UBA3_YEAST
ID UBA3_YEAST Reviewed; 299 AA.
AC Q99344; D6W470; E9P8X1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit;
DE EC=6.2.1.64;
DE AltName: Full=RUB1-activating enzyme E1;
DE AltName: Full=Ubiquitin-activating enzyme E1 3;
DE AltName: Full=Ubiquitin-like protein-activating enzyme;
GN Name=UBA3; OrderedLocusNames=YPR066W; ORFNames=YP9499.21;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 200912 / DF5;
RX PubMed=9545234; DOI=10.1093/emboj/17.8.2208;
RA Liakopoulos D., Doenges G., Matuschewski K., Jentsch S.;
RT "A novel protein modification pathway related to the ubiquitin system.";
RL EMBO J. 17:2208-2214(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalytic subunit of the dimeric UBA3-ULA1 E1 enzyme. E1
CC activates NEDD8/RUB1 by first adenylating its C-terminal glycine
CC residue with ATP, thereafter linking this residue to the side chain of
CC the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP.
CC E1 finally transfers NEDD8 to the catalytic cysteine of UBC12.
CC {ECO:0000269|PubMed:9545234}.
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 -!- PATHWAY: Protein modification; protein neddylation.
CC -!- SUBUNIT: Heterodimer of UBA3 and ULA1. Interacts with NEDD8 and UBC12
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q99344; Q12059: ULA1; NbExp=4; IntAct=EBI-37997, EBI-32882;
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000305}.
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DR EMBL; Y16891; CAA76517.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94974.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89183.1; -; Genomic_DNA.
DR EMBL; AY692781; AAT92800.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11486.1; -; Genomic_DNA.
DR PIR; S54087; S54087.
DR RefSeq; NP_015391.1; NM_001184163.1.
DR AlphaFoldDB; Q99344; -.
DR SMR; Q99344; -.
DR BioGRID; 36238; 339.
DR ComplexPortal; CPX-1414; UBA3-ULA1 E1 enzyme.
DR DIP; DIP-1719N; -.
DR IntAct; Q99344; 3.
DR MINT; Q99344; -.
DR STRING; 4932.YPR066W; -.
DR MaxQB; Q99344; -.
DR PaxDb; Q99344; -.
DR PRIDE; Q99344; -.
DR EnsemblFungi; YPR066W_mRNA; YPR066W; YPR066W.
DR GeneID; 856179; -.
DR KEGG; sce:YPR066W; -.
DR SGD; S000006270; UBA3.
DR VEuPathDB; FungiDB:YPR066W; -.
DR eggNOG; KOG2015; Eukaryota.
DR GeneTree; ENSGT00550000074831; -.
DR HOGENOM; CLU_013325_13_0_1; -.
DR InParanoid; Q99344; -.
DR OMA; CGGSCEW; -.
DR BioCyc; YEAST:G3O-34214-MON; -.
DR BRENDA; 6.2.1.64; 984.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00885; -.
DR PRO; PR:Q99344; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q99344; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0120123; C:ubiquitin activating enzyme complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IDA:SGD.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IDA:SGD.
DR Gene3D; 1.10.10.520; -; 1.
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.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF6; PTHR10953:SF6; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..299
FT /note="NEDD8-activating enzyme E1 catalytic subunit"
FT /id="PRO_0000194950"
FT ACT_SITE 168
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 12..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 33
FT /note="V -> L (in Ref. 4; AAT92800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 33278 MW; 2C355EF52AB8092F CRC64;
MDCKILVLGA GGLGCEILKN LTMLSFVKQV HIVDIDTIEL TNLNRQFLFC DKDIGKPKAQ
VAAQYVNTRF PQLEVVAHVQ DLTTLPPSFY KDFQFIISGL DAIEPRRFIN ETLVKLTLES
NYEICIPFID GGTEGLKGHV KTIIPGITAC WECSIDTLPS QQDTVPMCTI ANNPRCIEHV
VEYVSTIQYP DLNIESTADM EFLLEKCCER AAQFSISTEK LSTSFILGII KSIIPSVSTT
NAMVAATCCT QMVKIYNDLI DLENGNNFTL INCSEGCFMY SFKFERLPDC TVCSNSNSN
