ID A0A1Y5XY05_KIBAR Unreviewed; 387 AA.
AC A0A1Y5XY05;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Methionine-gamma-lyase {ECO:0000313|EMBL:SMD17788.1};
GN ORFNames=SAMN05661093_05632 {ECO:0000313|EMBL:SMD17788.1};
OS Kibdelosporangium aridum.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=2030 {ECO:0000313|EMBL:SMD17788.1, ECO:0000313|Proteomes:UP000192674};
RN [1] {ECO:0000313|EMBL:SMD17788.1, ECO:0000313|Proteomes:UP000192674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43828 {ECO:0000313|EMBL:SMD17788.1,
RC ECO:0000313|Proteomes:UP000192674};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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}.
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DR EMBL; FWXV01000005; SMD17788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5XY05; -.
DR OrthoDB; 9805790at2; -.
DR Proteomes; UP000192674; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_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; 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:SF90; CYSTATHIONINE GAMMA-LYASE; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:SMD17788.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000192674}.
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 387 AA; 41373 MW; DEEB10E2A6F0000B CRC64;
MHRETRAARL TAPAPGQPVT VPLYQTSNFR FESPQELTRA MSDPDSFAYS GYGNPTNRAL
EQAMADLEQG EKALVTASGS SALSTVLQTI LRHGDHIIAQ KALYGGTVAM FNHLADRWGI
EVTYVDGVDP AEVSTALRPS TKLLFLETIA NPIGHVPDLP ALAAEAKQNG LLTAVDSTFA
TPLLCRPIEH GADIVIHSAT KYLGGHHDVV GGVAVFADEA LYRQAWKHAI NLGVVADPFA
AWLIIRGLKT LPLRVNRACE SAAMLAERMA AHPAVSAVHY PGLPTHASHA RATKLLSGYG
AIIATEVTDA QQFMGNLELI MNASSLGGTE TTVMHPATTS HRHLTADELR TAGVSQNMVR
IAVGVEHPDD LWADIEQALS PARTSRA
//
