ID A0A1B0VLI5_FERIS Unreviewed; 342 AA.
AC A0A1B0VLI5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN ORFNames=NA23_10040 {ECO:0000313|EMBL:AMW33531.1};
OS Fervidobacterium islandicum.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=2423 {ECO:0000313|EMBL:AMW33531.1, ECO:0000313|Proteomes:UP000093740};
RN [1] {ECO:0000313|EMBL:AMW33531.1, ECO:0000313|Proteomes:UP000093740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW-1 {ECO:0000313|EMBL:AMW33531.1,
RC ECO:0000313|Proteomes:UP000093740};
RX PubMed=26421103; DOI=10.1186/s40793-015-0063-4;
RA Lee Y.J., Jeong H., Park G.S., Kwak Y., Lee S.J., Lee S.J., Park M.K.,
RA Kim J.Y., Kang H.K., Shin J.H., Lee D.W.;
RT "Genome sequence of a native-feather degrading extremely thermophilic
RT Eubacterium, Fervidobacterium islandicum AW-1.";
RL Stand. Genomic Sci. 10:71-71(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR634603-3,
CC ECO:0000256|RuleBase:RU366006};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR634603-3,
CC ECO:0000256|RuleBase:RU366006};
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000256|ARBA:ARBA00008031,
CC ECO:0000256|RuleBase:RU366006}.
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DR EMBL; CP014334; AMW33531.1; -; Genomic_DNA.
DR RefSeq; WP_033191633.1; NZ_CP014334.2.
DR AlphaFoldDB; A0A1B0VLI5; -.
DR STRING; 2423.NA23_10040; -.
DR KEGG; fia:NA23_10040; -.
DR eggNOG; COG4948; Bacteria.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000093740; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:UniProtKB-UniRule.
DR CDD; cd03319; L-Ala-DL-Glu_epimerase; 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; IPR034603; Dipeptide_epimerase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR NCBIfam; NF041118; A_G_epim_Thtga; 1.
DR PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDS00001; Enolase; 1.
DR SFLD; SFLDG00180; muconate_cycloisomerase; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU366006};
KW Magnesium {ECO:0000256|PIRSR:PIRSR634603-3, ECO:0000256|RuleBase:RU366006};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634603-3,
KW ECO:0000256|RuleBase:RU366006}.
FT DOMAIN 140..237
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 161
FT /note="Proton acceptor; specific for (R)-substrate
FT epimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT ACT_SITE 265
FT /note="Proton acceptor; specific for (S)-substrate
FT epimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ SEQUENCE 342 AA; 38278 MW; 66CF2D293F8162EB CRC64;
MGKIKSVKFK LNRFEYVKPF HITNNISYDT ENIEVAVELD NGVVGYGEAS PSFRVNGEKV
AALMGLESVV NDMIVGMDVR QYRQIFDVTD KLFSTPSIKA AVQYAVLDAF SEETGVPVYQ
ILGGAKTKIE TDYTISIGSI EERVEEAKQI VERGHNVIKV KVGENLEEDI QAMMAIYEVS
KGCKYIVDAN TGYTPKQAVK FVTELYRAGI DIHVFEQPVA MHDIEGLKYV RWNSPFPVAA
DESARTKYDV MRLIREEAVD YVNIKLMKSG ISDALAIVEM VKAANLRLMI GCMAESSLGV
NQSVHFALGT GAFDFHDLDS PLMLKEPEFR GKYKVDVPYY FV
//
