ID A0A4Y7L0Y8_PAPSO Unreviewed; 1072 AA.
AC A0A4Y7L0Y8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=C5167_002291 {ECO:0000313|EMBL:RZC78098.1};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469 {ECO:0000313|EMBL:RZC78098.1, ECO:0000313|Proteomes:UP000316621};
RN [1] {ECO:0000313|EMBL:RZC78098.1, ECO:0000313|Proteomes:UP000316621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HN1 {ECO:0000313|Proteomes:UP000316621};
RC TISSUE=Leaves {ECO:0000313|EMBL:RZC78098.1};
RX PubMed=30166436; DOI=.1126/science.aat4096;
RA Guo L., Winzer T., Yang X., Li Y., Ning Z., He Z., Teodor R., Lu Y.,
RA Bowser T.A., Graham I.A., Ye K.;
RT "The opium poppy genome and morphinan production.";
RL Science 362:343-347(2018).
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 -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR EMBL; CM010723; RZC78098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y7L0Y8; -.
DR STRING; 3469.A0A4Y7L0Y8; -.
DR EnsemblPlants; RZC78098; RZC78098; C5167_002291.
DR Gramene; RZC78098; RZC78098; C5167_002291.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000316621; Chromosome 9.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000316621};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 945..1067
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 648
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1072 AA; 119163 MW; 4D4B1B7855FA8E3A CRC64;
MLPCKRAAVG GESVLVGGGE KEENNNPNSS ITALIKKSRN SAGGDDENQT RVSAMALGDG
NSHEIDEDLH SRQLAVYGRE TMRRLFASNI LVSGMQGLGA EIAKNLILAG VKSVTLHDEG
NVELWDLSSN FIFSEDDVGK NRAVASVTKL QELNNAVLIS ALSTPLTTDQ LSNFQAVVFT
DVNLEKAFEF DEFCRSQEPP IAFIKTEVRG LFGSVFCDFG PNFTVLDVDG EEPHTGIIVS
ISNDNPALVS CVDDERLEFQ DGDLVLFSEV QGMPELNDGK PRKVKNTRPY SFNLDEDTTN
YGAYARGGIV TQVKQPKLLN FKSLREALKD PGDFLLSDFS KFDRPPLLHL AFQALDKFTT
ELQRFPVAGS EEDADKLISV AIAINEASED ARLEEVDKKI LRHFAFGARA VLNPMAAMFG
GIVGQEVMKA CSGKFHPLYQ FFYFDSLESL PTEPLDASDL KPQNSRYDAQ ISVFGSKIQK
KLEDAKVFMV GSGALGCEFL KNLALMGVCC NQQGKLTITD DDVIEKSNLS RQFLFRDWNI
GQGKSTVAAS AASSINPSLH VEALQNRASP ETENVFNDAF WENLDVVINA LDNVNARMYM
DQRCLYFQKP LLESGTLGAK CNTQMVIPHL TENYGASRDP PEKQAPMCTV HSFPHNIDHC
LTWARSEFEG LLEKTPAEAN AYLSNRSEYN AAMKTAGDAQ ARDNLERVIE CLDSERCESF
QDCITWARLK FGDYFANRVK QLTFTFPEDS ATSSGAPFWS APKRFPRPLE FSVDDPGHIN
FVMAGAILRA ETFGIPLPDW AKNPNKLADA VSKVIVPDFQ PKQGVKIVTD EKATNVSAAS
VDDDAVINDL ILRLENCFTK LPPGFKMNPI QFEKDDDTNY HMDMIAGLAN MRARNYSIPE
VDKLKAKFIA GRIIPAIATA TAMATGLVCL ELYKVIDGGH KLEDYRNTFA NLALPLFSIA
EPVPPKTFKH RDMSWTVWDR WIIRNNPTLK ELLQWMEDKG LNAYSISCGT CLLYNSMFSR
HRDRMDRTVV DLATEVARLE IPPYRNHVDV VVACDDDEDN DVDIPQVSVY FR
//
