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Database: UniProt
Entry: B5XVS2_KLEP3
LinkDB: B5XVS2_KLEP3
Original site: B5XVS2_KLEP3 
ID   B5XVS2_KLEP3            Unreviewed;       303 AA.
AC   B5XVS2;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
GN   Name=cysM {ECO:0000313|EMBL:ACI09314.1};
GN   OrderedLocusNames=KPK_1370 {ECO:0000313|EMBL:ACI09314.1};
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI09314.1, ECO:0000313|Proteomes:UP000001734};
RN   [1] {ECO:0000313|EMBL:ACI09314.1, ECO:0000313|Proteomes:UP000001734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342 {ECO:0000313|EMBL:ACI09314.1,
RC   ECO:0000313|Proteomes:UP000001734};
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC         Evidence={ECO:0000256|ARBA:ARBA00000298,
CC         ECO:0000256|RuleBase:RU003985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC       ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; CP000964; ACI09314.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XVS2; -.
DR   KEGG; kpe:KPK_1370; -.
DR   HOGENOM; CLU_021018_1_0_6; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000001734; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005858; CysM.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01136; cysKM; 1.
DR   NCBIfam; TIGR01138; cysM; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF162; CYSTEINE SYNTHASE B; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW   ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR605856-50};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          6..281
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         71
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         174..178
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         255
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   303 AA;  32558 MW;  B957BA402942690D CRC64;
     MNTLEHTIGN TPLVKLQRLG PDNGSEVWVK LEGNNPAGSV KDRAALSMIV EAEKRGEIQP
     GDVLIEATSG NTGIALAMIA ALKGYHMKLL MPDNMSQERR AAMRAYGAEL ILVTKEQGME
     GARDLALEMA QRGEGKLLDQ FNNPDNPYAH YTTTGPEIWQ QTAGRITHFV SSMGTTGTIT
     GVSRFLREQS KPVAIVGLQP EEGSSIPGIR RWPAEYMPGI FNASLVDAVL DIHQQDAENT
     MRQLAVREGI FCGVSSGGAV AGALRIAREN PGAVVVAIVC DRGDRYLSTG VFGEEHFSQG
     AGI
//
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