ID A0A0D9YU55_9ORYZ Unreviewed; 1696 AA.
AC A0A0D9YU55;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein {ECO:0000259|SMART:SM00922};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G22230.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G22230.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G22230.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR STRING; 40148.A0A0D9YU55; -.
DR EnsemblPlants; OGLUM02G22230.1; OGLUM02G22230.1; OGLUM02G22230.
DR Gramene; OGLUM02G22230.1; OGLUM02G22230.1; OGLUM02G22230.
DR eggNOG; KOG1223; Eukaryota.
DR eggNOG; KOG2382; Eukaryota.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:InterPro.
DR GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042550; P:photosystem I stabilization; IEA:EnsemblPlants.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:EnsemblPlants.
DR CDD; cd07037; TPP_PYR_MenD; 1.
DR CDD; cd02009; TPP_SHCHC_synthase; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR HAMAP; MF_01659; MenD; 1.
DR HAMAP; MF_01660; MenH; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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; IPR004433; MenaQ_synth_MenD.
DR InterPro; IPR032264; MenD_middle.
DR InterPro; IPR022485; SHCHC_synthase_MenH.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00173; menD; 1.
DR PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF16582; TPP_enzyme_M_2; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1155..1240
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT REGION 16..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1696 AA; 187528 MW; AE9B1C9651659E10 CRC64;
MLAVVSSSGH RLLPLPVLPG TFTTPPPPPP PPLLSPRRPL LAPRRRRCLC GGGGGGLLLL
RAVAARRAGI VIDVDEVGEV GDRDLPVDVS FTRRLPPVLT LGDGLAALRR AGEEVKACPP
AAAASGVIRF EVLVPPSTKA LKWLCTQFKR SSLFPQFYLS RKQTTDSSIQ LEISGAGSAI
CFHGSSRLDN GFDLISRYLS FNSHLIRAYG SVGVKYDKEL LSLEERIGSF YFFIPQVELS
EFDGYSMLSS TIVWDDSVSH TFEDSVCLFE SCFSQIWSSY DSSATICYEN MVTSYIGESR
MSESRNTQLV YLDAEFLAVI DGKAVTEKEN CPTSDQSFVR FSPQFLFCAN MDLCLQSNKI
ESFIRRCSNI NLAWASFIVE EFVRLGFTYF CIAPGSRSSP LALSASVHPL TTCISCYDER
SLGFHALGYG RGSRKPAIVI TSSGTAVSNL LPSVVEASQD FVPLILLTAD RPPELQDVGA
NQAINQVNHF GSFVRHFFSL PPPDDHIYAR TVLTTVDSAA YYAMQAPQGP VHINCAFREP
LDYGYQDWSV DCLKGLDKWF INREPYTRYL GMKIVSALVM EVLEIVKNAN QGLLLVGAIH
TEDDIWAVTL LARHLSWPIA ADVLSGLRMR KVQKSIPGLD KSICFIDHID QILLSESVKI
WKTPDVIVQI GSRITSKRVG TYLESCSPSS YILIDAHPCR HDPSHVVTHR IQATITEFAA
SLCQCNFQTK TSSWSDILMV LNSAVSQEIM FQVHSECSLT EPYVAHVIGE ALYGNATMFI
GNSMVIRDLD MFGKGWIDHS TNANNAMMHH FPGFLGAPVA GNRGASGIDG LLSTSIGFAI
GSNKHVFCVI GDISFLHDTN GLSLLNQRTQ RKPMTVIVIN NHGGAIFSLL PVAKTASLQI
LEKIFYTLHD ISISKLCAAH RIKHILVQTK AELHDALVKS HEGHVDCVVE VENRIVDNAN
FHRIISMFTD HTATMHLAYL LGGPYCKDGV NGFSVGRIHA AEYMFYRIQL AAPRTSGISE
SSFFHEGFIL KLCVGDSIVG FGEVAPIEIH EEDLLDVEEQ LRFLFHRMKD AELDVVPLLR
GSFSNWIWTT LGIPPSSVFP SVKCGLEMAI LNLLESQRID RSYGIFTGSN AVEYNQSSTA
SIQICALVDS CGTPMDVTLA VVKLVAEGFT TVKLKVGRRE NPAEDAAVIQ KVREIVGYKI
NIRADANRKW TYEQAIDFGS REPVDSVNDI IKFCENSGLP VALDETIDNL TGDVIPKLHQ
FSHPGIVALV IKPSVVGGFE TAAYIAKWAH MHDKMAVISS TYESSVGLAT YIQFAHYVDR
QNDITSRIKN KGSCGNVAHG LGTYQWLRED VSDQKLKIHA PPLGDGIRAS AEDAHGYLQH
LVINDKKIER TYSEEKLRSY FIQVDGDNFS YQVKLQEGGD CTHEKVILFL HGFLGTSEDW
VPMMKALSPS ARVIAVDLPG HGESEILQHD VENSNQISFS VQSVADLLLK LIRNITDGAV
VVVGYSMGAR IALHMALNQN HKISGAVIIS GSPGLRDEAS KRRRSAIDRS RAHFLSSCGL
ENFLETWYSA KMWASLREHP KFDSLVRTRM KHNNIKALSK VLADSSTGTQ KSLWEDLKHL
KSPLLIVAGE KDPKFKEISQ QMCREIRKHK DRESDGLCEM IIIPDSGHAV HVENPLPLVR
AIRKFLVRDI PDVISK
//