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Database: UniProt
Entry: A0A1I1FKY5_9LACT
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ID   A0A1I1FKY5_9LACT        Unreviewed;       399 AA.
AC   A0A1I1FKY5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Mannonate dehydratase {ECO:0000313|EMBL:SFC00067.1};
GN   ORFNames=SAMN04488102_102155 {ECO:0000313|EMBL:SFC00067.1};
OS   Alkalibacterium subtropicum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=753702 {ECO:0000313|EMBL:SFC00067.1, ECO:0000313|Proteomes:UP000199612};
RN   [1] {ECO:0000313|EMBL:SFC00067.1, ECO:0000313|Proteomes:UP000199612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23664 {ECO:0000313|EMBL:SFC00067.1,
RC   ECO:0000313|Proteomes:UP000199612};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has no detectable activity with D-mannonate and with a panel
CC       of 70 other acid sugars (in vitro), in spite of the conservation of the
CC       residues that are expected to be important for catalytic activity and
CC       cofactor binding. May have evolved a divergent function.
CC       {ECO:0000256|ARBA:ARBA00003553}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000256|ARBA:ARBA00010339}.
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DR   EMBL; FOLT01000002; SFC00067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1FKY5; -.
DR   STRING; 753702.SAMN04488102_102155; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000199612; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; 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; IPR034589; D-mannonate_dehydratase-like.
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; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF6; STARVATION-SENSING PROTEIN RSPA; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDG00033; mannonate_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; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          132..252
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   399 AA;  45118 MW;  AE0419A63C8ACB06 CRC64;
     MKPTIITNIK SYGIKPDRHN LVVVKVETDK GVSGLGCATF QFRPLAVQSL VDDYLKPLLV
     GKDANNIEDL WHLMTVNAYW RNGPVINNAI SGVDMALWDI KGKLSDMPLY QLLGGKSRNK
     VSAYAHAVGD TLDELFEQID THLANGFRYI RCQLGFYGGT DLNAETENEA LSGVYYDQQT
     YMDRTLEMFE AIEAKYGHSF QMLHDVHERL HPNQAVQFAK KVEPFNVYFL EDILPPDQTE
     WLKLVRTQTA TPIAIGELFN NPMEWKALIA SHQLDYLRVH VSQIGGITPA LKLAHLCDAF
     GVRVAWHTPS DISPIGLAVN THLNMHLHNA AVQESLVLKD NTKQLFKHSP EPKQGHFYPI
     ERPGIGVDFD KELARDYPVV YRSHDWTQSR LPDGTLFTP
//
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