ID   P93393_TOBAC            Unreviewed;      1080 AA.
AC   P93393;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 115.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN   Name=UBA1 {ECO:0000313|EMBL:CAA71762.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|EMBL:CAA71762.1};
RN   [1] {ECO:0000313|EMBL:CAA71762.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bright Yellow 2 {ECO:0000313|EMBL:CAA71762.1};
RC   TISSUE=Synchronised cell suspenssion culture
RC   {ECO:0000313|EMBL:CAA71762.1};
RA   Shen W.H., Gigot C.;
RT   "Ubiquitin activating enzye E1 of Nicotiana tabaccum.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAA71762.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bright Yellow 2 {ECO:0000313|EMBL:CAA71762.1};
RC   TISSUE=Synchronised cell suspenssion culture
RC   {ECO:0000313|EMBL:CAA71762.1};
RA   Shen W.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002457}.
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:0000256|ARBA:ARBA00000488};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR   EMBL; Y10804; CAA71762.1; -; mRNA.
DR   PIR; T03964; T03964.
DR   AlphaFoldDB; P93393; -.
DR   SMR; P93393; -.
DR   ProMEX; P93393; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0006974; P:DNA damage response; IEA:TreeGrafter.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR   CDD; cd01491; Ube1_repeat1; 1.
DR   CDD; cd01490; Ube1_repeat2; 1.
DR   FunFam; 3.40.50.12550:FF:000001; Ubiquitin-activating enzyme E1 1; 1.
DR   FunFam; 3.40.50.720:FF:000015; Ubiquitin-activating enzyme E1 1; 1.
DR   FunFam; 1.10.10.2660:FF:000002; Ubiquitin-activating enzyme E1 2; 1.
DR   FunFam; 3.10.290.60:FF:000001; Ubiquitin-activating enzyme E1 2; 1.
DR   FunFam; 2.40.30.180:FF:000001; ubiquitin-like modifier-activating enzyme 1; 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:SF4; UBIQUITIN-ACTIVATING ENZYME E1 C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 1.
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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000519};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000519};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          953..1075
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   REGION          52..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        656
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1080 AA;  120250 MW;  E714BDC40EF6A801 CRC64;
     MLPVKRTVEV GGENDTVSVD PLTKKHKATA AAAGDSSTVT MGGAGSAITG DVNANGNATN
     GKSPIDARNS PDIDEDLHSR QLAVYGRETM RRLFASNVLV SGLQGLGAEI AKNLILAGVK
     SVTLHDEGMW NCGIYLAILF LQRKMLGRIG HLLLSRKLQE LNNAVIISTL TDALTKEQLS
     NFQAVVFTDI SLEKAVKFDD YCHQHQPPIA FIKAEVRGLF GSVFCDFGPE FTIADVDGED
     PHTGIIASIS NDNPALVGCI DDERLEFQDG DLVIFSEVRG MTELNDGKPR KIKNARPYSF
     TIEEDTSNYA AYERGGIVTQ VKEPKVLKFK PLREAIKDPG DFLLSDFSKF DRPPILHLAF
     QALDRFVSES GRFPLAGSEE DAQRLISFVT DLNNSLSDGK LEEIDQKLLR NFAFGARAVL
     NPMAAMFGGI VGQEVVKACS GKFHPLYQFF YFDSVESLPT APLDPNDLKP LNSRYDAQIS
     VFGNKLQKKL EEAKAFVVGS GALGCEFLKN LALMGVCCGD KGKLTITDDD VIEKSNLSRQ
     FLFRDWNIGQ AKSTVAAAAA SLINPRIHIE ALQNRASPET ESVFDDTFWE NLSVVINALD
     NVNARLYIDQ RCLYFQKPLL ESGTLGAKCN TQMVIPHLTE NYGASRDPPE KQAPMCTVHS
     FPHNIDHCLT WARSEFEGLL EKTPTEVNAY LINPSDYISA MQKAGDAQAR DTLDRVLECL
     DKERCDTFQD CITWARLRFE DYFADRVKQL TFTFPEEATT SSGAPFWSAP KRFPRPLQFS
     VDDASHLQFL LAASILRAET FGILIPDWVK SPQKLAEAVD KVIVPDFQPK KDVKIVTDEK
     ATSMAASSID DAAVINELVM KLETCRQKLP SGYKMNPIQF EKDDDTNYHM DLIAGLANMR
     ARNYSIPEVD KLKAKFIAGR IIPAIATSTA MATGLVCLEL YKVLDGGHKV EDYRNTFANL
     ALPLFSMAEP VPPKVVKHQD MNWTVWDRWI LKDNPTLREL LQWLQNKGLN AYSISYGSCL
     LYNSMFPKHK ERMDRKLVDL AREVAKADLP PYRKHFDVVV ACEDEEDNDV DIPQMSIYFR
//