ID A0A077EM45_9FLAO Unreviewed; 303 AA.
AC A0A077EM45;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:AIL47309.1};
GN ORFNames=BD94_3534 {ECO:0000313|EMBL:AIL47309.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL47309.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL47309.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL47309.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL47309.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL47309.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP007547; AIL47309.1; -; Genomic_DNA.
DR RefSeq; WP_024566366.1; NZ_CP007547.1.
DR AlphaFoldDB; A0A077EM45; -.
DR STRING; 1338011.BD94_3534; -.
DR KEGG; eao:BD94_3534; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_0_10; -.
DR Proteomes; UP000028933; Chromosome.
DR GO; GO:0016829; F:lyase activity; 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; PTHR12128:SF73; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365}.
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 165
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 49
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 303 AA; 33264 MW; 4605210FEE5C5B14 CRC64;
MKNTLFEGVI AYPITPFDEN EKVNIPLFRR LTERLVTSGS HAIAPLGSTG VLPYLSDEEK
EAVTEATIQQ VAGRVPTLVG VSNLTTEKTV YHAQFAEKAG ATAVMIIPMS YWKLTDDEIV
KHYDAVASKI SIPIMAYNNP ATSGVDMSPV LLKRLLEIPN VTMIKESTGD VQRMHYLRKE
LGEEVAFYNG SNPLALAAFS AGANGWCTAA PNLIPELNVE LYNAIQNNDL ETARQLFYQQ
LDLLKFIVAK GLPRAIKAGL HILGEDGGTL RSPLKPLTEA ETEELRLILS RIRTPVVTAK
KAF
//
