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Database: UniProt
Entry: D2S0Y4_HALTV
LinkDB: D2S0Y4_HALTV
Original site: D2S0Y4_HALTV 
ID   D2S0Y4_HALTV            Unreviewed;       319 AA.
AC   D2S0Y4;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:ADB63031.1};
GN   OrderedLocusNames=Htur_4210 {ECO:0000313|EMBL:ADB63031.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG   Plasmid pHTUR01 {ECO:0000313|EMBL:ADB63031.1,
OG   ECO:0000313|Proteomes:UP000001903}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63031.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB63031.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RC   PLASMID=pHTUR01 {ECO:0000313|EMBL:ADB63031.1,
RC   ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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DR   EMBL; CP001861; ADB63031.1; -; Genomic_DNA.
DR   RefSeq; WP_012945275.1; NC_013744.1.
DR   AlphaFoldDB; D2S0Y4; -.
DR   GeneID; 8744838; -.
DR   KEGG; htu:Htur_4210; -.
DR   HOGENOM; CLU_049343_5_2_2; -.
DR   OrthoDB; 33636at2157; -.
DR   Proteomes; UP000001903; Plasmid pHTUR01.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProt.
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   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:ADB63031.1}.
FT   ACT_SITE        142
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        166
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
SQ   SEQUENCE   319 AA;  34822 MW;  F8991D03D77CAAB7 CRC64;
     MSLATAEVKE RLRGVAVGIL TPFDQDGEIE HWKIEENAQS LYDEGIRTFL AAANISEYHS
     LADQERIDVT EAAVTSLPSD ACVLAGVGGS TNQAQDLIRA YDQIGVDAMM VMPPDHTYLH
     EQGLLEYYRS LADATETPLV PYVRGFDPSV EYLAQLTKLD GVVGIKYALT DSVKLGAGIS
     AGADDVVWVN GLAEPYAVSY WAEGVEGFSA GVSNFRPEIG LELYDALANE NWSRARELRD
     VSLPYQSFRE KTGQNNTIAG GVSVPAVKKG LELAGLYGGD VREPIRSLTP QEEKRAEELY
     DQLNDKLEQL LSNDTVEKA
//
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