ID F0SIV5_RUBBR Unreviewed; 313 AA.
AC F0SIV5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:ADY61804.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:ADY61804.1};
GN OrderedLocusNames=Plabr_4231 {ECO:0000313|EMBL:ADY61804.1};
OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS 15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Rubinisphaera.
OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY61804.1, ECO:0000313|Proteomes:UP000006860};
RN [1] {ECO:0000313|Proteomes:UP000006860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC {ECO:0000313|Proteomes:UP000006860};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Planctomyces brasiliensis DSM 5305.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP002546; ADY61804.1; -; Genomic_DNA.
DR RefSeq; WP_013630509.1; NC_015174.1.
DR AlphaFoldDB; F0SIV5; -.
DR STRING; 756272.Plabr_4231; -.
DR KEGG; pbs:Plabr_4231; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_0; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000006860; Chromosome.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; 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; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 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:UP000006860}.
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 177
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 61
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 221
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 313 AA; 34055 MW; B1A0C521F7A77CE5 CRC64;
MAQTDNVIDS ARSSLLKLSG IVPPLLTPIS ARDTLDKDGL QRLLEHVIQG GVSGVFILGT
TGEAPSLSYR LRREMISETI RLVNGRVPVL VGVTDTAFVE SVELAKHAAD CGADAAVLTT
PYYFPAGQTE LTAYVQNIAP LIPLPLMLYN MPGLTKIWYE IETLRTLTAI DSIIGVKDSS
GDLDYFAQVC QLKQERPDWS ILIGPEAKLV EAHAAGGDGG VCGGANVAPH FFVDCYRGLV
ENDEARVNCN QQQIDRFQDI YEIGKYASRH IKATKSAASL LGLCSDLPAD PFHPFYEPER
ERVAVILKEL GLL
//
