ID A0A168EZX2_9MICO Unreviewed; 311 AA.
AC A0A168EZX2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=cysK1 {ECO:0000313|EMBL:ANC30712.1};
GN ORFNames=I598_1145 {ECO:0000313|EMBL:ANC30712.1};
OS Isoptericola dokdonensis DS-3.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC30712.1, ECO:0000313|Proteomes:UP000076794};
RN [1] {ECO:0000313|EMBL:ANC30712.1, ECO:0000313|Proteomes:UP000076794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-3 {ECO:0000313|EMBL:ANC30712.1,
RC ECO:0000313|Proteomes:UP000076794};
RA Kwon S.-K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT dokdonensis DS-3.";
RL Submitted (JAN-2016) 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 -!- 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; CP014209; ANC30712.1; -; Genomic_DNA.
DR RefSeq; WP_068202043.1; NZ_CP014209.1.
DR AlphaFoldDB; A0A168EZX2; -.
DR STRING; 1300344.I598_1145; -.
DR KEGG; ido:I598_1145; -.
DR PATRIC; fig|1300344.3.peg.1151; -.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000076794; 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:UP000076794};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 9..294
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 179..183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 267
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 311 AA; 32338 MW; 9AD6A8D9094E5FFB CRC64;
MATIYDDATK LIGRTPLVRI NRLTEGAGAT VLAKLEFYNP ASSVKDRIGV SIVDAAEASG
ELKPGGTIVE GTSGNTGIAL AFVGAARGYD VVLAMPETMS KERRALLRAY GAELILTPAA
EGMKGAVAAA ERIAAERPGA ILARQFANEA NPKIHRETTA EEIWADTDGE VDILIAGVGT
GGTITGVGQV LKERKPGVQI IAVEPEESPI LNGGAPGPHK IQGIGANFVP EILDTSVYDE
VIDVNAETAV EWAKRSAQEE GLLVGISSGA ALAAAAQVAQ RPENAGKTIV VIIPSFGERY
LSTVLFSDLL D
//
