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Database: UniProt
Entry: M0FMY8_9EURY
LinkDB: M0FMY8_9EURY
Original site: M0FMY8_9EURY 
ID   M0FMY8_9EURY            Unreviewed;       378 AA.
AC   M0FMY8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Mandelate racemase {ECO:0000313|EMBL:ELZ60637.1};
GN   ORFNames=C459_16271 {ECO:0000313|EMBL:ELZ60637.1};
OS   Haloferax sp. ATCC BAA-645.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1227463 {ECO:0000313|EMBL:ELZ60637.1, ECO:0000313|Proteomes:UP000011673};
RN   [1] {ECO:0000313|EMBL:ELZ60637.1, ECO:0000313|Proteomes:UP000011673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-645 {ECO:0000313|EMBL:ELZ60637.1,
RC   ECO:0000313|Proteomes:UP000011673};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ60637.1}.
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DR   EMBL; AOLE01000036; ELZ60637.1; -; Genomic_DNA.
DR   RefSeq; WP_008572962.1; NZ_AOLE01000036.1.
DR   AlphaFoldDB; M0FMY8; -.
DR   PATRIC; fig|1227463.4.peg.3251; -.
DR   Proteomes; UP000011673; 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   CDD; cd03316; MR_like; 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; 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   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.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   4: Predicted;
FT   DOMAIN          145..241
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   REGION          341..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  41285 MW;  F1244041B6ED2E7E CRC64;
     MHVTDIEVIP ISHRLPDGQG LGDARGFGHD RATTLIRVDT DTGEVGWGEA FAPGSVVVPV
     VDEFFRDDVV GMDPFDVRRL AEESYTDPYH FGGSVFVQSA LSGIDVALWD LVGKATGKPV
     HRLLGGTPRE TLTAYASTMY FTEANRDIAA PIRDAVDEGF SAAKIKIGTG TDSDVERVRT
     ARQLLGDDAR LMVDINGNYR PRQAIRTAKA IEEFDITWME EPVPPENLSG YREVKRGVDV
     PLAAGEAHYG RFEFKRLVDD RTVDVVQPNL GRCGGLSEAS RIADLASTEN VAVRPHVWNS
     AVGLAAAVQF AASVSDYPHT RHVPDPMMVE FDRSENPLRD EILKSPFDPT GGEVDVPQGP
     GLGVDIDEDA LERYRADN
//
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