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Database: UniProt
Entry: A0A077LTM6_9MICO
LinkDB: A0A077LTM6_9MICO
Original site: A0A077LTM6_9MICO 
ID   A0A077LTM6_9MICO        Unreviewed;       306 AA.
AC   A0A077LTM6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Dihydrodipicolinate synthetase family protein {ECO:0000313|EMBL:CCH76963.1};
GN   ORFNames=BN12_1560023 {ECO:0000313|EMBL:CCH76963.1};
OS   Tetrasphaera japonica T1-X7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH76963.1, ECO:0000313|Proteomes:UP000035721};
RN   [1] {ECO:0000313|EMBL:CCH76963.1, ECO:0000313|Proteomes:UP000035721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T1-X7 {ECO:0000313|EMBL:CCH76963.1,
RC   ECO:0000313|Proteomes:UP000035721};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:CCH76963.1}.
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DR   EMBL; CAJB01000064; CCH76963.1; -; Genomic_DNA.
DR   RefSeq; WP_048553836.1; NZ_HF570958.1.
DR   AlphaFoldDB; A0A077LTM6; -.
DR   STRING; 1194083.BN12_1560023; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000035721; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
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.
DR   PROSITE; PS00665; DHDPS_1; 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:UP000035721};
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         51
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         209
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   306 AA;  32123 MW;  7AD46C350490FCC7 CRC64;
     MTTTLELRGI LPAMLTPFTE DGSAIDTTAL AALTNRLVDA GVGGLIPGGS TGEFAALSHD
     ERRLLHETVV EAAAGRVPVI AQTGALTAGE AVALSRHAEQ VGAAGVMVVP PFYDGLSFRE
     LKAYFTAVAE SIDIPVMIYH IPGVTGQQLT PDEIGELASI PGVASIKDSG GDAGALTAVQ
     ERYGDRLQVC NGWDILTYFG LSYGLKASVW GAANIFPELA VELFETISVK GDLDAARSLW
     SRLVPVVNWL DEESYTARVK AATRLLGVQV GPVRSPFQEP TDEALAEVRP LLAELGLPVE
     GLASVG
//
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