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Database: UniProt
Entry: A0A136LK13_9BACT
LinkDB: A0A136LK13_9BACT
Original site: A0A136LK13_9BACT 
ID   A0A136LK13_9BACT        Unreviewed;       461 AA.
AC   A0A136LK13;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=L-cysteine desulfhydrase {ECO:0000313|EMBL:KXK21988.1};
DE            EC=4.1.99.1 {ECO:0000313|EMBL:KXK21988.1};
GN   Name=tnaA_1 {ECO:0000313|EMBL:KXK21988.1};
GN   ORFNames=UZ12_BCD005003408 {ECO:0000313|EMBL:KXK21988.1};
OS   Bacteroidetes bacterium OLB12.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK21988.1, ECO:0000313|Proteomes:UP000070129};
RN   [1] {ECO:0000313|EMBL:KXK21988.1, ECO:0000313|Proteomes:UP000070129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB12 {ECO:0000313|EMBL:KXK21988.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK21988.1}.
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DR   EMBL; LNFR01000116; KXK21988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136LK13; -.
DR   STRING; 1619897.UZ12_BCD005003408; -.
DR   PATRIC; fig|1619897.3.peg.3734; -.
DR   Proteomes; UP000070129; Unassembled WGS sequence.
DR   GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-EC.
DR   CDD; cd00617; Tnase_like; 1.
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:KXK21988.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR611166-50}.
FT   DOMAIN          52..427
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ   SEQUENCE   461 AA;  52230 MW;  F584D7A3EF6FAF30 CRC64;
     MIKKLQKRSW AEPYKMKMVE LLKQTTRGQR SRAIKAAGYN TFLLKSEDVY IDLLTDSGTN
     AMSDRQWSAL MLGDEAYAGS NSYYKLEKAV QKFLWLQIFS AHTPGRGAEN ILSRILIRKG
     DVVPGNMYFT TTRLHQELAG GTFEDIIIDE AHDPTNEFPF KGNVDLEKLT RLIKKHGAKK
     IPYVSIATNV NMAGGQPISM KNLKELRKFT KQHGIRIIHD MTRVAENAYF IQQREKGYEK
     KSVKDIVKEI CSLTDGATMS AKKDALVNIG GFMATNEWDV FEEARNLVVI YEGLHTYGGL
     AGRDMEAIAV GIEESLNDRH QQARIGQVEY LGQQLESYGI PIVKPIGGHG VFVDAKAFLP
     HLTQDEFPAQ TLAAELYIES GVRTMERGMV SAGRKPNGEN YYPKLELVRF TIPRRVYTQA
     HMDVVAESAA AVFARRNKIR GLKVVYEPKY LRFFQARFER K
//
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