ID F2PKL1_TRIEC Unreviewed; 385 AA.
AC F2PKL1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Mandelate racemase/muconate lactonizing enzyme family protein {ECO:0000313|EMBL:EGE02429.1};
GN ORFNames=TEQG_01465 {ECO:0000313|EMBL:EGE02429.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; DS995722; EGE02429.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PKL1; -.
DR VEuPathDB; FungiDB:TEQG_01465; -.
DR eggNOG; ENOG502QRWW; Eukaryota.
DR HOGENOM; CLU_030273_3_2_1; -.
DR Proteomes; UP000009169; 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; SFLDG00179; mandelate_racemase; 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;
FT DOMAIN 126..228
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 385 AA; 43018 MW; C480D8983501F8B0 CRC64;
MAKIKTIEHF RVLPRWLFVK ITDEQGGYGW GESTLEGHSE SIEGTLNAFS RQIQGYEADD
IEHIWQTAWR QGFYRGGPVF MSALSGIDIA LWDLKAKRLG VPIYQLLGGK VRNKISVYAW
IGGDRPADVK AAGLSRLAQG FKAIKMNATE DINWLDSPRT LEASVERLKT VKNLGLDAAL
DFHGRLHKPM AKQLAKMVEP YQPLFIEEPL LSEHPEGIKQ LSSQTTTPIA LGERLYNRWD
VKRFLEDSSV DILQPDISHC GGISELRRIA AMAETYDVAI APHCPLGPIA LAACMQVDLS
IPNFVIQEMS LGIHYNTTES GEEYDITNYI KDRSVFDVKD GYVKALEGPG LGIEVDEEEV
RRVSKGAKPW VTTGFFGPDG SIREW
//
