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Database: UniProt
Entry: A0A327ZK18_9ACTN
LinkDB: A0A327ZK18_9ACTN
Original site: A0A327ZK18_9ACTN 
ID   A0A327ZK18_9ACTN        Unreviewed;       462 AA.
AC   A0A327ZK18;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Tryptophanase {ECO:0000313|EMBL:RAK43202.1};
GN   ORFNames=B0I29_101332 {ECO:0000313|EMBL:RAK43202.1};
OS   Actinoplanes lutulentus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK43202.1, ECO:0000313|Proteomes:UP000249341};
RN   [1] {ECO:0000313|EMBL:RAK43202.1, ECO:0000313|Proteomes:UP000249341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK43202.1,
RC   ECO:0000313|Proteomes:UP000249341};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RAK43202.1}.
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DR   EMBL; QLMJ01000001; RAK43202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327ZK18; -.
DR   Proteomes; UP000249341; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0009072; P:aromatic 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; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR611166-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249341}.
FT   DOMAIN          50..427
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         261
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ   SEQUENCE   462 AA;  49825 MW;  31BF3EED1E8CA22B CRC64;
     MSADHIPLPP PYRIKVVEPI PFLTPEQRRD AIETAGYNPF NLRSDQITVD LLSDSGTGAT
     SSAQEAAAAL GDESYAGARS WFRFRDEVAD LTGYPHLLPV HQGRAGERIL FSSLLKPGQI
     CVSNTHFDTT HANVSIAGAT PLDLPCAAAA DLDSSEPFKG NIDLEALEST LAGPDGSRVG
     LVLMTITNNG LGAQPVSMAN LEAVRALCQR FRVPFFLDAA RFAENAWLVQ QREPGYQDWT
     PRQIATRAFE LADGCLISLK KDGLTAIGGL IGLRDDALFA QCEANLIATE GFSTYGGLSG
     RDLERLAVGL REVVDPAYLA SRAAQTAALA RMINDAGVDT IQPAGIHALY LNAGRLLPHL
     SPSEFPGHSL GCQMYLDGGI RVAELGSLYL GELDASYRVV KPAPFELVRL AIPRRVYTAE
     HFEYVAAVLG AIAKDPERIR GYRIVSAPPL LRHFKVRLTP IG
//
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