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
//