ID   A0A172TG86_9BACL        Unreviewed;       312 AA.
AC   A0A172TG86;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00019371, ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
GN   ORFNames=SY83_06380 {ECO:0000313|EMBL:ANE45972.1};
OS   Paenibacillus swuensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE45972.1, ECO:0000313|Proteomes:UP000076927};
RN   [1] {ECO:0000313|EMBL:ANE45972.1, ECO:0000313|Proteomes:UP000076927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY6 {ECO:0000313|EMBL:ANE45972.1,
RC   ECO:0000313|Proteomes:UP000076927};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011388; ANE45972.1; -; Genomic_DNA.
DR   RefSeq; WP_068605289.1; NZ_CP011388.1.
DR   AlphaFoldDB; A0A172TG86; -.
DR   STRING; 1178515.SY83_06380; -.
DR   KEGG; pswu:SY83_06380; -.
DR   PATRIC; fig|1178515.4.peg.1272; -.
DR   OrthoDB; 9808024at2; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000076927; 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; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01139; cysK; 1.
DR   NCBIfam; TIGR01136; cysKM; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000076927};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          8..296
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         75
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         182..186
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         270
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   312 AA;  33023 MW;  3864A4E5D99B8ADC CRC64;
     MAKLVQSITD LIGDTPLVRL NRVVPEDSAE IYLKLEFQNP GASVKDRIAI NMIESAEKDG
     TLKPGATIIE PTSGNTGIGL AMVAAAKGYK AILVMPETMS MERRNLLRAY GAELVLTPGA
     EGMKGAIRKA EELQAENPSY FIPQQFKNQA NVEIHIKTTG PEIVEAIKAH DSQLDAFISG
     IGTGGTITGA GSVLKENFPG IQIIAVEPAA SPVLSGGKPG PHKIQGIGAG FVPDILNTEI
     YDEIIQVENE DAFATARRVA KEEGILGGIS SGAAIHAALQ VAKKLGKGKR VVAVIPSNGE
     RYLSTPLYQF ED
//