UBE11_ARATH
ID UBE11_ARATH Reviewed; 1080 AA.
AC P93028; Q8RX82;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ubiquitin-activating enzyme E1 1;
DE Short=AtUBA1 {ECO:0000303|PubMed:9076989};
DE EC=6.2.1.45 {ECO:0000269|PubMed:9076989};
DE AltName: Full=Protein MODIFIER OF SNC1 5;
GN Name=UBA1; Synonyms=MOS5; OrderedLocusNames=At2g30110; ORFNames=T27E13.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=9076989; DOI=10.1046/j.1365-313x.1997.11020213.x;
RA Hatfield P.M., Gosink M.M., Carpenter T.B., Vierstra R.D.;
RT "The ubiquitin-activating enzyme (E1) gene family in Arabidopsis
RT thaliana.";
RL Plant J. 11:213-226(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 1032-ARG--VAL-1037.
RX PubMed=17217463; DOI=10.1111/j.1365-313x.2006.02978.x;
RA Goritschnig S., Zhang Y., Li X.;
RT "The ubiquitin pathway is required for innate immunity in Arabidopsis.";
RL Plant J. 49:540-551(2007).
CC -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC glycine residue with ATP, and thereafter linking this residue to the
CC side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC thioester and free AMP. {ECO:0000269|PubMed:17217463,
CC ECO:0000269|PubMed:9076989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000269|PubMed:9076989};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:9076989}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, roots and stems.
CC Detected in germinating seeds, cotyledons, hypocotyls, vascular
CC tissues, anthers, filaments, pollen, style, stigma, sepals, petals,
CC ovary, developing ovules, funiculi and silique walls.
CC {ECO:0000269|PubMed:9076989}.
CC -!- DEVELOPMENTAL STAGE: Expressed over the entire range of development.
CC {ECO:0000269|PubMed:9076989}.
CC -!- MISCELLANEOUS: Both UBA1 and UBA2 are able to activate ubiquitin and
CC transfer it to the E2s with equal efficiency.
CC {ECO:0000269|PubMed:9076989}.
CC -!- MISCELLANEOUS: Mutation in UBA1 (mos5) suppresses snc1-mediated
CC constitutive resistance and affects the resistance responses conferred
CC by only a subset of R-proteins. {ECO:0000269|PubMed:17217463}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; U80808; AAB39246.1; -; Genomic_DNA.
DR EMBL; AC004165; AAC16961.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08346.1; -; Genomic_DNA.
DR EMBL; AY090248; AAL90910.1; -; mRNA.
DR EMBL; BT006363; AAP21171.1; -; mRNA.
DR PIR; T00587; T00587.
DR RefSeq; NP_565693.1; NM_128566.4.
DR AlphaFoldDB; P93028; -.
DR SMR; P93028; -.
DR BioGRID; 2911; 33.
DR IntAct; P93028; 1.
DR STRING; 3702.AT2G30110.1; -.
DR iPTMnet; P93028; -.
DR PaxDb; P93028; -.
DR PRIDE; P93028; -.
DR ProteomicsDB; 243240; -.
DR EnsemblPlants; AT2G30110.1; AT2G30110.1; AT2G30110.
DR GeneID; 817562; -.
DR Gramene; AT2G30110.1; AT2G30110.1; AT2G30110.
DR KEGG; ath:AT2G30110; -.
DR Araport; AT2G30110; -.
DR TAIR; locus:2060854; AT2G30110.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; P93028; -.
DR OMA; CIREKCN; -.
DR OrthoDB; 91748at2759; -.
DR PhylomeDB; P93028; -.
DR BRENDA; 6.2.1.45; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:P93028; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93028; baseline and differential.
DR Genevisible; P93028; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0051707; P:response to other organism; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..1080
FT /note="Ubiquitin-activating enzyme E1 1"
FT /id="PRO_0000399395"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 656
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 600..601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT MUTAGEN 1032..1037
FT /note="RMDKKV->S: In mos5; enhanced disease
FT susceptibility."
FT /evidence="ECO:0000269|PubMed:17217463"
FT CONFLICT 883
FT /note="D -> G (in Ref. 4; AAP21171/AAL90910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1080 AA; 120251 MW; 4B442A35DAFD34D0 CRC64;
MLHKRASEAN DKNDNTIIGS DLASSKKRRI DFTESSSDKS SSILASGSSR GFHGDSVVQQ
IDMAFGNSNR QEIDEDLHSR QLAVYGRETM RRLFASNVLI SGMHGLGAEI AKNLILAGVK
SVTLHDERVV ELWDLSSNFV FSEDDVGKNR ADASVQKLQD LNNAVVVSSL TKSLNKEDLS
GFQVVVFSDI SMERAIEFDD YCHSHQPPIA FVKADVRGLF GSVFCDFGPE FAVLDVDGEE
PHTGIIASIS NENQAFISCV DDERLEFEDG DLVVFSEVEG MTELNDGKPR KIKSTRPYSF
TLDEDTTNYG TYVKGGIVTQ VKQPKLLNFK PLREALKDPG DFLFSDFSKF DRPPLLHLAF
QALDHFKAEA GRFPVAGSEE DAQKLISIAT AINTGQGDLK VENVDQKLLR HFSFGAKAVL
NPMAAMFGGI VGQEVVKACS GKFHPLFQFF YFDSVESLPS EPVDSSDFAP RNSRYDAQIS
VFGAKFQKKL EDAKVFTVGS GALGCEFLKN LALMGVSCGS QGKLTVTDDD IIEKSNLSRQ
FLFRDWNIGQ AKSTVAASAA AVINPRFNIE ALQNRVGAET ENVFDDAFWE NLTVVVNALD
NVNARLYVDS RCLYFQKPLL ESGTLGTKCN TQSVIPHLTE NYGASRDPPE KQAPMCTVHS
FPHNIDHCLT WARSEFEGLL EKTPAEVNAY LSSPVEYTNS MMSAGDAQAR DTLERIVECL
EKEKCETFQD CLTWARLRFE DYFVNRVKQL IYTFPEDAAT STGAPFWSAP KRFPRPLQYS
SSDPSLLNFI TATAILRAET FGIPIPEWTK NPKEAAEAVD RVIVPDFEPR QDAKIVTDEK
ATTLTTASVD DAAVIDDLIA KIDQCRHNLS PDFRMKPIQF EKDDDTNYHM DVIAGLANMR
ARNYSIPEVD KLKAKFIAGR IIPAIATSTA MATGLVCLEL YKVLDGGHKV EAYRNTFANL
ALPLFSMAEP LPPKVVKHRD MAWTVWDRWV LKGNPTLREV LQWLEDKGLS AYSISCGSCL
LFNSMFTRHK ERMDKKVVDL ARDVAKVELP PYRNHLDVVV ACEDEDDNDV DIPLVSIYFR
