ID A0A1H8YPA4_9PSEU Unreviewed; 418 AA.
AC A0A1H8YPA4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=SAMN04489732_12546 {ECO:0000313|EMBL:SEP53208.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP53208.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEP53208.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP53208.1,
RC ECO:0000313|Proteomes:UP000198582};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC dioxopentanoate from D-glucarate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005183}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GlucD subfamily. {ECO:0000256|ARBA:ARBA00009938}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOEF01000025; SEP53208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8YPA4; -.
DR STRING; 394193.SAMN04489732_12546; -.
DR OrthoDB; 193563at2; -.
DR Proteomes; UP000198582; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03323; D-glucarate_dehydratase; 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; IPR034593; DgoD-like.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR034598; GlucD-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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198582}.
FT DOMAIN 167..261
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
SQ SEQUENCE 418 AA; 45099 MW; DAD3347591DAD6DC CRC64;
MKIQDVVLTP VAFADPPLLN VMGVHEPFAL RSVVQVRCED GVVGLGESYG DSAFLGEVRK
VVPELAGHDV FDLPGLKRIV TRVLAGTVLT DEHGLIGGFS IRKTIASVYA LFEVACLDAQ
GHCLGRPVAD LLGGKARDAV DFSAYLFYKY GAHIGAKEDS WGEVVTPEQL VGAAKRMVDE
YGFRSIKLKG GVFEPAQEVD GIRALAEAFP GHPLRIDPNA AWTPQTSIRV AEELDGVLEY
LEDPTPGIEG MAKVAERASM PLATNMCVVN FGDIEPAFRA RAIGVLLSDH HFWGGMRDTQ
ALSVTCESFG VGLSMHSNSH LGISLAAMVH VAAATPHLTY ACDTHWPWKT ADVIAPGALE
FADGAVAVPD KPGLGIEIDP DALARAHEDY VRCGLTKRDD VTYMRRWTPG FEPNTARW
//
