ID UBE11_WHEAT Reviewed; 1051 AA.
AC P20973;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Ubiquitin-activating enzyme E1 1;
DE EC=6.2.1.45 {ECO:0000269|PubMed:1634524};
GN Name=UBA1 {ECO:0000303|PubMed:1634524};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Augusta;
RX PubMed=2203788; DOI=10.1016/s0021-9258(18)55470-3;
RA Hatfield P.M., Callis J., Vierstra R.D.;
RT "Cloning of ubiquitin activating enzyme from wheat and expression of a
RT functional protein in Escherichia coli.";
RL J. Biol. Chem. 265:15813-15817(1990).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF CYSTEINE RESIDUES,
RP AND ACTIVE SITE.
RX PubMed=1634524; DOI=10.1016/s0021-9258(18)42110-2;
RA Hatfield P.M., Vierstra R.D.;
RT "Multiple forms of ubiquitin-activating enzyme E1 from wheat.
RT Identification of an essential cysteine by in vitro mutagenesis.";
RL J. Biol. Chem. 267:14799-14803(1992).
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:1634524}.
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:1634524};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:1634524}.
CC -!- SUBUNIT: Monomer.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC allowing it to accommodate two ubiquitin moieties at a time, with a new
CC ubiquitin forming an adenylate intermediate as the previous one is
CC transferred to the thiol site. {ECO:0000305}.
CC -!- MISCELLANEOUS: There are multiple genes encoding E1 in wheat.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M55604; AAA34308.1; -; mRNA.
DR AlphaFoldDB; P20973; -.
DR SMR; P20973; -.
DR STRING; 4565.P20973; -.
DR PaxDb; 4565-Traes_5BL_87CFD581E-1; -.
DR eggNOG; KOG2012; Eukaryota.
DR BioCyc; MetaCyc:MONOMER-16752; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P20973; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006974; P:DNA damage response; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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:SF204; UBIQUITIN-ACTIVATING ENZYME E1 1; 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; Direct protein sequencing; Ligase; Nucleotide-binding;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..1051
FT /note="Ubiquitin-activating enzyme E1 1"
FT /id="PRO_0000194963"
FT REPEAT 56..194
FT /note="1-1"
FT REPEAT 453..605
FT /note="1-2"
FT REGION 56..605
FT /note="2 approximate repeats"
FT ACT_SITE 626
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132,
FT ECO:0000269|PubMed:1634524"
FT BINDING 472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 570..571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT MUTAGEN 626
FT /note="C->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:1634524"
SQ SEQUENCE 1051 AA; 117008 MW; 9BAB85FE3BACA621 CRC64;
MLPRKREIVA GEVEDLQKKT RAGEGEVTRE EGDAAMAGRG NEIDEDLHSR QLAVYGRETM
KRLFGSNVLV SGLQGLGAEI AKNLVLAGVK SVTLHDDGNV ELWDLSSNFF LSENDVGQNR
AQACVQKLQE LNNAVLVSAL TGDLTKEHLS KFQAVVFTDI SLDKAIEFDD YCHSQQPPIA
FIKSEVRGLF GSVFCDFGPE FTVLDVDGEE PHTGIVASIS NDNPALVSCV DDERLEFQDG
DLVVFSEVHG MTELNDGKPR KVKNARPYSF FLEEDTSSFG AYVRGGIVTQ VKPPKVIKFK
PLKEAMSEPG EFLMSDFSKF ERPPLLHLAF QALDKFRTEL SRFPVAGSTD DVQRVIEYAI
SINDTLGDRK LEEIDKKLLH HFASGSRAVL NPMAAMFGGI VGQEVVKACS GKFHPLYQFF
YFDSVESLPV DPLEPGDLKP KNSRYDAQIS VFGSKLQNKL EEAKIFMVGS GALGCEFLKN
LALMGISCSQ NGNLTLTDDD VIEKSNLSRQ FLFRDWNIGQ PKSTVAATAA MVINPKLHVE
ALQNRASPET ENVFNDAFWE NLDAVVNALD NVTARMYIDS RCVYFQKPLL ESGTLGAKCN
TQMVIPHLTE NYGASRDPPE KQAPMCTVHS FPHNIDHCLT WARSEFEGLL EKTPTEVNAF
LSNPTTYISA ARTAGDAQAR DQLERVIECL DRDKCETFQD SITWARLKFE DYFSNRVKQL
TFTFPEDSMT SSGAPFWSAP KRFPRPVEFS SSDQSQLSFI LAAAILRAET FGIPIPEWAK
TPNKLAAEAV DKVIVPDFQP KQGVKIVTHE KATSLSSASV DDAAVIEELI AKLEEVSKTL
PSGFHMNPIQ FEKDDDTNFH MDVIAGFANM RARNYSIPEV DKLKAKFIAG RIIPAIATST
AMATGLVCLE LYKALAGGHK VEDYRNTFAN LAIPLFSIAE PVPPKTIKHQ ELSWTVWDRW
TVTGNITLRE LLEWLKEKGL NAYSISCGTS LLYNSMFPRH KERLDRKVVD VAREVAKMEV
PSYRRHLDVV VACEDDDDND VDIPLVSVYF R
//
