ID   A0A4P6Q6F7_9ACTN        Unreviewed;       311 AA.
AC   A0A4P6Q6F7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=L-2-keto-3-deoxyarabonate dehydratase {ECO:0000313|EMBL:QBI54971.1};
DE            EC=4.2.1.43 {ECO:0000313|EMBL:QBI54971.1};
GN   Name=araD {ECO:0000313|EMBL:QBI54971.1};
GN   ORFNames=EKD16_15995 {ECO:0000313|EMBL:QBI54971.1};
OS   Streptomonospora litoralis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=2498135 {ECO:0000313|EMBL:QBI54971.1, ECO:0000313|Proteomes:UP000292235};
RN   [1] {ECO:0000313|EMBL:QBI54971.1, ECO:0000313|Proteomes:UP000292235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2 {ECO:0000313|EMBL:QBI54971.1,
RC   ECO:0000313|Proteomes:UP000292235};
RA   Khodamoradi S., Hahnke R.L., Kaempfer P., Schumann P., Rohde M.,
RA   Steinert M., Luzhetskyy A., Wink J., Ruckert C.;
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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; CP036455; QBI54971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P6Q6F7; -.
DR   KEGG; strr:EKD16_15995; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000292235; Chromosome.
DR   GO; GO:0047449; F:2-dehydro-3-deoxy-L-arabinonate dehydratase activity; IEA:UniProtKB-EC.
DR   CDD; cd00408; DHDPS-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR12128:SF73; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; 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|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000292235}.
FT   BINDING         214
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   311 AA;  33427 MW;  A9F389B78A9949D9 CRC64;
     MPITASERGV FAIAPTPFHD DGALDRTSLD RLTDFYLQSG VSGITVLGQL GEAPKLEHAE
     AVDVASRVVA RAGVPVVVGV SAPGFAAMRA LAGEVMDAGA AGVMIAPPNS LRTDDQIIAY
     YRNAAQAIGP DIPFVIQDYP LTFSVVMAPK VIRAITEENP NCVMLKHEDW PGLEKISALR
     GFEAEGSMRR LSILCGNGGL FLDFEPERGA DGAMTGYCFP DMLVELVQLA ARGEREAAHD
     LFDAHLPLLR YEQQPGAGLA VRKYVFMRRG ILASEAQRRP SAPLSPTARE EVDFLLARLA
     GKDKRAELPT G
//