ID K6DDZ1_9BACI Unreviewed; 312 AA.
AC K6DDZ1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=N-acetylneuraminate lyase {ECO:0000313|EMBL:EKN66494.1};
GN ORFNames=BABA_15332 {ECO:0000313|EMBL:EKN66494.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN66494.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN66494.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:EKN66494.1}.
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DR EMBL; AJLS01000115; EKN66494.1; -; Genomic_DNA.
DR AlphaFoldDB; K6DDZ1; -.
DR STRING; 1117379.BABA_15332; -.
DR PATRIC; fig|1117379.3.peg.3171; -.
DR eggNOG; COG0329; Bacteria.
DR Proteomes; UP000006316; 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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 168
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 210
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 312 AA; 34926 MW; F531304A68E24768 CRC64;
MTEWDLSKFK GVFVAMYSAY DEAGDVCEDR VKKLARFYVH SGVKGLYVGG SSGEGILQTV
EERKRVVEAV MQEVGQELTI IVHVAANSTK ESKELAIHAE TCGAHAISAV PSIYYRLSEN
AVEKHWQEMI DCSSLPFIIY NIPQTTGFNL SQTLFQKVAA QDKVIGIKMS GESVFDLQQF
KAHAGKEFLV FNGPDEQYLG GRIMGADGGI GGTYGVMPEL FCVLDQYITS NQLEKAQELQ
FHINRIIKKL LSYPSLYGAC KYILSLRNIE TGFPRLPLLP VTQQDYPSLS VLNDEIKQLI
NQYTKEMERV IQ
//
