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Database: UniProt
Entry: S9RXD1_9RHOB
LinkDB: S9RXD1_9RHOB
Original site: S9RXD1_9RHOB 
ID   S9RXD1_9RHOB            Unreviewed;       299 AA.
AC   S9RXD1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Dihydrodipicolinate synthase/N-acetylneuraminate lyase {ECO:0000313|EMBL:EPX78629.1};
GN   ORFNames=Salmuc_04210 {ECO:0000313|EMBL:EPX78629.1};
OS   Salipiger mucosus DSM 16094.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX78629.1, ECO:0000313|Proteomes:UP000015347};
RN   [1] {ECO:0000313|Proteomes:UP000015347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX   PubMed=25197501; DOI=10.4056/sigs.4909790;
RA   Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT   strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT   clade.";
RL   Stand. Genomic Sci. 9:1331-1343(2014).
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {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:EPX78629.1}.
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DR   EMBL; APVH01000038; EPX78629.1; -; Genomic_DNA.
DR   RefSeq; WP_021120565.1; NZ_KE557279.1.
DR   AlphaFoldDB; S9RXD1; -.
DR   STRING; 1123237.Salmuc_04210; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_5_2_5; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000015347; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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: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|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015347}.
FT   ACT_SITE        140
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        164
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         52
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   299 AA;  31056 MW;  E73677C8C364D283 CRC64;
     MALDLDTALT GISGILVTPY DEAGEIAPAK LAPILDRALG AGMHMPVVNS NTGEFYALTT
     DEACTMVREV AGLVDGRAPL LAGVGRGIRD ACTLARASAE AGATALMIHQ PPDPFVSPRG
     TVDYVEAVSE AGGGLPIMLY LRNDAIGTAG IKALCDIPGV KGVKWATPNP LKLAAAIEAC
     DPSIVWVAGL AEVWAPPLYA VGARGFTSGL INVWPERSMA IHGALAKGDF ARANALIAEM
     RPFEEIRAEE LNGTNVTGVK AALHALGQDC GPTRPPSAWP LTEAQQGTLR RFLSDNGLA
//
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