Caboche M., Lepiniec L., Faure J.D., Rochat C.
EMBO Rep. 5:515-520(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-1588 AND GLY-1787.
Strain: cv. Wassilewskija.
[12]"The GURKE gene encoding an acetyl-CoA carboxylase is required for partitioning the embryo apex into three subregions in Arabidopsis."
Kajiwara T., Furutani M., Hibara K., Tasaka M.
Plant Cell Physiol. 45:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[13]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1031 AND SER-1192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Very-long-chain fatty acids are involved in polar auxin transport and developmental patterning in Arabidopsis."
Roudier F., Gissot L., Beaudoin F., Haslam R., Michaelson L., Marion J., Molino D., Lima A., Bach L., Morin H., Tellier F., Palauqui J.C., Bellec Y., Renne C., Miquel M., Dacosta M., Vignard J., Rochat C. expand/collapse author list , Markham J.E., Moreau P., Napier J., Faure J.D.
Plant Cell 22:364-375(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
Plant Physiol. Biochem. 0:0-0(2013)
Cited for: REVIEW, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27074 Genomic DNA. Translation: AAC41645.1.
D34630 mRNA. Translation: BAA07012.1.
AF062308 Genomic DNA. Translation: AAG40563.1.
AC006228 Genomic DNA. Translation: AAF18638.2. Sequence problems.
AC025781 Genomic DNA. Translation: AAG51250.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31849.1.
CP002684 Genomic DNA. Translation: AEE31850.1.
AK229488 mRNA. Translation: BAF01346.1.
PIRD86483.
RefSeqNP_001185143.1. NM_001198214.1.
NP_174849.2. NM_103313.3.
UniGeneAt.39402.

3D structure databases

ProteinModelPortalQ38970.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid25753. 4 interactions.
IntActQ38970. 1 interaction.
STRING3702.AT1G36160.1-P.

Proteomic databases

PRIDEQ38970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G36160.1; AT1G36160.1; AT1G36160.
AT1G36160.2; AT1G36160.2; AT1G36160.
GeneID840521.
KEGGath:AT1G36160.

Organism-specific databases

TAIRAT1G36160.

Phylogenomic databases

eggNOGCOG0511.
HOGENOMHOG000214115.
InParanoidQ38970.
KOK11262.
OMAETESFQM.
PhylomeDBQ38970.
ProtClustDBCLSN2681517.

Enzyme and pathway databases

BioCycARA:AT1G36160-MONOMER.
ARA:GQT-1121-MONOMER.
UniPathwayUPA00655; UER00711.

Gene expression databases

ArrayExpressQ38970.
GenevestigatorQ38970.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
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.
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.
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.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ38970.

Entry information

Entry nameACC1_ARATH
AccessionPrimary (citable) accession number: Q38970
Secondary accession number(s): Q0WNF3 expand/collapse secondary AC list , Q38971, Q9C8G1, Q9SKV1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names