ID A0A1H3KJH2_9RHOB Unreviewed; 361 AA.
AC A0A1H3KJH2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:SDY52307.1};
GN ORFNames=SAMN05444486_102588 {ECO:0000313|EMBL:SDY52307.1};
OS Lentibacter algarum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lentibacter.
OX NCBI_TaxID=576131 {ECO:0000313|EMBL:SDY52307.1, ECO:0000313|Proteomes:UP000199026};
RN [1] {ECO:0000313|EMBL:SDY52307.1, ECO:0000313|Proteomes:UP000199026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24677 {ECO:0000313|EMBL:SDY52307.1,
RC ECO:0000313|Proteomes:UP000199026};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNPR01000002; SDY52307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3KJH2; -.
DR STRING; 576131.SAMN05444486_102588; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000199026; 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 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:SDY52307.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000199026}.
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 361 AA; 38208 MW; 277531403EAB878B CRC64;
MSLPAPIESR LLAMLHARTD TLEAGDPIPE PLVLSSAFAL PSNPDARRTY ARYTNPTIEA
TEARLAALED APCLLFPSGM GAYSAAFMAL LKGGDRVLML SDGYYAARNL VSDIMAPFGV
VLETCPAANI LTADLAGYAA VVVETPSNPG LDVIDLRALA ERCRTAGAKL VVDNTVLTPL
LQQPLDLGAD IVIVSDTKAM AGHTDVLMGH VASRDAAYME RLLSVRNLTG NIPAPYEAWL
LLRGLETVEL RLERMCANAR AALPLLQASE AVSEVIYPDP SPQALDQGFL IGATFASAAA
ADRFLERAGF AKMTSFGGLH SSGDRRARWG DTVPEGFLRL SFGVEPTAAL IDAVQAALAD
G
//
