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Database: UniProt
Entry: A0A1U9R934_9GAMM
LinkDB: A0A1U9R934_9GAMM
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ID   A0A1U9R934_9GAMM        Unreviewed;       298 AA.
AC   A0A1U9R934;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=B2G49_05695 {ECO:0000313|EMBL:AQU82134.1};
OS   Halomonas sp. 'Soap Lake #7'.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1962264 {ECO:0000313|EMBL:AQU82134.1, ECO:0000313|Proteomes:UP000189672};
RN   [1] {ECO:0000313|EMBL:AQU82134.1, ECO:0000313|Proteomes:UP000189672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU82134.1,
RC   ECO:0000313|Proteomes:UP000189672};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AQU82134.1, ECO:0000313|Proteomes:UP000189672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU82134.1,
RC   ECO:0000313|Proteomes:UP000189672};
RA   Mormile M.R.;
RT   "Halomonas from Soap Lake, Washington USA.";
RL   Submitted (MAR-2017) 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; CP019915; AQU82134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9R934; -.
DR   STRING; 1962264.B2G49_05695; -.
DR   KEGG; haso:B2G49_05695; -.
DR   OrthoDB; 9805733at2; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000189672; 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          7..283
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         73
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         176..180
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         257
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         43
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   298 AA;  31734 MW;  54C8B95A2EFE4AE8 CRC64;
     MNYPTLEDVV GNTPLVRLKR ITAGRNNTLL AKLEGNNPAG SVKDRPALSM LGEAEARGEI
     TPGDTLIEAT SGNTGIALAM AAAIKGYNMV LVMPENASAE RKQAMAAYGA TLISASKEGG
     MEEARDIADA MIARGEGKPL NQFANPDNPL AHYRTTGPEV WRQTGGEVTH FVSSMGTTGT
     IMGVSRYLKE QNEAIQIVGL QPADGASIPG IRRWPQEYLP AIFEAPRVDV TLDIGQQEAE
     THMRRLAREE GILAGVSSGG SLAGALRIAE QTENAVIVFI VCDRGDRYLS TGLFAPEI
//
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