ID X5DJP3_9CORY Unreviewed; 446 AA.
AC X5DJP3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:AHW63293.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:AHW63293.1};
GN Name=metY {ECO:0000313|EMBL:AHW63293.1};
GN ORFNames=CGLY_04225 {ECO:0000313|EMBL:AHW63293.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW63293.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW63293.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW63293.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP006842; AHW63293.1; -; Genomic_DNA.
DR RefSeq; WP_038546546.1; NZ_CP006842.1.
DR AlphaFoldDB; X5DJP3; -.
DR STRING; 1404245.CGLY_04225; -.
DR KEGG; cgy:CGLY_04225; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_11; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000023703; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Lyase {ECO:0000313|EMBL:AHW63293.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000023703};
KW Transferase {ECO:0000313|EMBL:AHW63293.1}.
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 446 AA; 47387 MW; 4F1F3A930F6F2EFA CRC64;
MSTRYDNSDS ASWGFASRAV HAGQTVDSDT GARNQPIYLT TSYVFDSAEH AKQRFALEDL
GPVYSRLTNP TQEALENRIG SLEGGVHAVA FASGQAAETA AIFNLAGAGD HIVTSPRLYG
GTETLFGITL ARLGIEVTFV EEPDNLDSWQ AAVQPNTKAF YGETFANPQA DVLDIPALAE
VAHRNNVPLI VDNTIATAAL VRPLELGADI VVASLTKFYT GNGSGLGGIL VDGGSFDWTV
ERDGEPVFPS FVTPDPAYHG LKYADLGAAA FGLKARVGLL RDTGAALSAF NAWVTIQGLD
TLALRVRKHN ENAEIVAGSL AENPAVATVN YAGLPDSPWY ATKEKLGLEY TGSVLSFDLA
VDDVWSDEAR EKAWAFIDAL KLHSNLANVG DVRSLVVHPA TTTHSQSDQK GLARAGVNLA
TVRLSVGIED IEDILADLQL GFDAIN
//
