ID G3B8A1_CANTC Unreviewed; 455 AA.
AC G3B8A1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-MAY-2023, entry version 44.
DE SubName: Full=Enolase C-terminal domain-like protein {ECO:0000313|EMBL:EGV61724.1};
GN ORFNames=CANTEDRAFT_135663 {ECO:0000313|EMBL:EGV61724.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV61724.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; GL996527; EGV61724.1; -; Genomic_DNA.
DR RefSeq; XP_006687894.1; XM_006687831.1.
DR AlphaFoldDB; G3B8A1; -.
DR STRING; 590646.G3B8A1; -.
DR GeneID; 18249897; -.
DR KEGG; cten:CANTEDRAFT_135663; -.
DR eggNOG; ENOG502QU7C; Eukaryota.
DR HOGENOM; CLU_030273_2_0_1; -.
DR OrthoDB; 2903547at2759; -.
DR Proteomes; UP000000707; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProt.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
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; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR046945; RHMD-like.
DR PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDS00001; Enolase; 1.
DR SFLD; SFLDF00270; L-galactonate_dehydratase; 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; PS00909; MR_MLE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT DOMAIN 202..299
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 455 AA; 50195 MW; 7AD66B69937966D7 CRC64;
MSLDSIVITG FKVYDIRFPT SLDGIGSDAM HVGTNGSHPY LQLLTSSDVI GEGMAFSNGR
GSDLVCAAIE PFAERVVGKT LASLVENMGV TWRYMVSDSQ YRWLGPEKSI THLATAAVIN
AIWDLWGKAT NRPVWKIVAD MTPEEIVRCV DFRYILDVIN PEEAVEMLKK TQVGKEARIQ
EAFDNVAVPA YTTSAGWLAF SGDKMKRVLQ ETIDAGFKIF KFKVGSDLEA DKERLEAVRD
IIGYDNEYQI MLDANQVWSV PEAIEWMKQL VKFKPVFIEE PTSPDDILGH ATIRKALKPF
GVGVATGEMA ANRVIFKQLL QAESIDVCQI DAVRLGGVNE CLAVMLMALK FDVPCVPHNG
AMGLTELTSH LSTIDYIAIS GRKSMLEAAE SYRENLAHPC VIKDAHYVTP LDPGYSIGYV
PGAIDKFLYP NGTFWTSKVG EEIKRAPKGG EGLIR
//
