ID A0A0M8X001_9ACTN Unreviewed; 425 AA.
AC A0A0M8X001;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=glucarate dehydratase {ECO:0000256|ARBA:ARBA00011973};
DE EC=4.2.1.40 {ECO:0000256|ARBA:ARBA00011973};
GN ORFNames=ADL04_22595 {ECO:0000313|EMBL:KOV94707.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV94707.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOV94707.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV94707.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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 -!- 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:KOV94707.1}.
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DR EMBL; LGDZ01000194; KOV94707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8X001; -.
DR PATRIC; fig|1519493.3.peg.4807; -.
DR Proteomes; UP000037702; 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:UP000037702}.
FT DOMAIN 172..266
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634598-1"
SQ SEQUENCE 425 AA; 45882 MW; D0E752A21AAB08AA CRC64;
MTIAEVRLTP ILVADPPLLN TQGVHQPYTP RLIVEVVTAG GVTGLGETYG DTKYLELARP
LADRLIGHSV MDVNGLFRID LGVDESRVQG EVDAGGLRGV QSADKLRLSV LSAFEVACLD
AQGKALGLPV HALLGGKVRD AVEYSAYLFY KWDRHPAGVP AEPDPWGAAL DPAGVVRQAR
RLQELHGFGS FKLKGGVFPP DEEIAAVRAL AEAFPGHPLR LDPNGAWSVE TSLKVAEELG
DVLEYLEDPT LGTPAMAQVA AGTEVPLATN MCVTTFGEIR EAFTKDAVQV VLSDHHYWGG
LRNTQRLAAI CAAFGVGVSM HSNTHLGISL AAMTQVAATV PDLHHACDSH YPWQSEDVLT
ERLVFEGGRV AVSDAPGLGV ELDRGELDRL HRRWTEDDGS LRDRDDAAAL RRAEPGRRTP
VMPRW
//
