ID E4N6M2_KITSK Unreviewed; 307 AA.
AC E4N6M2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Putative dihydrodipicolinate synthase {ECO:0000313|EMBL:BAJ26853.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:BAJ26853.1};
GN Name=dapA4 {ECO:0000313|EMBL:BAJ26853.1};
GN OrderedLocusNames=KSE_10180 {ECO:0000313|EMBL:BAJ26853.1};
OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS / NBRC 14216 / KM-6054) (Streptomyces setae).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ26853.1, ECO:0000313|Proteomes:UP000007076};
RN [1] {ECO:0000313|EMBL:BAJ26853.1, ECO:0000313|Proteomes:UP000007076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA Takahashi Y., Fujita N.;
RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT snapshot of the family Streptomycetaceae.";
RL DNA Res. 17:393-406(2010).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; AP010968; BAJ26853.1; -; Genomic_DNA.
DR RefSeq; WP_014134172.1; NC_016109.1.
DR AlphaFoldDB; E4N6M2; -.
DR STRING; 452652.KSE_10180; -.
DR KEGG; ksk:KSE_10180; -.
DR PATRIC; fig|452652.3.peg.1011; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_11; -.
DR Proteomes; UP000007076; Chromosome.
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 InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000007076};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 139
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 167
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 211
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 307 AA; 32004 MW; 99E8EEF4152DAF3A CRC64;
MTARRPAFSG VVPPVVTPLT ADGEIDTASL ERLVGFLLEG GVDGLFALGS SSETAYLTEA
QRTRVLEVVV GANAGQVPVI AGCIETTTNR VIERALISRQ SGADAVVATA PFYTRTHPVE
IERHFREIAA AAELPLFAYD IPVCVHNKLD TGMLLRLAAD GVLAGVKDSS GDDVAFRYLC
LGARQLPDFA VLTGHEVVVD GALLGGADGV VPGLGNVDPH GYRRLADHAA AGDWTAAAAE
QDRLARLFEI VTVAKDTSGT AAGLGAFKTA LMLRGIIATN AMSTPMAPYD TEQTAAVAAL
LDRAGLR
//
