ID A0A0A0F3Q4_9GAMM Unreviewed; 406 AA.
AC A0A0A0F3Q4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KGM57439.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:KGM57439.1};
GN ORFNames=N799_08375 {ECO:0000313|EMBL:KGM57439.1};
OS Lysobacter arseniciresistens ZS79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM57439.1, ECO:0000313|Proteomes:UP000029989};
RN [1] {ECO:0000313|EMBL:KGM57439.1, ECO:0000313|Proteomes:UP000029989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS79 {ECO:0000313|EMBL:KGM57439.1,
RC ECO:0000313|Proteomes:UP000029989};
RX PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA Liu L., Zhang S., Luo M., Wang G.;
RT "Genomic information of the arsenic-resistant bacterium Lysobacter
RT arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT genomes.";
RL Stand. Genomic Sci. 10:88-88(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|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:KGM57439.1}.
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DR EMBL; AVPT01000003; KGM57439.1; -; Genomic_DNA.
DR RefSeq; WP_036207638.1; NZ_AVPT01000003.1.
DR AlphaFoldDB; A0A0A0F3Q4; -.
DR STRING; 913325.N799_08375; -.
DR eggNOG; COG0626; Bacteria.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000029989; Unassembled WGS sequence.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); 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; IPR011821; O_succ_thio_ly.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR02080; O_succ_thio_ly; 1.
DR PANTHER; PTHR11808:SF75; CYSTATHIONINE GAMMA-SYNTHASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029989};
KW Transferase {ECO:0000313|EMBL:KGM57439.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 406 AA; 42270 MW; A2224337D3FC48F3 CRC64;
MSVDLLRPAA GATAHGCTAA VRAGIDHDTA YGAVTPPLVL SSNFSFAGFN DKRRYDYSRS
GNPTRDLLAD ALSELEGGAG GVVTATGMAA ITLVLHTLLE PGDRLVVPHD GYGGSWRLFN
ALAAKGAFEL LTVDLTDPRA LADALAQGPA VVWIETPSNP LLRITDLRFV IEAAHAAGAL
AVVDNTFLSP ALQQPIAFGA DVVVHSTTKY INGHSDVVGG AVVARDAELH ERLSWWANCL
GITGAPFDSF LTLRGLRTLD ARLRVHQENT AALVGLLEAH PAVRAVHYPG RPSHPGHAVA
ARQQRGFGAM LSVEIDGGEA GVRAFIDGLH CFTLAESLGG VESLVAHPAT MTHAAMSPEA
RAAAGIGDGL LRLSVGIEHV DDLRADIAAA LERVAAVVAG KCSVSK
//