ID F0GUT7_9FIRM Unreviewed; 315 AA.
AC F0GUT7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Putative N-acetylneuraminate lyase {ECO:0000313|EMBL:EGC82460.1};
GN ORFNames=HMPREF9290_1511 {ECO:0000313|EMBL:EGC82460.1};
OS Anaerococcus prevotii ACS-065-V-Col13.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=879305 {ECO:0000313|EMBL:EGC82460.1, ECO:0000313|Proteomes:UP000005286};
RN [1] {ECO:0000313|EMBL:EGC82460.1, ECO:0000313|Proteomes:UP000005286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-065-V-Col13 {ECO:0000313|EMBL:EGC82460.1,
RC ECO:0000313|Proteomes:UP000005286};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGC82460.1}.
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DR EMBL; AEXM01000012; EGC82460.1; -; Genomic_DNA.
DR RefSeq; WP_004834328.1; NZ_AEXM01000012.1.
DR AlphaFoldDB; F0GUT7; -.
DR STRING; 879305.HMPREF9290_1511; -.
DR PATRIC; fig|879305.3.peg.569; -.
DR eggNOG; COG0329; Bacteria.
DR Proteomes; UP000005286; 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 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000005286}.
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 52
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 208
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 315 AA; 35071 MW; 495C0F3DAB437FE4 CRC64;
MSKFSIKDFN GVIPAAITPF DINENIDLDA TREFTEFLLG NDIHGLYLTG STGEGFLMKS
EERMKVVETV MEVAKDKVPV VVHVGNIGTK RTIELARHAK EAGATAISSV PPFYWHFDSK
QIFNYYKDIA EAVDIPMIIY NVPLAGVLPI SLIKELGKID NIVGVKYTNT DIYQIPVIKD
ELGDDFMIYG GADELASSNI LVGVDGIVGS FYNLFPGLFV DIYNAVKNDN VKEAYKLQEK
AVRLINYVVS TNNMVAGIKS ILRDAGINAG YARKPFLNFY DKDQEQLSKE IIEIADKYDI
KGVTVIDKLK EKYQG
//
