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Database: UniProt
Entry: F2R487_STRVP
LinkDB: F2R487_STRVP
Original site: F2R487_STRVP 
ID   F2R487_STRVP            Unreviewed;       422 AA.
AC   F2R487;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE            EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN   OrderedLocusNames=SVEN_0076 {ECO:0000313|EMBL:CCA53364.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53364.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA53364.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA53364.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O;
CC         Xref=Rhea:RHEA:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:30612,
CC         ChEBI:CHEBI:42819; EC=4.2.1.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00001426};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC       dioxopentanoate from D-glucarate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005183}.
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DR   EMBL; FR845719; CCA53364.1; -; Genomic_DNA.
DR   RefSeq; WP_015031284.1; NZ_JABVZO010000044.1.
DR   AlphaFoldDB; F2R487; -.
DR   STRING; 953739.SVEN_0076; -.
DR   GeneID; 69862305; -.
DR   KEGG; sve:SVEN_0076; -.
DR   PATRIC; fig|953739.5.peg.3512; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_9_0_11; -.
DR   OMA; WGRFVRT; -.
DR   OrthoDB; 193563at2; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0008872; F:glucarate dehydratase activity; IEA:UniProtKB-EC.
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; 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   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF4; GLUCARATE DEHYDRATASE; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDG00055; glucarate_dehydratase; 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   Lyase {ECO:0000313|EMBL:CCA53364.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   DOMAIN          167..261
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   422 AA;  45169 MW;  98FBE2BCA9979EF9 CRC64;
     MKITSVVVTP VAFADPPLLN AVGVHEPYAL RSVVEVRTDT GAYGLGESYG DAPHLELLRL
     VADELPGLDP FDLNELSRRV GATVGGRVAR DAHGLIGDGG AAKTVASVTS PFEVACHDLQ
     GKHLGRPVSD LLGGATRDRI DFCGYLFAKW AAHPGHRPDA WGPALDAAGL VAQARLLADR
     FGFRSFKLKG GVLPPDEEIA AIRALREAFP GHPLRLDPNA SWDPATAARV ADELTGVLEY
     LEDPVAGIPA MADLARLAPM PLATNMCVVT WEHLPRAVPS RAVGVLLGDH HFWGGLKASQ
     HLATCCHQFG IGMSMHSNSH LGISLAAMVH LAAATPAIGH DLDTHWPWKR PEDDVVKQPW
     TFTDGAITVP RTPGLGVELD RDALARLHEQ YLGCGLTRRD DSGYLARVAP GVRLREDVHE
     PA
//
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