ID A0A292Z6V9_9PSEU Unreviewed; 362 AA.
AC A0A292Z6V9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:GAY12262.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:GAY12262.1};
GN ORFNames=TOK_0654 {ECO:0000313|EMBL:GAY12262.1};
OS Pseudonocardia sp. N23.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY12262.1, ECO:0000313|Proteomes:UP000222857};
RN [1] {ECO:0000313|EMBL:GAY12262.1, ECO:0000313|Proteomes:UP000222857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N23 {ECO:0000313|EMBL:GAY12262.1,
RC ECO:0000313|Proteomes:UP000222857};
RA Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4-
RT dioxane-degrading ability.";
RL Submitted (AUG-2017) 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|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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:GAY12262.1}.
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DR EMBL; BEGX01000114; GAY12262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292Z6V9; -.
DR OrthoDB; 9805790at2; -.
DR Proteomes; UP000222857; Unassembled WGS sequence.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:GAY12262.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 362 AA; 37170 MW; E628895A013B1C49 CRC64;
MTELGDGTRC VHGGGPAPGV GEPLHPGPVL SSTFELGLPG DPAGADFYGR AGNPTWRVLE
SAIGGLEGGD CTLFASGMAA TAAVLLSCAR GGEVVLPSDG YYLARALAAD LGLPVRLVPT
TLAAEAPMHD VALVLLETPS NPGLDVCDIV VVAARAHAAG ALVAVDNTTA TPLGQRPLEL
GADLVVASDT KALAGHGDVV LGHVTTADPA LAARLRDTRT RGGAVPGPME VWLAHRGLGT
LDLRLERQAA NARALATALR GHPAVRDVRW PGLADDPAHA VAARQMRRWN GVLRFTLRDP
AAVGAFLAAS RFVESATSFG GLRTSADRRE RWGDDVASGL VRLSAGCEDT ADLVEDVLAA
LD
//
