ID Q9S2H1_STRCO Unreviewed; 316 AA.
AC Q9S2H1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE SubName: Full=Cysteine synthase {ECO:0000313|EMBL:CAB50991.1};
GN OrderedLocusNames=SCO2910 {ECO:0000313|EMBL:CAB50991.1};
GN ORFNames=SCE19A.10c {ECO:0000313|EMBL:CAB50991.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB50991.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB50991.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50};
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR EMBL; AL939114; CAB50991.1; -; Genomic_DNA.
DR PIR; T36133; T36133.
DR RefSeq; NP_627136.1; NC_003888.3.
DR RefSeq; WP_003975900.1; NZ_VNID01000010.1.
DR AlphaFoldDB; Q9S2H1; -.
DR STRING; 100226.gene:17760521; -.
DR PaxDb; 100226-SCO2910; -.
DR PATRIC; fig|100226.15.peg.2969; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_11; -.
DR InParanoid; Q9S2H1; -.
DR OrthoDB; 9805733at2; -.
DR PhylomeDB; Q9S2H1; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR005856; Cys_synth.
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 PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF255; O-PHOSPHOSERINE SULFHYDRYLASE; 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|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..287
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 316 AA; 33866 MW; 03E7B952747F6C04 CRC64;
MRYDSPLAAV GNTPLVRLPR LSPSDDVRIW AKLEDRNPTG SIKDRPALHM IEQAEKDGRL
TQGCTILEPT SGNTGISLAM AARLKGYRIV CVMPENTSQE RRDLLTMWGA EIISSPAAGG
SNTAVRVAKE LSAEHPDWVM LYQYGNPDNA GAHYAGTGPE ILADLPSVTH FVAGLGTTGT
LMGVGRYLRE HKPDVKIVAA EPRYDDLVYG LRNLDEGFVP ELYDASVLTT RFSVGSADAV
TRTRELLQQE GIFAGVSTGA ALHAAIGVGK KAVKAGESAD IVFVVADGGW KYLSTGVYTA
ETTEAAIETL HGQLWA
//
