ID A0A1S2VQA5_9BACT Unreviewed; 357 AA.
AC A0A1S2VQA5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN ORFNames=BLX24_02330 {ECO:0000313|EMBL:OIN60942.1};
OS Arsenicibacter rosenii.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arsenicibacter.
OX NCBI_TaxID=1750698 {ECO:0000313|EMBL:OIN60942.1, ECO:0000313|Proteomes:UP000181790};
RN [1] {ECO:0000313|EMBL:OIN60942.1, ECO:0000313|Proteomes:UP000181790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:OIN60942.1,
RC ECO:0000313|Proteomes:UP000181790};
RA Huang K.;
RT "Arsenicibacter rosenii gen. nov., sp. nov., an efficient arsenic-
RT methylating bacterium isolated from an arsenic-contaminated paddy soil.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OIN60942.1}.
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DR EMBL; MORL01000001; OIN60942.1; -; Genomic_DNA.
DR RefSeq; WP_071501446.1; NZ_MORL01000001.1.
DR AlphaFoldDB; A0A1S2VQA5; -.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000181790; 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:UP000181790}.
FT DOMAIN 141..235
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 266
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 357 AA; 39518 MW; 424F8C071A66D24D CRC64;
MRIRDIRVYT RNLALAKPYT IAYQHITTVD NVFVEVELEN GITGRGAANP DPDVVSETLA
DVVQNLSGEV VQGFAGADIR MFNTLLNRIE QTFVHCPGTL AALDIALHDA FCQYLEMPVV
RFYGQHIKAL PTSVTIGIMD VAATLEEARA YQQQGFRVLK VKTGRDVDLD SERVIRLHET
VGHNVTIRVD ANQGYNARQL RQFLHTTRHV DIELIEQPFP VGQENELLNF DPDIRLRIAA
DESLTDGKTA IRLAQEPALF GIFNIKLMKC GGIRAGLALG QLARHAGLRL FWGCNDESRV
SITAALHAAF ACPNTTYLDL DGSLDLAEDL VTGGFVMENG LMYPVMRPGL GLQPIHE
//
