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
//