CEFD2_ACRCH
ID CEFD2_ACRCH Reviewed; 383 AA.
AC Q8J0F0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Isopenicillin N epimerase component 2;
DE Short=IPN epimerase component 2;
DE EC=5.1.1.17;
DE AltName: Full=Isopenicillin N epimerase acyl-CoA racemase component;
DE EC=5.1.99.-;
GN Name=cefD2;
OS Acremonium chrysogenum (Cephalosporium acremonium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=5044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 48278 / C10;
RX PubMed=12228250; DOI=10.1074/jbc.m207482200;
RA Ullan R.V., Casqueiro J., Banuelos O., Fernandez F.J., Gutierrez S.,
RA Martin J.F.;
RT "A novel epimerization system in fungal secondary metabolism involved in
RT the conversion of isopenicillin N into penicillin N in Acremonium
RT chrysogenum.";
RL J. Biol. Chem. 277:46216-46225(2002).
CC -!- FUNCTION: Together with cefD1, catalyzes the reversible isomerization
CC between isopenicillin N and penicillin N. This two-component IPN
CC epimerase system may function by two sequential steps, an activation of
CC isopenicillin N by the acyl-CoA synthase component cefD1, followed by
CC epimerization by the acyl-CoA racemase component cefD2.
CC {ECO:0000269|PubMed:12228250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isopenicillin N = penicillin N; Xref=Rhea:RHEA:20033,
CC ChEBI:CHEBI:58399, ChEBI:CHEBI:58408; EC=5.1.1.17;
CC -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR EMBL; AJ507632; CAD45624.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8J0F0; -.
DR SMR; Q8J0F0; -.
DR UniPathway; UPA00172; -.
DR GO; GO:0045439; F:isopenicillin-N epimerase activity; IMP:UniProtKB.
DR GO; GO:0042318; P:penicillin biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Isomerase.
FT CHAIN 1..383
FT /note="Isopenicillin N epimerase component 2"
FT /id="PRO_0000418514"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 383 AA; 41397 MW; 64179554E671E209 CRC64;
MDPSRPHPLS GKLVVELAGL APGPFCGMLL ADYGASVLRI DGPRSPKGDV LARNKSSICI
DLKHPPSRKV LLSILSRADV LIDPFRPGVL ERLGLSPTEV LLKANARLVV ARLTGFRRDG
KYQDMAGHDI NYLAVSGVLA MLGRAGENPF PPANILGDFA GGGAMCVVGI LLALVSRDAT
GLGQVVEANM VDGSAYLATM PRLATKTPFW GSPRGENVLD GGCPWYATYR TKDPGGKYMA
VGALEPHFYE VLVRGLGLDK TDLPPREDRA NWPRLRALFE AKFAERTRSE WAEVFDGTDA
CVTPVLEQGE LEKAGFEQRL PVNLGATPGK PILPGQGDWT GRTLAKGHGG EEILRRWIGW
ERGVDYHVEE NSGILVACSR EKL