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Database: UniProt
Entry: A1SH52_NOCSJ
LinkDB: A1SH52_NOCSJ
Original site: A1SH52_NOCSJ 
ID   A1SH52_NOCSJ            Unreviewed;       462 AA.
AC   A1SH52;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Tryptophanase {ECO:0000313|EMBL:ABL81137.1};
DE            EC=4.1.99.1 {ECO:0000313|EMBL:ABL81137.1};
GN   OrderedLocusNames=Noca_1624 {ECO:0000313|EMBL:ABL81137.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL81137.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL81137.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A.,
RA   Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S.,
RA   Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A.,
RA   Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R.,
RA   Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete
RT   Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR611166-50};
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000256|ARBA:ARBA00009721}.
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DR   EMBL; CP000509; ABL81137.1; -; Genomic_DNA.
DR   RefSeq; WP_011755084.1; NC_008699.1.
DR   AlphaFoldDB; A1SH52; -.
DR   STRING; 196162.Noca_1624; -.
DR   KEGG; nca:Noca_1624; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_11; -.
DR   OrthoDB; 9764079at2; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-EC.
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; IPR011166; Beta-eliminating_lyase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR32325; BETA-ELIMINATING LYASE-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32325:SF4; TRYPTOPHANASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF001386; Trpase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ABL81137.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR611166-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640}.
FT   DOMAIN          50..423
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         260
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ   SEQUENCE   462 AA;  50751 MW;  DDBEF77BBFA14F6D CRC64;
     MDQPFRTIIE PFRIHSVEPM RMTTAEERRT HLAAVDYNLF QLRAEHVLID LLTDSGTGAM
     SRDQWAAVQR GDESYAGSPS YFVFRDAVRR LFDFEHIIPV HQGRAAERIL FSVLGGAGKV
     IPNNTHFDTT RANIEATGAE AVDLVIAEGR DPRSDHPFKG NMDLAALEQL LEAHADDVPC
     VMVTITNNSG GGQPVSLANL RGVRALCDRF GKPLFLDACR FAENAWFIRE REAGQGERDV
     VDIIRDVTGL ADGVTMSAKK DPLGNIGGWL ALADDDLAAQ CRNIVILTEG FPTYGGLAGR
     DLEALAQGLA EVVQHDYLRY RIGSTAYLGR ALAERGVPVL SPFGGHAIYL DARALLPHLD
     PLEYPGQAVA VALYEIGGIR SCEIGTVMFG RHPDGSEQPA AMDLVRLAIP RRTYTQSHID
     YVIEVCERIL DRASDLPGYR IVEEPPALRH FTARFAPLGR TA
//
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