ID A0A3M8EGT5_9BACT Unreviewed; 482 AA.
AC A0A3M8EGT5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Tryptophanase {ECO:0000313|EMBL:RNC64596.1};
DE EC=4.1.99.1 {ECO:0000313|EMBL:RNC64596.1};
GN ORFNames=D7D25_10835 {ECO:0000313|EMBL:RNC64596.1};
OS Proteiniphilum sp. X52.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Proteiniphilum.
OX NCBI_TaxID=2382159 {ECO:0000313|EMBL:RNC64596.1, ECO:0000313|Proteomes:UP000272792};
RN [1] {ECO:0000313|EMBL:RNC64596.1, ECO:0000313|Proteomes:UP000272792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X52 {ECO:0000313|EMBL:RNC64596.1,
RC ECO:0000313|Proteomes:UP000272792};
RA Hivarkar S., Lanjekar V.B., Dhakephalkar P.K., Dagar S.;
RL Submitted (OCT-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:RNC64596.1}.
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DR EMBL; RDSD01000012; RNC64596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8EGT5; -.
DR OrthoDB; 9764079at2; -.
DR Proteomes; UP000272792; Unassembled WGS sequence.
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:RNC64596.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR611166-50}.
FT DOMAIN 55..428
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 482 AA; 54052 MW; DA43CB041887CF48 CRC64;
MNEIKFYNGE NIPLELHKVR VVQKLHLVPI ERRLEALREG GFNTFRLNTK DVFLDMLTDS
GTNAMSDNQM AAMMQADDAY AGSQSFFRLQ KAVEDVLGKK YYLPVHQGRA AENILSNAYV
RKGNLVPMNY HFTTAMAHIT QYGGKIAELL YDEAYVIDSS HPFKGNMNIE KLEEVIKVHG
AKNIPFIRME ASTNLIGGQP FSVQNLRDVR AIADKYNIRL VLDASLLGEN AYLVIQREEE
FKGSSMGEVM KVMTGLADIV YFSARKLSSS RGGGICTDNS DIYREMEALV PLFEGFLTYG
GISVREIEAM AVGLYETLDE TMISQSPDFI AYLVNALDAH GVPVVKPAGV LGAHVDAMKV
CDHIPQKEYP AGALAAALFL ISGIRGMERG SISNQRDEYG NETYADMELV RLAVPRRVFT
LSQIKYVEDR MTWLYENRAL IGGLRFVYEP PVLRFFMGGL EPVNDWPQKL IAKFKEDFGE
SL
//
