ID A0A1D7QJK1_9SPHI Unreviewed; 379 AA.
AC A0A1D7QJK1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AOM78854.1};
GN ORFNames=BFS30_17735 {ECO:0000313|EMBL:AOM78854.1};
OS Pedobacter steynii.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM78854.1, ECO:0000313|Proteomes:UP000094313};
RN [1] {ECO:0000313|EMBL:AOM78854.1, ECO:0000313|Proteomes:UP000094313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX4 {ECO:0000313|EMBL:AOM78854.1,
RC ECO:0000313|Proteomes:UP000094313};
RA Seilhamer J.J.;
RL Submitted (AUG-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; CP017141; AOM78854.1; -; Genomic_DNA.
DR RefSeq; WP_069380518.1; NZ_CP017141.1.
DR AlphaFoldDB; A0A1D7QJK1; -.
DR KEGG; psty:BFS30_17735; -.
DR OrthoDB; 9773476at2; -.
DR Proteomes; UP000094313; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000094313}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 379 AA; 42074 MW; 01342CC9BDE3AEA8 CRC64;
MKFATKAIHA GQEPDPSTGA VMTPIYQTST YWQKSPGDHQ GFEYSRGTNP TRKALEACLA
ALENAKHGLA FSSGMGATDT VLRLLQPGDE VITGNDLYGG SYRIFTKVYA KYGIKFHFLD
LSKPENMLPY INDKTKLVWI ETPTNPTMQI IDIEGIARIT KERKLILTVD NTFASPYLQN
PMDLGADIVM HSVTKYIGGH SDVVMGALLV NDDQLYKDLW FIYNACGATP GPQDAFLVLR
GIKTLHLRMK AHCENGEKVA RFLKSHPKVD KIYWPGFEDH PNHDIAKKQM RGFGGMVSIT
LKDADLQETF RIASSFKVFT LAESLGGVES LINHPVSMTH GSIPKEEREK VGVTDNLLRL
SVGVEDIDDL IADLEQALK
//
