CYSK_BACSU
ID CYSK_BACSU Reviewed; 308 AA.
AC P37887;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cysteine synthase;
DE Short=CSase;
DE EC=2.5.1.47;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE Short=OAS-TL;
DE AltName: Full=Superoxide-inducible protein 11;
DE Short=SOI11;
GN Name=cysK; OrderedLocusNames=BSU00730;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-14.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT "Cold shock stress-induced proteins in Bacillus subtilis.";
RL J. Bacteriol. 178:4611-4619(1996).
RN [4]
RP PROTEIN SEQUENCE OF 2-14.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [5]
RP DETERMINATION OF TRANSCRIPTIONAL START SITE, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=168 / BGSC1A1;
RX PubMed=11445163; DOI=10.1111/j.1574-6968.2001.tb10728.x;
RA van der Ploeg J.R., Barone M., Leisinger T.;
RT "Functional analysis of the Bacillus subtilis cysK and cysJI genes.";
RL FEMS Microbiol. Lett. 201:29-35(2001).
RN [6]
RP CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=17056751; DOI=10.1128/jb.01273-06;
RA Hullo M.-F., Auger S., Soutourina O., Barzu O., Yvon M., Danchin A.,
RA Martin-Verstraete I.;
RT "Conversion of methionine to cysteine in Bacillus subtilis and its
RT regulation.";
RL J. Bacteriol. 189:187-197(2007).
RN [7]
RP FUNCTION AS A REGULATOR OF CYMR ACTIVITY, INDUCTION, SUBUNIT, AND
RP INTERACTION WITH CYMR.
RC STRAIN=168;
RX PubMed=18974048; DOI=10.1074/jbc.m805951200;
RA Tanous C., Soutourina O., Raynal B., Hullo M.-F., Mervelet P.,
RA Gilles A.-M., Noirot P., Danchin A., England P., Martin-Verstraete I.;
RT "The CymR regulator in complex with the enzyme CysK controls cysteine
RT metabolism in Bacillus subtilis.";
RL J. Biol. Chem. 283:35551-35560(2008).
CC -!- FUNCTION: Catalyzes the conversion of O-acetylserine to cysteine. Also
CC acts as a sensor of cysteine availability in the signal transduction
CC pathway modulating CymR activity. When cysteine is present, the pool of
CC O-acetylserine (OAS) is low, which leads to the formation of a CymR-
CC CysK complex and transcriptional repression of the CymR regulon occurs.
CC In the absence of cysteine, the OAS pool is high and the CymR-CysK
CC complex is mostly dissociated, leading to a faster dissociation of CymR
CC from its DNA targets and the lifting of CymR-dependent repression.
CC {ECO:0000269|PubMed:18974048}.
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:17056751};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer. Forms CymR(2):CysK(2) or CymR(4):CysK(4) complexes
CC in the absence of O-acetylserine. {ECO:0000269|PubMed:18974048}.
CC -!- INDUCTION: Highly expressed in the presence of methionine, but poorly
CC expressed in the presence of cystine. Also induced by superoxide.
CC Repressed both by sulfate and cysteine. {ECO:0000269|PubMed:11445163,
CC ECO:0000269|PubMed:18974048}.
CC -!- DISRUPTION PHENOTYPE: Grows very slowly with sulfate, butanesulfonate
CC or cystine as sole sulfur source. {ECO:0000269|PubMed:11445163,
CC ECO:0000269|PubMed:17056751}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D26185; BAA05308.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11849.1; -; Genomic_DNA.
DR PIR; S66103; S66103.
DR RefSeq; NP_387954.1; NC_000964.3.
DR RefSeq; WP_003244491.1; NZ_JNCM01000028.1.
DR AlphaFoldDB; P37887; -.
DR SMR; P37887; -.
DR IntAct; P37887; 1.
DR MINT; P37887; -.
DR STRING; 224308.BSU00730; -.
DR MoonProt; P37887; -.
DR jPOST; P37887; -.
DR PaxDb; P37887; -.
DR PRIDE; P37887; -.
DR EnsemblBacteria; CAB11849; CAB11849; BSU_00730.
DR GeneID; 936636; -.
DR KEGG; bsu:BSU00730; -.
DR PATRIC; fig|224308.179.peg.73; -.
DR eggNOG; COG0031; Bacteria.
DR InParanoid; P37887; -.
DR OMA; FWDSGER; -.
DR PhylomeDB; P37887; -.
DR BioCyc; BSUB:BSU00730-MON; -.
DR BRENDA; 2.5.1.47; 658.
DR SABIO-RK; P37887; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IDA:CAFA.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:CAFA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:CAFA.
DR GO; GO:0009087; P:methionine catabolic process; IMP:CAFA.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:CAFA.
DR GO; GO:1904798; P:positive regulation of core promoter binding; IDA:CAFA.
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 Amino-acid biosynthesis; Cysteine biosynthesis; Direct protein sequencing;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8755892,
FT ECO:0000269|PubMed:9298659"
FT CHAIN 2..308
FT /note="Cysteine synthase"
FT /id="PRO_0000167081"
FT BINDING 75
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 179..183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 308 AA; 32820 MW; 79350923DF2B73CA CRC64;
MVRVANSITE LIGNTPIVKL NRLADENSAD VYLKLEYMNP GSSVKDRIGL AMIEAAEKEG
KLKAGNTIIE PTSGNTGIGL AMVAAAKGLK AILVMPDTMS MERRNLLRAY GAELVLTPGA
EGMKGAIKKA EELAEKHGYF VPQQFNNPSN PEIHRQTTGK EIVEQFGDDQ LDAFVAGIGT
GGTITGAGEV LKEAYPSIKI YAVEPSDSPV LSGGKPGPHK IQGIGAGFVP DILNTEVYDE
IFPVKNEEAF EYARRAAREE GILGGISSGA AIYAALQVAK KLGKGKKVLA IIPSNGERYL
STPLYQFD
