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Database: UniProt
Entry: A0A0Q9RU98_9BACL
LinkDB: A0A0Q9RU98_9BACL
Original site: A0A0Q9RU98_9BACL 
ID   A0A0Q9RU98_9BACL        Unreviewed;       372 AA.
AC   A0A0Q9RU98;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Isomerase {ECO:0000313|EMBL:KRF13541.1};
GN   ORFNames=ASG93_13525 {ECO:0000313|EMBL:KRF13541.1};
OS   Paenibacillus sp. Soil787.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF13541.1, ECO:0000313|Proteomes:UP000051948};
RN   [1] {ECO:0000313|EMBL:KRF13541.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF13541.1,
RC   ECO:0000313|Proteomes:UP000051948};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF13541.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF13541.1,
RC   ECO:0000313|Proteomes:UP000051948};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRF13541.1}.
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DR   EMBL; LMSP01000044; KRF13541.1; -; Genomic_DNA.
DR   RefSeq; WP_056837376.1; NZ_LMSP01000044.1.
DR   AlphaFoldDB; A0A0Q9RU98; -.
DR   STRING; 1736411.ASG93_13525; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000051948; Unassembled WGS sequence.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProt.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03316; MR_like; 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; 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; IPR046945; RHMD-like.
DR   PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR   PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDG00179; mandelate_racemase; 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   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:KRF13541.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          137..235
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   372 AA;  42071 MW;  35661F1F960CB267 CRC64;
     MLIRKIDTFP LLYHLPKPYG DANGLKAYRT CYLIRITTDL GVEGWGECVD WLPTLHKGFQ
     ERIIPYLIGK SVADRTILVR TLNKWHSRSA TAVSMALTEI MAKTCHISVC DLWGGKVREK
     VPVYASFQSY SEEANWQKHS LSAIEQAINQ GFDKIKVKIG GKSIPEDQQH IKMVQALLQE
     KIGLALDANQ SYDVTAALRW QSMLDTWPNL LWFEEPLEIS RIAEYVLLRN RLSVPLAGGE
     NLEKAADFVP IFLQYALDFI TPDTLHLTGI DGYRETLSLA RSFGTRVTPH SYDGALSRLY
     AIFAHACLEP WGKMEEDSIE PLEWDVMDNP FTKLFGFQPL NSEISIPSGT GIGLEIDSEM
     LAFYQWDGNS YG
//
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