ID A0A0L9TTW8_PHAAN Unreviewed; 436 AA.
AC A0A0L9TTW8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|ARBA:ARBA00015203, ECO:0000256|RuleBase:RU368009};
DE EC=6.2.1.64 {ECO:0000256|ARBA:ARBA00023624, ECO:0000256|RuleBase:RU368009};
GN ORFNames=LR48_Vigan01g318000 {ECO:0000313|EMBL:KOM33624.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM33624.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- FUNCTION: Catalytic subunit of the dimeric E1 enzyme, which activates
CC NEDD8. {ECO:0000256|RuleBase:RU368009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC protein]-yl-L-cysteine.; EC=6.2.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00024626,
CC ECO:0000256|RuleBase:RU368009};
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|RuleBase:RU368009}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000256|ARBA:ARBA00006310,
CC ECO:0000256|RuleBase:RU368009}.
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DR EMBL; CM003371; KOM33624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9TTW8; -.
DR STRING; 3914.A0A0L9TTW8; -.
DR EnsemblPlants; KOM33624; KOM33624; LR48_Vigan01g318000.
DR Gramene; KOM33624; KOM33624; LR48_Vigan01g318000.
DR OMA; ATSCNPY; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000053144; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR CDD; cd01488; Uba3_RUB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR014929; E2-binding.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030468; Uba3_N.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF6; NEDD8-ACTIVATING ENZYME E1 CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF08825; E2_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368009};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU368009};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368009};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 331..422
FT /note="E2 binding"
FT /evidence="ECO:0000259|SMART:SM01181"
FT ACT_SITE 208
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 436 AA; 48327 MW; 111A0228AADF795F CRC64;
MADTSSRSRD LDKLLLRPGN LVGPRFEPGA ELRDDLQAFA KVLVVGAGGL GCELLKDLAL
TGFRNLEVID MDRIEVTNLN RQFLFRLEDV GKPKAEVAAK RVMERISGVQ IVPHFCRIED
KEIEFYNDFS IIALGLDSVE ARSYINTVAC SFLEYESDDS PREETIKPMV DGGTEGFKGH
ARVILPGITP CFECTIWLFP PQVKFPLCTL AETPRTAAHC IEYAHLIKWN EVHGGVAFDP
DNPEHMKWVY DEAIKRAELF GIPGVTYSLT QGVVKNIIPA IASTNAIISA ACALETLKIA
TEYNGSAGLH TEVAEFERDK DCLVCGPGIR IELDTSITLQ KFMDLLEEHP KLRLSKASIT
HRGKNLYMQA PPVLEEMTRS NLSLSLFNLM GKLPKDVVHV NGMTIKNDQK FSCLRKLRVV
FKGVDGITDM DTAGGA
//
