ID F4BS89_CARS1 Unreviewed; 399 AA.
AC F4BS89;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=L-Ala-D/L-Glu epimerase {ECO:0000313|EMBL:AEB30159.1};
DE EC=5.1.1.- {ECO:0000313|EMBL:AEB30159.1};
GN Name=ykfB {ECO:0000313|EMBL:AEB30159.1};
GN OrderedLocusNames=CAR_c15000 {ECO:0000313|EMBL:AEB30159.1};
OS Carnobacterium sp. (strain 17-4).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=208596 {ECO:0000313|EMBL:AEB30159.1, ECO:0000313|Proteomes:UP000008304};
RN [1] {ECO:0000313|EMBL:AEB30159.1, ECO:0000313|Proteomes:UP000008304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-4 {ECO:0000313|EMBL:AEB30159.1,
RC ECO:0000313|Proteomes:UP000008304};
RX PubMed=21551290; DOI=10.1128/JB.05113-11;
RA Voget S., Klippel B., Daniel R., Antranikian G.;
RT "Complete gnome sequence of Carnobacterium sp. 17-4.";
RL J. Bacteriol. 193:3403-3404(2011).
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; CP002563; AEB30159.1; -; Genomic_DNA.
DR RefSeq; WP_013711101.1; NC_015391.1.
DR AlphaFoldDB; F4BS89; -.
DR STRING; 208596.CAR_c15000; -.
DR KEGG; crn:CAR_c15000; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_9; -.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000008304; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 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 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 Isomerase {ECO:0000313|EMBL:AEB30159.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008304}.
FT DOMAIN 132..252
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 399 AA; 45134 MW; 062A60EB1CD01DA3 CRC64;
MKPTIITAIK SYTIKPDRHN LVVVKVETNR GVTGYGCATF QQRPLAVKGM VDEYLKPLLI
GKDANNIEDL FQMMTVNSYW RNGPVINNAI SGVDMALWDI KGKLCDMPLY QLLGGKSRDA
IASYTHAVAD NLEDLYGEID SILAEGYQYI RCQLGFYGGP ATELNTPKNT SEGSYFDQYQ
YMDTTLKMFA AIRNKYGNSF QMLHDVHERL YPNQAVQFAK KSEEFNLFFL EDLLPPDQNE
WLKQIRSQSS TPIATGELFN NPMEWQSLVK NREIDYMRAH VSQLGGITPA IKLAHFCDAM
GIRMAWHTPS DITPIGIAVN THLNIHLHNA AVQENIVVPE NTANLFSHVP VAEKGYFYPI
DKPGIGVDFN EELAEEYPIE YRPHEWTQSR TPDGTIVTP
//
