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Database: UniProt
Entry: K9DN72_9BURK
LinkDB: K9DN72_9BURK
Original site: K9DN72_9BURK 
ID   K9DN72_9BURK            Unreviewed;       371 AA.
AC   K9DN72;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=HMPREF9710_04521 {ECO:0000313|EMBL:EKU80247.1};
OS   Massilia timonae CCUG 45783.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU80247.1, ECO:0000313|Proteomes:UP000009874};
RN   [1] {ECO:0000313|EMBL:EKU80247.1, ECO:0000313|Proteomes:UP000009874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU80247.1,
RC   ECO:0000313|Proteomes:UP000009874};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Massilia timonae CCUG 45783.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:EKU80247.1}.
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DR   EMBL; AGZI01000059; EKU80247.1; -; Genomic_DNA.
DR   RefSeq; WP_005670296.1; NZ_JH992925.1.
DR   AlphaFoldDB; K9DN72; -.
DR   STRING; 47229.LO55_4350; -.
DR   PATRIC; fig|883126.3.peg.4560; -.
DR   eggNOG; COG2008; Bacteria.
DR   HOGENOM; CLU_029381_4_0_4; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000009874; Unassembled WGS sequence.
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:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 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:UP000009874}.
FT   DOMAIN          28..294
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   371 AA;  41182 MW;  E0E90A251A29EB77 CRC64;
     MSDTDLQRRC HTIFPGHRQR RPAELFAAMA AWCEEHDVDH DVYGNGALIQ DFERKVAALL
     GFEAAVFCIS GTMAQVTALR LGASDRGSRL VALHPTSHIF VHERSNYQML DHFQALSVGD
     RHRPWVEADL AAVPDRLGAV GLEIPMREIG GQLSSWDELE AIKRHCRSRG IHLHMDGARL
     WEAQAGHGRG VAEIAAGFDS VYVSLYKGIG GLGGAMLLGS RAFVDRCAEW FRRQGGNVIH
     RSPYIVAAAM QFDERLAAMP AYFERTRFLY QALRAHPELR VNPAAPQSNM LHVHLPVDRE
     RALAVRDALA REHGIWMFNR AVHGALPASS VVEIYVGDNL LSMSDETVRE ALRRFAAALV
     ANAKMTDSPK P
//
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