ID   A0A2Z5FSN6_9BACT        Unreviewed;       320 AA.
AC   A0A2Z5FSN6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=ACPOL_0108 {ECO:0000313|EMBL:AXC09495.1};
OS   Acidisarcina polymorpha.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidisarcina.
OX   NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC09495.1, ECO:0000313|Proteomes:UP000253606};
RN   [1] {ECO:0000313|EMBL:AXC09495.1, ECO:0000313|Proteomes:UP000253606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBC82 {ECO:0000313|EMBL:AXC09495.1,
RC   ECO:0000313|Proteomes:UP000253606};
RX   PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA   Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA   Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT   "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT   and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT   Peatlands.";
RL   Front. Microbiol. 9:2775-2775(2018).
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   -!- 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; CP030840; AXC09495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z5FSN6; -.
DR   KEGG; abas:ACPOL_0108; -.
DR   Proteomes; UP000253606; 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:UP000253606};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          20..305
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         87
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         191..195
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         278
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         57
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   320 AA;  34130 MW;  B565A05D57A81808 CRC64;
     MRAFVDHPPV HTGLRVAEDI TELMGRTPML HLRRLCGPGD ADLFAKLEFL NPGGSVKDRA
     ALGMILDAEA RGLLKPGSTI LEATAGNTGV GLALVGVNRG YKVILFVPEG FAEEKCILMR
     AFGAKVVKTP ETEGMSGAIR RALAMAKEIP DAFTALQFEN QANPRFHHDT TAVELWEQME
     GRIDAFVSGV GTGGTFSGVA QFLKEQDSSI LTVAVETEGS VLQGGEPQHH KIEGIGVSFV
     PKTFHREVTD EIVKVADADA FNMVRRMAAE EGLLGGSSAG AMVFAAAAVA RRLGPGKRVA
     TMIPDSAERY LSKKIFEGGI
//