ID A0A286DI50_9ACTN Unreviewed; 312 AA.
AC A0A286DI50;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN06297387_10191 {ECO:0000313|EMBL:SOD58321.1};
OS Streptomyces zhaozhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1300267 {ECO:0000313|EMBL:SOD58321.1, ECO:0000313|Proteomes:UP000219072};
RN [1] {ECO:0000313|EMBL:SOD58321.1, ECO:0000313|Proteomes:UP000219072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7095 {ECO:0000313|EMBL:SOD58321.1,
RC ECO:0000313|Proteomes:UP000219072};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OCNE01000001; SOD58321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286DI50; -.
DR OrthoDB; 8995637at2; -.
DR UniPathway; UPA00564; UER00628.
DR Proteomes; UP000219072; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000219072}.
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 165
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 53
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 312 AA; 32922 MW; AE0603AE7A056435 CRC64;
MTDARLGERL DGLLFFPVTA YGPDGSLHLD AYRAHVRAGV DAGAGAVFAC CGTGEFHALT
PDEFERCVAA AVEETAGAVP VVAGAGYGTA LAGEFARRAE RAGADGLLAM PPYLVVADQR
GLLRHFTELA AATSLDVIVY QRDNVVLAPD TVAALAATPG IVGLKDGLGD LDLLQRTISA
VRAAHPDRPF RYFNGLPTAE LTGLAYRGLG VTLYSSAVFA FLPEVALAFH AALHAEGPEH
EETLRRLLDG FYRPLVELRN EGRGYAVSLV KAGVRMRGLD VGEVRAPLSE PLPAHLDRLA
ALIDTGLGLV RS
//
