ID UBE12_ARATH Reviewed; 1077 AA.
AC P92974;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Ubiquitin-activating enzyme E1 2;
DE Short=AtUBA2 {ECO:0000303|PubMed:9076989};
DE EC=6.2.1.45 {ECO:0000269|PubMed:9076989};
GN Name=UBA2; OrderedLocusNames=At5g06460; ORFNames=MHF15.2;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 DISRUPTION PHENOTYPE.
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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: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 -!- DISRUPTION PHENOTYPE: No visible phenotype and no changes in disease
CC susceptibility. {ECO:0000269|PubMed:17217463}.
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 -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; U40566; AAB37569.1; -; Genomic_DNA.
DR EMBL; AB006700; BAB08968.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91020.1; -; Genomic_DNA.
DR RefSeq; NP_568168.1; NM_120729.4.
DR AlphaFoldDB; P92974; -.
DR SMR; P92974; -.
DR BioGRID; 15813; 31.
DR IntAct; P92974; 1.
DR STRING; 3702.P92974; -.
DR iPTMnet; P92974; -.
DR PaxDb; 3702-AT5G06460-1; -.
DR ProteomicsDB; 228718; -.
DR EnsemblPlants; AT5G06460.1; AT5G06460.1; AT5G06460.
DR GeneID; 830534; -.
DR Gramene; AT5G06460.1; AT5G06460.1; AT5G06460.
DR KEGG; ath:AT5G06460; -.
DR Araport; AT5G06460; -.
DR TAIR; AT5G06460; UBA 2.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; P92974; -.
DR OMA; ERMDRKM; -.
DR OrthoDB; 20494at2759; -.
DR PhylomeDB; P92974; -.
DR BRENDA; 2.3.2.23; 399.
DR BRENDA; 6.2.1.45; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:P92974; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92974; baseline and differential.
DR Genevisible; P92974; AT.
DR GO; GO:0005634; C:nucleus; TAS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR CDD; cd01491; Ube1_repeat1; 1.
DR CDD; cd01490; Ube1_repeat2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 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 NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF235; UBIQUITIN-ACTIVATING ENZYME E1 2; 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_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
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..1077
FT /note="Ubiquitin-activating enzyme E1 2"
FT /id="PRO_0000399396"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 653
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 597..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
SQ SEQUENCE 1077 AA; 119624 MW; CE39A36AAA99A218 CRC64;
MEPFVVKENI IASASSPMKK RRIDHTESAD GSAINASNSS SIGLNNSIGG NDTVMSMAEF
GNDNSNNQEI DEDLHSRQLA VYGRETMRKL FASNVLISGM QGLGVEIAKN IILAGVKSVT
LHDENVVELW DLSSNFVFTE EDIGKNRALA SVHKLQELNN AVAVSTLTGK LTKEQLSDFQ
VVVFVDISFE KATEIDDYCH SHQPPIAFIK ADVRGLFGSL FCDFGPHFTV LDVDGEEPHS
GIIASVSNEN PGFVSCVDDE RLEFEDGNLV VFSEVEGMTE LNDGKPRKIK NVKPFSFTLE
EDTSSYGQYM KGGIVTQVKQ PKVLNFKPLR EALKDPGDFL LSDFSKFDRP PLLHLAFQAL
DRFSSQAGRF PFAGSEEDAQ KLVEIAVDIN EGLGDARLED VNSKLLRHLA FGSRAVLNPM
AAMFGGIVGQ EVVKACSGKF HPIFQFFYFD SVESLPKEPL DASEFRPQNS RYDAQISVFG
STLQKKLEDA RVFVVGAGAL GCEFLKNLAL MGVSCGTQGK LTVTDDDVIE KSNLSRQFLF
RDWNIGQAKS TVAATAAAGI NSRLNIDALQ NRVGPETENV FDDSFWENLT VVVNALDNVT
ARLYVDSRCV YFQKPLLESG TLGAKCNTQM VIPHLTENYG ASRDPPEKQA PMCTVHSFPH
NIDHCLTWAR SEFEGLLEKT PAEVNAYLSD PVEYMKAMRT AGDAQARDTL GRVVECLEKE
KCNSFQDCIT WARLRFEDYF ANRVKQLCYT FPEDAATSTG APFWSAPKRF PRPLQFSSTD
LSHINFVMAA SILRAETFGI PTPEWAKTRA GLAEAVERVI VPDFEPKKDA TIVTDEKATT
LSTASVDDAA VIDELNAKLV RCRMSLQPEF RMKAIQFEKD DDTNYHMDMI AGLANMRARN
YSVPEVDKLK AKFIAGRIIP AIATSTAMAT GFVCLEMYKV LDGSHKVEDY RNTFANLALP
LFSMAEPVPP KVVKHQDQSW TVWDRWVMRG NPTLRELLDW LKEKGLNAYS ISCGSSLLYN
SMFSRHKERM NRRVVDLARD VAGVELPAYR RHVDVVVACE DDNDADVDIP LVSVYFA
//
