CYSK_MYCTU
ID CYSK_MYCTU Reviewed; 310 AA.
AC P9WP55; L0TC08; P0A534; P95230;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=O-acetylserine sulfhydrylase {ECO:0000303|PubMed:17567578};
DE Short=OAS sulfhydrylase {ECO:0000303|PubMed:17567578};
DE Short=OASS {ECO:0000303|PubMed:17567578};
DE EC=2.5.1.47 {ECO:0000269|PubMed:17567578};
DE AltName: Full=Cysteine synthase A;
DE Short=CSase A;
DE AltName: Full=O-acetylserine (thiol)-lyase A;
DE Short=OAS-TL A;
DE AltName: Full=O-acetylserine-specific cysteine synthase;
DE AltName: Full=Sulfide-dependent cysteine synthase;
GN Name=cysK1; Synonyms=cysK; OrderedLocusNames=Rv2334; ORFNames=MTCY98.03;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH
RP THE REACTION INTERMEDIATE ALPHA-AMINOACRYLATE OR PEPTIDE INHIBITOR,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP REACTION MECHANISM.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17567578; DOI=10.1074/jbc.m703518200;
RA Schnell R., Oehlmann W., Singh M., Schneider G.;
RT "Structural insights into catalysis and inhibition of O-acetylserine
RT sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the
RT enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex.";
RL J. Biol. Chem. 282:23473-23481(2007).
CC -!- FUNCTION: Catalyzes the conversion of O-acetylserine (OAS) to cysteine
CC through the elimination of acetate and addition of hydrogen sulfide.
CC {ECO:0000269|PubMed:17567578}.
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:0000269|PubMed:17567578};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17567578};
CC -!- ACTIVITY REGULATION: Competitively inhibited by a four-residue peptide
CC derived from the C-terminus of serine acetyltransferase (CysE). This
CC suggests that CysK1 may associate with CysE in vivo to form a bi-enzyme
CC complex, in which the OASS activity is down-regulated.
CC {ECO:0000269|PubMed:17567578}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17567578}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45122.1; -; Genomic_DNA.
DR PIR; G70660; G70660.
DR RefSeq; WP_003899275.1; NZ_NVQJ01000012.1.
DR RefSeq; YP_177868.1; NC_000962.3.
DR PDB; 2Q3B; X-ray; 1.80 A; A=1-310.
DR PDB; 2Q3C; X-ray; 2.10 A; A=1-310.
DR PDB; 2Q3D; X-ray; 2.20 A; A=1-310.
DR PDB; 3ZEI; X-ray; 2.00 A; A=1-310.
DR PDBsum; 2Q3B; -.
DR PDBsum; 2Q3C; -.
DR PDBsum; 2Q3D; -.
DR PDBsum; 3ZEI; -.
DR AlphaFoldDB; P9WP55; -.
DR SMR; P9WP55; -.
DR STRING; 83332.Rv2334; -.
DR BindingDB; P9WP55; -.
DR ChEMBL; CHEMBL2321612; -.
DR PaxDb; P9WP55; -.
DR DNASU; 886016; -.
DR GeneID; 45426318; -.
DR GeneID; 886016; -.
DR KEGG; mtu:Rv2334; -.
DR TubercuList; Rv2334; -.
DR eggNOG; COG0031; Bacteria.
DR OMA; FWDSGER; -.
DR PhylomeDB; P9WP55; -.
DR BRENDA; 2.5.1.47; 3445.
DR Reactome; R-MTU-936721; Cysteine synthesis from O-acetylserine.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:P9WP55; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:MTBBASE.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:MTBBASE.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:MTBBASE.
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; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01139; cysK; 1.
DR TIGRFAMs; TIGR01136; cysKM; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="O-acetylserine sulfhydrylase"
FT /id="PRO_0000167094"
FT BINDING 74
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17567578"
FT BINDING 178..182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17567578"
FT BINDING 266
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17567578"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:17567578"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:2Q3B"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:2Q3B"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:2Q3B"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:2Q3B"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2Q3B"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2Q3B"
SQ SEQUENCE 310 AA; 32753 MW; 597B1106CA6D0B9A CRC64;
MSIAEDITQL IGRTPLVRLR RVTDGAVADI VAKLEFFNPA NSVKDRIGVA MLQAAEQAGL
IKPDTIILEP TSGNTGIALA MVCAARGYRC VLTMPETMSL ERRMLLRAYG AELILTPGAD
GMSGAIAKAE ELAKTDQRYF VPQQFENPAN PAIHRVTTAE EVWRDTDGKV DIVVAGVGTG
GTITGVAQVI KERKPSARFV AVEPAASPVL SGGQKGPHPI QGIGAGFVPP VLDQDLVDEI
ITVGNEDALN VARRLAREEG LLVGISSGAA TVAALQVARR PENAGKLIVV VLPDFGERYL
STPLFADVAD
