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Database: UniProt
Entry: A0A0B0D3Z4_9BACI
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ID   A0A0B0D3Z4_9BACI        Unreviewed;       308 AA.
AC   A0A0B0D3Z4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=LD39_05940 {ECO:0000313|EMBL:KHE72168.1};
OS   Halobacillus sp. BBL2006.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE72168.1, ECO:0000313|Proteomes:UP000030879};
RN   [1] {ECO:0000313|EMBL:KHE72168.1, ECO:0000313|Proteomes:UP000030879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BBL2006 {ECO:0000313|EMBL:KHE72168.1,
RC   ECO:0000313|Proteomes:UP000030879};
RA   Kirchner G., Treves D., Francis J.III.;
RT   "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT   BBL2006.";
RL   Submitted (SEP-2014) 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}.
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:KHE72168.1}.
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DR   EMBL; JRNX01000166; KHE72168.1; -; Genomic_DNA.
DR   RefSeq; WP_035543949.1; NZ_JRNX01000166.1.
DR   AlphaFoldDB; A0A0B0D3Z4; -.
DR   OrthoDB; 9808024at2; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000030879; Unassembled WGS sequence.
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:UP000030879};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          7..291
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         74
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         177..181
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         265
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         44
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   308 AA;  32530 MW;  7021B786EC8964C9 CRC64;
     MRIANNVSEL VGQTPMVKLV GSADDDSADI YLKLEYMNPG SSVKDRIALS MVEEAEKAGH
     LKDGDTIVEP TSGNTGIGLA MIAAAKGYKS VLVMPDTMSQ ERRNLLRAYG ADLVLTPGSE
     GMKGAIKKAA ELSEKHGYFM PQQFNNEANP LIHEKTTGPE IVEQMGDQLD AFVAGIGTGG
     TITGAGKVLK DRYPDVKIYA IEPEGSPVLS GGDPGPHKIQ GIGAGFVPGI LNTKVYDEVV
     QVSTEDSFAA AREAARKDGI LGGISSGAAI HVAKQVAKKL GKGKKVVAII PSNGERYLST
     PLYQFDEE
//
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