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Database: UniProt
Entry: A0A0Q7J7H9_9BACL
LinkDB: A0A0Q7J7H9_9BACL
Original site: A0A0Q7J7H9_9BACL 
ID   A0A0Q7J7H9_9BACL        Unreviewed;       365 AA.
AC   A0A0Q7J7H9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Mandelate racemase {ECO:0000313|EMBL:KQX47172.1};
GN   ORFNames=ASD40_16565 {ECO:0000313|EMBL:KQX47172.1};
OS   Paenibacillus sp. Root444D2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736538 {ECO:0000313|EMBL:KQX47172.1, ECO:0000313|Proteomes:UP000051657};
RN   [1] {ECO:0000313|EMBL:KQX47172.1, ECO:0000313|Proteomes:UP000051657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root444D2 {ECO:0000313|EMBL:KQX47172.1,
RC   ECO:0000313|Proteomes:UP000051657};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX47172.1, ECO:0000313|Proteomes:UP000051657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root444D2 {ECO:0000313|EMBL:KQX47172.1,
RC   ECO:0000313|Proteomes:UP000051657};
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:KQX47172.1}.
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DR   EMBL; LMEO01000050; KQX47172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7J7H9; -.
DR   STRING; 1736538.ASD40_16565; -.
DR   Proteomes; UP000051657; Unassembled WGS sequence.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
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; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
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.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051657}.
FT   DOMAIN          148..245
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   365 AA;  41168 MW;  ED27E27AEF5F227D CRC64;
     MKITKVESFV LHVPITPPIT DAINIATHWG LAGVRIFTDE GFIGYGYTGT CAHGDDMIVD
     TIDKYYAPLL VGKDPFMVRE LWNDMRFGKM HWIGRSGVTH MALAAVDIAI WDIMAKSVDK
     PLWQFLGGAK SQPIKAYNTN GGWLNWSKER LVKDCADIVE SGFTGVKIKV GKPDSREDYD
     RCKAVRKAIG DDVIFMVDVN QQWNINTAMT WGKKLEEFDL FWLEEPLNPD DILGHKKLAD
     ALNVPIALGE HVYNKYAFRD YIHQGAIEYC QVDVTRVGGI TEWLQVAGLA ASYDVPICPH
     VGDMGQIHLH LVASTPGAIM LEYIPWIRHI FEEPATVKDG HYVLPQMPGA STTILPRYFE
     EYRIR
//
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