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Database: UniProt
Entry: Q7MWW1_PORGI
LinkDB: Q7MWW1_PORGI
Original site: Q7MWW1_PORGI 
ID   Q7MWW1_PORGI            Unreviewed;       345 AA.
AC   Q7MWW1;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:AAQ65669.1};
GN   OrderedLocusNames=PG_0474 {ECO:0000313|EMBL:AAQ65669.1};
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ65669.1, ECO:0000313|Proteomes:UP000000588};
RN   [1] {ECO:0000313|EMBL:AAQ65669.1, ECO:0000313|Proteomes:UP000000588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX   PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA   Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA   Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA   Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA   Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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DR   EMBL; AE015924; AAQ65669.1; -; Genomic_DNA.
DR   RefSeq; WP_005873862.1; NC_002950.2.
DR   AlphaFoldDB; Q7MWW1; -.
DR   STRING; 242619.PG_0474; -.
DR   EnsemblBacteria; AAQ65669; AAQ65669; PG_0474.
DR   KEGG; pgi:PG_0474; -.
DR   eggNOG; COG2008; Bacteria.
DR   HOGENOM; CLU_049619_1_0_10; -.
DR   Proteomes; UP000000588; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000588}.
FT   DOMAIN          30..290
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   345 AA;  38107 MW;  1D74CA4C89999FA6 CRC64;
     MSKISFKNDY SEGAHPDILH ALTDTNFVPQ EGYGYDSYCE EARAMIRREC NKPDAEVHFV
     SGGTQTNLLA ISHLLRPHEA VIAAQSGHIN VHETGAIEST GHKVCTVPTP LGKLSVEHIR
     EVLAFHTDEH MVRPSMVYIS QSTELGTLYS RHELSDLSTF CRANGLLLYL DGARIGSAIM
     AETEDNPTLT DIATLTDAFY IGGTKNGALL GEAIVFPRPR PDDAFLYQIK QRGAMLAKGR
     VLGIQFATLF RDGLYYRLAA HANRMAADLA TAISFCGYSF LYPPQTNQIF PILPNDLIER
     LKTVFDFYVW QAVSPDSSAI RLVTSWATPS ENVAAFAEYL STSHI
//
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