UBCX_PICAN
ID UBCX_PICAN Reviewed; 188 AA.
AC O60015;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Ubiquitin-conjugating enzyme E2-21 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;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=9649431; DOI=10.1093/emboj/17.13.3608;
RA van der Klei I.J., Hilbrands R.E., Kiel J.A.K.W., Rasmussen S.W.,
RA Cregg J.M., Veenhuis M.;
RT "The ubiquitin-conjugating enzyme Pex4p of Hansenula polymorpha is required
RT for efficient functioning of the PTS1 import machinery.";
RL EMBO J. 17:3608-3618(1998).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Essential for peroxisome biogenesis. Required for UBC4-
CC independent ubiquitination of PEX5. {ECO:0000255|PROSITE-
CC ProRule:PRU00388}.
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 -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AF061604; AAC16238.1; -; Genomic_DNA.
DR PDB; 5NKZ; X-ray; 2.85 A; A/B=3-188.
DR PDB; 5NL8; X-ray; 2.20 A; A=3-188.
DR PDBsum; 5NKZ; -.
DR PDBsum; 5NL8; -.
DR AlphaFoldDB; O60015; -.
DR SMR; O60015; -.
DR UniPathway; UPA00143; -.
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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
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 3D-structure; ATP-binding; Nucleotide-binding; Peroxisome biogenesis;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..188
FT /note="Ubiquitin-conjugating enzyme E2-21 kDa"
FT /id="PRO_0000082557"
FT DOMAIN 3..182
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 119
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:5NL8"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:5NL8"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:5NL8"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:5NL8"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:5NL8"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5NKZ"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:5NKZ"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5NL8"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:5NL8"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5NL8"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:5NL8"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5NL8"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:5NL8"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:5NL8"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5NL8"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:5NL8"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5NL8"
SQ SEQUENCE 188 AA; 21531 MW; 0BC293A5E0787CB8 CRC64;
MSSTEKRLLK EYRAVKKELT EKRSPIHDTG IVDLHPLEDG LFRWSAVIRG PDQSPFEDAL
WKLEIDIPTN YPLDPPKIKF VVFGEEKIRQ LQRKTSSGAR KVCYKMPHPN VNFKTGEICL
DILQQKWSPA WTLQSALVAI VVLLANPEPL SPLNIDMANL LKCDDTTAYK DLVHYYIAKY
SAYESNDV
