ID   A0A0C2JFQ6_9ACTN        Unreviewed;       310 AA.
AC   A0A0C2JFQ6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   18-JUN-2025, entry version 48.
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=LP52_17700 {ECO:0000313|EMBL:KIH97665.1};
OS   Streptomonospora alba.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsidaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH97665.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
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}.
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:KIH97665.1}.
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DR   EMBL; JROO01000033; KIH97665.1; -; Genomic_DNA.
DR   RefSeq; WP_040275117.1; NZ_JROO01000033.1.
DR   AlphaFoldDB; A0A0C2JFQ6; -.
DR   STRING; 183763.LP52_17700; -.
DR   OrthoDB; 8995637at2; -.
DR   UniPathway; UPA00564; UER00628.
DR   Proteomes; UP000031675; Unassembled WGS sequence.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:TreeGrafter.
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-UniRule.
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   NCBIfam; NF002958; PRK03620.1; 1.
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   PRINTS; PR00146; DHPICSNTHASE.
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:UP000031675}.
FT   ACT_SITE        142
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        167
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         55
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   310 AA;  32536 MW;  DD4FE4A2CD6D1664 CRC64;
     MPLSPAELGE SFTGLLGFPV TPFTDAGELD LPRFKEHLDD MLEAGPGALF VACGTGEFAS
     LTLEEHRTAV RTAVEHVGGA VPVLAGVGGG ARVAKEYLRS AEGEGADGAL VLPPYLQVGP
     QRGLLSHYRD LLDSTGLGLI PYQRSTAVFT PETVAELAGN DRVVALKDGH GDIELLQRIR
     TVTENRLPLL NGMPTAETFA RAYRAVGAAA YSSAVLAFAP AVATAFFAAS ERGDEAVQDE
     LLREFYVPLA ELRNTTPGYA VSLVKAGLEI RGRSAGPVRP PLAEPSPEHK AELADIIDRG
     LAVASAEVAA
//