ID A0A1M5CTQ1_9CLOT Unreviewed; 296 AA.
AC A0A1M5CTQ1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=N-acetylneuraminate lyase {ECO:0000313|EMBL:SHF57692.1};
GN ORFNames=SAMN02745158_04274 {ECO:0000313|EMBL:SHF57692.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHF57692.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHF57692.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHF57692.1,
RC ECO:0000313|Proteomes:UP000184245};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; FQVI01000045; SHF57692.1; -; Genomic_DNA.
DR RefSeq; WP_072854787.1; NZ_FQVI01000045.1.
DR AlphaFoldDB; A0A1M5CTQ1; -.
DR STRING; 1122155.SAMN02745158_04274; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000184245; Unassembled WGS sequence.
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 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000184245}.
FT ACT_SITE 136
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 163
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 206
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 296 AA; 32163 MW; 533BDCED09DFFE36 CRC64;
MDVKRFSGVY PAVITPFNEA GEVDTQKLTV YTEYLCGKVD GLFVGGSYGS GPIMTAEQRK
TVAETVMAVA KGRVPVILMI GCTDTNSTIE LAKHAQRVGA DAVAAVTPCY YRHTEDVIIQ
YYRDLIQAVD LPVIAYNNPK YSNFCISGDL LAKLADIGLE GIKDSSADIA LFYDYMAKVK
KEGFLFLIGS QTHLVPAVVG GAHGVVSGLS NAFPEFIKEI YDACKAGAFQ KARDMQLKAN
LLRSVTGSGI PVPFYHAVLP MLGIDIGIPK KPFLPRTEEE VERIRKALVE TKMIIG
//
