ID A0A5C5YKN0_9BACT Unreviewed; 307 AA.
AC A0A5C5YKN0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Putative 2-keto-3-deoxy-galactonate aldolase YagE {ECO:0000313|EMBL:TWT75338.1};
DE EC=4.1.2.- {ECO:0000313|EMBL:TWT75338.1};
GN Name=yagE {ECO:0000313|EMBL:TWT75338.1};
GN ORFNames=CA85_06290 {ECO:0000313|EMBL:TWT75338.1};
OS Allorhodopirellula solitaria.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Allorhodopirellula.
OX NCBI_TaxID=2527987 {ECO:0000313|EMBL:TWT75338.1, ECO:0000313|Proteomes:UP000318053};
RN [1] {ECO:0000313|EMBL:TWT75338.1, ECO:0000313|Proteomes:UP000318053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CA85 {ECO:0000313|EMBL:TWT75338.1,
RC ECO:0000313|Proteomes:UP000318053};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op Den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) 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:TWT75338.1}.
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DR EMBL; SJPK01000001; TWT75338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C5YKN0; -.
DR OrthoDB; 9782828at2; -.
DR Proteomes; UP000318053; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR020625; Schiff_base-form_aldolases_AS.
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; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000318053};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 171
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 55
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 215
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 307 AA; 33230 MW; 422008A44E51AE44 CRC64;
MSDPSTSTAF SLGGIVPPLI TPLSARDVLD REGLARLLDH VIDGGVTGVF ILGTTGEAPS
LSYRLRRELI AETMQLVDGR VRVLVGVTDT AFVETVNLAQ YAADCGADAA VLTTPYYFPA
GQTELTSYVE AIQPLIPLPL MLYNMPQLTK VWFEIDTLRR LSAIDGIVGV KDSSGDMDYF
AQLCQLKQDR PDWSILLGPE AKLAEAHALG GDGGVCGGAN VAPRLFTSCF ESLQERDASA
VDSIQQKIDR FQDIYDIGKY ASRHIKATKA AASLIGICND LPADPFHAFA QPERERVAEI
LRSIDIL
//
