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Database: UniProt
Entry: R9GM51_9SPHI
LinkDB: R9GM51_9SPHI
Original site: R9GM51_9SPHI 
ID   R9GM51_9SPHI            Unreviewed;       354 AA.
AC   R9GM51;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   ORFNames=ADIARSV_4085 {ECO:0000313|EMBL:EOR92803.1};
OS   Arcticibacter svalbardensis MN12-7.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR92803.1, ECO:0000313|Proteomes:UP000014174};
RN   [1] {ECO:0000313|EMBL:EOR92803.1, ECO:0000313|Proteomes:UP000014174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN12-7 {ECO:0000313|EMBL:EOR92803.1,
RC   ECO:0000313|Proteomes:UP000014174};
RX   PubMed=23846277;
RA   Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA   Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT   Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT   Sample.";
RL   Genome Announc. 1:E00484-13(2013).
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}.
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:EOR92803.1}.
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DR   EMBL; AQPN01000143; EOR92803.1; -; Genomic_DNA.
DR   RefSeq; WP_016197304.1; NZ_AQPN01000143.1.
DR   AlphaFoldDB; R9GM51; -.
DR   STRING; 1150600.ADIARSV_4085; -.
DR   PATRIC; fig|1150600.3.peg.4044; -.
DR   eggNOG; COG4948; Bacteria.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000014174; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014174}.
FT   DOMAIN          141..241
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        162
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         190
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   354 AA;  39299 MW;  DB4B9C9D7B085E60 CRC64;
     MNIKSIKAYS KNLAVKRPYT IARNTVSDAE IVFFEVELMN GMVGIGSANT DVEVVNETAS
     QTLDNLQSDL VAELVGKDIR LFLSLIARYR RDFFAFPGTL AALDIALHDA FGKYLGVSIL
     DFYGRYHQKM VTSVTIGIKG VAETLEEAKE YYDSGFRALK VKTGLNVLED AERIIMLREK
     YGDYFHIRVD ANTGYNPAQL QKFIDLTVEQ GVELIEQPFL PGKENDLLDF PAEVRNRLAA
     DESLKNAHSA LTLLQHRPYG IYNIKLMKCG GLVGAFEIAN IARPADIDLF WGCNDESMIS
     ITAALHAAFS CPNTRYIDLD GSLDLAEDVV IDGFTLQDGF MFPNDKPGLG LTLL
//
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