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Database: UniProt
Entry: I0AJ50_IGNAJ
LinkDB: I0AJ50_IGNAJ
Original site: I0AJ50_IGNAJ 
ID   I0AJ50_IGNAJ            Unreviewed;       375 AA.
AC   I0AJ50;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Dipeptide epimerase {ECO:0000256|RuleBase:RU366006};
DE            EC=5.1.1.- {ECO:0000256|RuleBase:RU366006};
GN   Name=murI {ECO:0000313|EMBL:AFH49007.1};
GN   OrderedLocusNames=IALB_1297 {ECO:0000313|EMBL:AFH49007.1};
OS   Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS   Mat9-16).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Ignavibacteriaceae; Ignavibacterium.
OX   NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49007.1, ECO:0000313|Proteomes:UP000007394};
RN   [1] {ECO:0000313|EMBL:AFH49007.1, ECO:0000313|Proteomes:UP000007394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC   {ECO:0000313|Proteomes:UP000007394};
RX   PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA   Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA   Bryant D.A.;
RT   "Complete genome of Ignavibacterium album, a metabolically versatile,
RT   flagellated, facultative anaerobe from the phylum Chlorobi.";
RL   Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH49007.1; -; Genomic_DNA.
DR   RefSeq; WP_014560162.1; NC_017464.1.
DR   AlphaFoldDB; I0AJ50; -.
DR   STRING; 945713.IALB_1297; -.
DR   GeneID; 78242975; -.
DR   KEGG; ial:IALB_1297; -.
DR   PATRIC; fig|945713.3.peg.1295; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_4_3_10; -.
DR   OMA; YHEEFPV; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000007394; 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; IPR034593; DgoD-like.
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   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF3; ENOLASE SUPERFAMILY MEMBER DDB_G0284701; 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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Isomerase {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:UP000007394};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..375
FT                   /note="Dipeptide epimerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003624780"
FT   DOMAIN          174..265
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        193
FT                   /note="Proton acceptor; specific for (R)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   ACT_SITE        291
FT                   /note="Proton acceptor; specific for (S)-substrate
FT                   epimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-1"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634603-3"
SQ   SEQUENCE   375 AA;  42274 MW;  F696416600920116 CRC64;
     MKQNRRDFLK TTSLLTAASI SGLSSKSFAT NFIQNKGTKM KFSFKPYTLE LKHVFTVAVN
     SRTTTPVMLT EIEYDGVKGY GEASMPPYLG ESQETATRFL SKVNLEQFDD PFEIEKILEY
     IDSIDEKNTA AKASVDIALH DLVGKLIGKP WYKIWGFDKT KTPYTTFTIG IDTPEVVRQK
     VKEADEFKIL KVKLGRENDR EMIETIRSVT DKPLTADANQ GWKDKNYALE MIQWLSEQNV
     LYIEQPMPKE MIEENAWITE RSPIPVLGDE SIQRIPDLIK MKDVYSGVVI KLMKCTGMRE
     AYKMITLARS LGMKVMLGCM TETSCAISAA AQLSPEVDWA DLDGNLLIKN DPFEGVKVIN
     GKITLNDYPG IGLIS
//
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