ID   UBCX_PICPA              Reviewed;         204 AA.
AC   P49428;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-24 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme PEX4;
DE   AltName: Full=Peroxin-4;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=PEX4; Synonyms=PAS4;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8063827; DOI=10.1016/s0021-9258(17)31879-3;
RA   Crane D.I., Kalish J.E., Gould S.J.;
RT   "The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme
RT   required for peroxisome assembly.";
RL   J. Biol. Chem. 269:21835-21844(1994).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Essential for peroxisome biogenesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC         ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; U12511; AAA53634.1; -; Genomic_DNA.
DR   PIR; A53848; A53848.
DR   AlphaFoldDB; P49428; -.
DR   SMR; P49428; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding; Peroxisome; Peroxisome biogenesis;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..204
FT                   /note="Ubiquitin-conjugating enzyme E2-24 kDa"
FT                   /id="PRO_0000082567"
FT   DOMAIN          2..196
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        133
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MUTAGEN         133
FT                   /note="C->S,A: Loss of activity."
SQ   SEQUENCE   204 AA;  23566 MW;  46680ABD73121F6C CRC64;
     MSAEKRLLQE YRSILKEQRQ KGSASTLSSN GILDLKPVSE DNFYKWTAKL KGPTDTGYQD
     AFWELQIDIP SNYPTQPPKF TFIVSDDIPR NRRQRQTNQI QDDDEFEGAE KEVLRHCYRM
     PHPNIAFNTG EICLDILQAK WTPAWTLSSA LTAIVLLLND PEPLSPLDID MANLMKINDL
     KAYNSLIEYY VGRYSIEEEV YILN