UBE12_WHEAT
ID UBE12_WHEAT Reviewed; 1051 AA.
AC P31251;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ubiquitin-activating enzyme E1 2;
DE EC=6.2.1.45 {ECO:0000250|UniProtKB:P20973};
GN Name=UBA2;
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].
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:0000250|UniProtKB:P20973}.
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:0000250|UniProtKB:P20973};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P20973}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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:0000250|UniProtKB:P20973}.
CC -!- MISCELLANEOUS: There are multiple genes encoding E1 in wheat.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; M90663; AAA34265.1; -; mRNA.
DR AlphaFoldDB; P31251; -.
DR SMR; P31251; -.
DR STRING; 4565.Traes_5DL_0BE2B1D42.2; -.
DR PRIDE; P31251; -.
DR eggNOG; KOG2012; Eukaryota.
DR BioCyc; MetaCyc:MON-16753; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P31251; baseline and differential.
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: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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..1051
FT /note="Ubiquitin-activating enzyme E1 2"
FT /id="PRO_0000194964"
FT REPEAT 56..194
FT /note="1-1"
FT REPEAT 453..605
FT /note="1-2"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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"
SQ SEQUENCE 1051 AA; 116826 MW; B1F8370F6A299B73 CRC64;
MLPRKREIVA GEVEDLQKKT RAGEGEATRE EGDAAMAGRG NEIDEDLHSR QLAVYGRETM
KPLFGSNVLV SGLQGLGAEI AKNLVLAGVK SVTLHDDGNV ELWDLSSNFF LSENDVGQNR
AQACVQKLQE LNNAVLVSAL TGDLTKEHLS KFQAVVFTDI SLDKAIEFDD YCHSHQPPIA
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 VFGSTLQNKL EEAKIFMVGS GALGCEFLKN
LALMGISCSQ NGNLTVTDDD 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 SSDPSQLSFI LAAAILRAET FGIPISEWAK
TPNKLAAEAV DKVIVPDFQP KQGVKIVTDE 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
