ID A0A3N6GIM8_9ACTN Unreviewed; 379 AA.
AC A0A3N6GIM8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=L-Ala-D/L-Glu epimerase {ECO:0000313|EMBL:RPK85233.1};
DE EC=5.1.1.- {ECO:0000313|EMBL:RPK85233.1};
GN ORFNames=EES45_02755 {ECO:0000313|EMBL:RPK85233.1};
OS Streptomyces sp. ADI97-07.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK85233.1, ECO:0000313|Proteomes:UP000281409};
RN [1] {ECO:0000313|EMBL:RPK85233.1, ECO:0000313|Proteomes:UP000281409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK85233.1,
RC ECO:0000313|Proteomes:UP000281409};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000256|ARBA:ARBA00008031}.
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:RPK85233.1}.
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DR EMBL; RPGY01000007; RPK85233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6GIM8; -.
DR Proteomes; UP000281409; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 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; 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.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RPK85233.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000281409}.
FT DOMAIN 138..234
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT REGION 336..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 38976 MW; 8B3361BC46738A2F CRC64;
MKVTQHTVRL VLTEPLRISR STLAARDAVR LTVTHEGLSG HGEAVTSVFY GLDTPALQRL
LTEAAECLAR FPGPETALHA LRVGELTAPD TPAAVTAAVE AALLDLVGKR TATAVHRFLG
SAVAPRVATA RTISLTSPGR AAAHARRLAG AGFSVIKIKA GDRDEEADLD RVRAVHAAAP
EARLLLDPNG AWTAGQARAL LPRFAELGVE AVEQPLAPGD PEALARLAAR SPLPVIADED
AVTYEDACRL AGRVQGINVK LAKCGGVHAA LRIAALIEGS GTDLMLGCLT ASTLGIAPAV
HIADRARWTD LDGHLLLAHD PWSGIGGGDG FVSASAQPGL GVRPRTAASG PGTAGAGPRA
AEDAEQTGPR DTGAWDVAS
//
