ID A0A517NET5_9BACT Unreviewed; 314 AA.
AC A0A517NET5;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=N-acetylneuraminate lyase {ECO:0000313|EMBL:QDT05640.1};
DE EC=4.1.3.3 {ECO:0000313|EMBL:QDT05640.1};
GN Name=nanA {ECO:0000313|EMBL:QDT05640.1};
GN ORFNames=K227x_40410 {ECO:0000313|EMBL:QDT05640.1};
OS Rubripirellula lacrimiformis.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rubripirellula.
OX NCBI_TaxID=1930273 {ECO:0000313|EMBL:QDT05640.1, ECO:0000313|Proteomes:UP000318538};
RN [1] {ECO:0000313|EMBL:QDT05640.1, ECO:0000313|Proteomes:UP000318538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22_7 {ECO:0000313|EMBL:QDT05640.1,
RC ECO:0000313|Proteomes:UP000318538};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP036525; QDT05640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A517NET5; -.
DR KEGG; rlc:K227x_40410; -.
DR OrthoDB; 9771791at2; -.
DR Proteomes; UP000318538; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-EC.
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; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128:SF21; 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:UP000318538}.
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 53
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 314 AA; 34090 MW; 185A80442724F82E CRC64;
MTQQNSVHRL QGLIAATYTP MNRDGSLNLA VVPEMVQHLI RDGVSGIYVC GSTGEGMSLT
SDERRQVAQS YVTAVDGRLP VIVQVGHNSL AEAKQLAAHA SEIGADIVSA TCPSYFKVSD
VPTLVDCMAD LASAAADLPF YYYHIPILTG STIQMADFLE HAADRIPNLA GLKYTDTKLF
EFQHCLELAD RKFDVVWGCD EMLLGAIATG AEAAIGSTYN IAAPVYQHVI DAVAAGDLPR
ARRWQARSID MIRTMGRYPF HSAMKAVLAI RGLDFGGCRL PQGRLSQSET ETLQRELDAI
GFFEWSSPQS SADS
//
