ID   DAPAL_RHIML             Reviewed;         300 AA.
AC   O69782;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Uncharacterized DapA-like lyase;
DE            EC=4.-.-.-;
GN   Name=dapAL;
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OG   Plasmid pRmeGR4b.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND EXPRESSION IN E.COLI.
RC   STRAIN=GR4;
RX   PubMed=10896225; DOI=10.1007/s002030000169;
RA   Garcia-Rodriguez F.M., Zekri S., Toro N.;
RT   "Characterization of the Sinorhizobium meliloti genes encoding a functional
RT   dihydrodipicolinate synthase (dapA) and dihydrodipicolinate reductase
RT   (dapB).";
RL   Arch. Microbiol. 173:438-444(2000).
CC   -!- FUNCTION: Upon expression in E.coli complements a dapA deletion
CC       mutation, but this may not be its physiological function.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Expressed in vegetatively growing cells and in nodules.
CC       {ECO:0000269|PubMed:10896225}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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DR   EMBL; AJ222715; CAA10957.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69782; -.
DR   SMR; O69782; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Plasmid; Schiff base.
FT   CHAIN           1..300
FT                   /note="Uncharacterized DapA-like lyase"
FT                   /id="PRO_0000103142"
FT   ACT_SITE        49
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            137
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  32297 MW;  5B2F50DDF5625FB5 CRC64;
     MALRTDWNGV FPAMVTPFRE NGSFDEASFK ALIELYISEG VKGVVVTGST GEWYSMSDAE
     RATVWEVAVE ASSGRITVIA GTSAVGTREA LALTRTAKAV GVDGCMLLPP GGIFAARNEV
     VNYFHTLAGV GLPIMVYNNP PRTGVNMDAD MVAEIAKSEE IVSFKDINRY LYAASEIIYR
     VCDKLAVFTG LEPYASSVLP RGAVGVVSTI SNICAANMVS YYNAVISGDS ATAYKTQKLI
     DQLYHFLPTL GAPAFVSVKA AMKLLGRPGG EIRLPHLPAN EALIGKLREE LRRLKMMTLN