ID A0A1C6NLS6_9ACTN Unreviewed; 334 AA.
AC A0A1C6NLS6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Probable 5-dehydro-4-deoxyglucarate dehydratase {ECO:0000256|HAMAP-Rule:MF_00694};
DE EC=4.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00694};
DE AltName: Full=5-keto-4-deoxy-glucarate dehydratase {ECO:0000256|HAMAP-Rule:MF_00694};
DE Short=KDGDH {ECO:0000256|HAMAP-Rule:MF_00694};
GN ORFNames=YWIDRAFT_05872 {ECO:0000313|EMBL:SCK31974.1};
OS Streptomyces sp. SceaMP-e96.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1100824 {ECO:0000313|EMBL:SCK31974.1, ECO:0000313|Proteomes:UP000199486};
RN [1] {ECO:0000313|Proteomes:UP000199486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SceaMP-e96 {ECO:0000313|Proteomes:UP000199486};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydro-4-deoxy-D-glucarate + H(+) = 2,5-dioxopentanoate +
CC CO2 + H2O; Xref=Rhea:RHEA:24608, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:42819,
CC ChEBI:CHEBI:58136; EC=4.2.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001446, ECO:0000256|HAMAP-
CC Rule:MF_00694};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC dioxopentanoate from D-glucarate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004983, ECO:0000256|HAMAP-Rule:MF_00694}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|ARBA:ARBA00007592,
CC ECO:0000256|HAMAP-Rule:MF_00694, ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; FMHL01000022; SCK31974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6NLS6; -.
DR UniPathway; UPA00564; UER00628.
DR Proteomes; UP000199486; Unassembled WGS sequence.
DR GO; GO:0047448; F:5-dehydro-4-deoxyglucarate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00694; KDGDH; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR017655; Dehydro-deoxyglucarate_dehyd.
DR PANTHER; PTHR12128:SF19; 5-DEHYDRO-4-DEOXYGLUCARATE DEHYDRATASE 2-RELATED; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00694}.
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 184
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 72
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 334 AA; 34703 MW; 60EAA8BD166ACCE4 CRC64;
MTSAPPPATS PSLRPGDALR RHPRLADRLD GLLFFPVTAY GPDGALDPAA FGAHVRDGID
AGAAAVFACC GTGEFHALTP GEFADCVAAA VEEAAGRVPV IAGTGYGTAL AAQFAHLAHE
AGADGLLALP PYLVVAGQQG LLTHYTELAA ATPLPVIVYQ RDNAVFTPAT VAALARIPGI
IGLKDGLGDL DLLQRIISAV RTEAPEEDFL YFNGLPTAEL TGPAYRGLGV RLYSSAVFAF
APEIALAFHR ALDTGDDDTV RRLLDGFYRP LVELRNQGRG YAVSLVKAGV RMRGPDVGEV
RPPLSEPSPA HLKELAGLIE RGLALVTDTA GAGA
//
