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Database: UniProt
Entry: A0A0M9EFR4_9RHOB
LinkDB: A0A0M9EFR4_9RHOB
Original site: A0A0M9EFR4_9RHOB 
ID   A0A0M9EFR4_9RHOB        Unreviewed;       319 AA.
AC   A0A0M9EFR4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:KPA20760.1};
DE            EC=4.3.3.7 {ECO:0000313|EMBL:KPA20760.1};
GN   Name=dapA_1 {ECO:0000313|EMBL:KPA20760.1};
GN   ORFNames=shim_30070 {ECO:0000313|EMBL:KPA20760.1};
OS   Shimia sp. SK013.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA20760.1, ECO:0000313|Proteomes:UP000037951};
RN   [1] {ECO:0000313|EMBL:KPA20760.1, ECO:0000313|Proteomes:UP000037951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK013 {ECO:0000313|EMBL:KPA20760.1,
RC   ECO:0000313|Proteomes:UP000037951};
RA   Voget S., Kanukollu S., Daniel R., Engelen B.;
RT   "Genome Sequence of Shimia sp. SK013.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPA20760.1}.
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DR   EMBL; LAJH01000016; KPA20760.1; -; Genomic_DNA.
DR   RefSeq; WP_054003450.1; NZ_LAJH01000016.1.
DR   AlphaFoldDB; A0A0M9EFR4; -.
DR   STRING; 1389006.shim_30070; -.
DR   PATRIC; fig|1389006.3.peg.3096; -.
DR   OrthoDB; 6142028at2; -.
DR   Proteomes; UP000037951; Unassembled WGS sequence.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase 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:SF74; BLL4423 PROTEIN; 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|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037951}.
FT   ACT_SITE        136
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         209
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   319 AA;  34203 MW;  96A0E0D5CAB2893D CRC64;
     MSKNVFTGTM PALMTPCKAD RTPDYDALVR KGHEMIAAGM SAVVYCGSMG DWPLLTDAER
     MTGVKRLVDA GVPVVVGTGA INSKSAVAHA AHAQKVGAVG LMVIPRVLSR GASAAAQENH
     FKAILTAAPD VPAIIYNSPV YGFATKADLF FALRAAHPNL IGFKEFGGKD DLRYAAEHIT
     SRDDQVTLMV GVDTEVYHGF VNCGATGSIT GIGTALPKEA LLLAALSQKA ADGNAEARVR
     ALELEEAFGV LASFDEGTDL VLYYKHLLVL NGEEEYRLHF VETDALSDAQ RRYCEAHYTQ
     FRAWFADWSA QGGIIAQCM
//
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