ID A0A0A2IH55_PENEN Unreviewed; 383 AA.
AC A0A0A2IH55;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Mandelate racemase/muconate lactonizing enzyme, C-terminal {ECO:0000313|EMBL:KGO56441.1};
GN ORFNames=PEX2_080480 {ECO:0000313|EMBL:KGO56441.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO56441.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO56441.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO56441.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO56441.1}.
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DR EMBL; JQFZ01000170; KGO56441.1; -; Genomic_DNA.
DR RefSeq; XP_016598236.1; XM_016745318.1.
DR AlphaFoldDB; A0A0A2IH55; -.
DR STRING; 27334.A0A0A2IH55; -.
DR GeneID; 27680738; -.
DR HOGENOM; CLU_030273_3_2_1; -.
DR OrthoDB; 1691455at2759; -.
DR PhylomeDB; A0A0A2IH55; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0008869; F:galactonate dehydratase activity; IEA:InterPro.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR GO; GO:0034194; P:D-galactonate catabolic process; IEA:InterPro.
DR CDD; cd03325; D-galactonate_dehydratase; 1.
DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR InterPro; IPR034593; DgoD-like.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR023592; Galactonate_deHydtase.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080:SF2; D-GALACTONATE DEHYDRATASE; 1.
DR PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00003; D-galactonate_dehydratase; 1.
DR SFLD; SFLDS00001; Enolase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 126..228
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 383 AA; 42749 MW; 77CC51890C374031 CRC64;
MAKIKSIEYF RVKPRWLFVK VTDEEGRFGW GEGTLEGHSL AVEGALDEII TRIVGYEAND
IQHIWQTVWR LGFYRGGPVF MSALSGIDIA LWDLKGRRLG VPVHELLGGK VRQKVQVYAW
IGGDRPSDVE AAAKERIAQG LKCVKMNATE DVNWLDSPAV LQSCVERLKQ VKALGLDAGL
DFHGRLHRPM AKQLAKALEP YHPLFIEEPL LCEHPEAIKQ LSEQTTIPIA FGERLYSRWD
IKRFLEDSSV DILQPDIAHA GGISETLRIA NMAEAYDVAI APHCPLGPIA LAASLQVAVS
IPNFVIQEMS LGMHYNVEAG DIDLNSYLVD KTVFDIKEGY VAAPSKPGLG IDIDEDLVRK
ISKETEPWQP KEFYGPDGSI REW
//
