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Database: UniProt
Entry: Q3YV34_SHISS
LinkDB: Q3YV34_SHISS
Original site: Q3YV34_SHISS 
ID   Q3YV34_SHISS            Unreviewed;       386 AA.
AC   Q3YV34;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AAZ90628.1};
GN   Name=metB {ECO:0000313|EMBL:AAZ90628.1};
GN   OrderedLocusNames=SSON_4113 {ECO:0000313|EMBL:AAZ90628.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ90628.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ90628.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ90628.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ90628.1; -; Genomic_DNA.
DR   RefSeq; WP_001297633.1; NC_007384.1.
DR   AlphaFoldDB; Q3YV34; -.
DR   GeneID; 75203230; -.
DR   KEGG; ssn:SSON_4113; -.
DR   HOGENOM; CLU_018986_2_0_6; -.
DR   Proteomes; UP000002529; Chromosome.
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:UP000002529}.
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   386 AA;  41580 MW;  F62AD71619A43343 CRC64;
     MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG NPTRDVVQRA
     LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC YGGSYRLFDS LAKRGCYRVL
     FVDQGDEQAL RAALAEKPKL VLVESPSNPL LRVVDIAKIC HLAREVGAVS VVDNTFLSPA
     LQNPLALGAD LVLHSCTKYL NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL
     LLRGLRTLVP RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML
     SFELDGDEQT LRRFLSGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR AAAGISETLL
     RISTGIEDGE DLIADLENGF RAANKG
//
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