ID R2VCN9_9ENTE Unreviewed; 377 AA.
AC R2VCN9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Cystathionine beta-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UKC_02658 {ECO:0000313|EMBL:EOI55450.1};
OS Enterococcus gilvus ATCC BAA-350.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI55450.1, ECO:0000313|Proteomes:UP000013750};
RN [1] {ECO:0000313|EMBL:EOI55450.1, ECO:0000313|Proteomes:UP000013750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI55450.1,
RC ECO:0000313|Proteomes:UP000013750};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus gilvus ATCC BAA-350.";
RL Submitted (FEB-2013) 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:EOI55450.1}.
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DR EMBL; AJDQ01000008; EOI55450.1; -; Genomic_DNA.
DR RefSeq; WP_010781031.1; NZ_KB946874.1.
DR AlphaFoldDB; R2VCN9; -.
DR PATRIC; fig|1158614.3.peg.2651; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000013750; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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:SF15; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 377 AA; 41735 MW; 4667B748F45F3486 CRC64;
MNINTKIIHG YPMIDEKTGA SSIPKIQAST FHQKDLSATQ KYTYSRFGNP TVEAMEQAVA
ALENGEFGIA FSSGVAAISS VLLLLSARDH IVLCQNIYGG TYQIVVNLLD SFNIEYTFVE
EMPASNWEEV IKENTKMIYM ETPSNPTLKI TDIQAVSAIA KEKDIITVCD NTFMTPYYQN
PLDLGVDIVI HSGTKFLNGH SDVVAGIVVT NDVIQNQRIV NQRTILGGIL GVEDAWLLMR
GIKTLGVRME RSEYNALLIS SVLNRNDNVK KVYHPSLNSH YGRKTHTRQA RGFGSVLSFE
LENVAAVENF LQKVTIPLVG VSLGGVETIL SYPWSMSHGG MTEEEKMTRQ VTPELIRLSV
GIEDVADLIM DLEQALQ
//
