CYSK_NEIMB
ID CYSK_NEIMB Reviewed; 310 AA.
AC Q7DDL5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=O-acetylserine sulfhydrylase;
GN Name=cysK; OrderedLocusNames=NMB0763;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT "Characterization of the protein content of a meningococcal outer membrane
RT vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT spectrometry.";
RL Hum. Vaccin. 1:80-84(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AE002098; AAF41176.1; -; Genomic_DNA.
DR PIR; H81161; H81161.
DR RefSeq; NP_273805.1; NC_003112.2.
DR RefSeq; WP_002217611.1; NC_003112.2.
DR AlphaFoldDB; Q7DDL5; -.
DR SMR; Q7DDL5; -.
DR STRING; 122586.NMB0763; -.
DR PaxDb; Q7DDL5; -.
DR PRIDE; Q7DDL5; -.
DR EnsemblBacteria; AAF41176; AAF41176; NMB0763.
DR GeneID; 61280995; -.
DR KEGG; nme:NMB0763; -.
DR PATRIC; fig|122586.8.peg.967; -.
DR HOGENOM; CLU_021018_1_0_4; -.
DR OMA; FWDSGER; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR GO; GO:0080146; F:L-cysteine desulfhydrase 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 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; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Cysteine synthase"
FT /id="PRO_0000320266"
FT BINDING 74
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 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 32821 MW; FE9C74BF7C2AFD7A CRC64;
MKIANSITEL IGNTPLVKLN RLTEGLKAEV AVKLEFFNPG SSVKDRIAEA MIEGAEKAGK
INKNTVIVEA TSGNTGVGLA MVCAARGYKL AITMPESMSK ERKMLLRAFG AELILTPAAE
GMAGAIAKAK SLVDAHPDTY FMPRQFDNEA NPEVHRKTTA EEIWRDTDGK VDVFVAGVGT
GGTITGVGEV LKKYKPEVKV VAVEPEASPV LSGGEKGPHP IQGIGAGFIP TVLNTKIYDS
ITKVSNEAAF ETARAIAEKE GILVGISSGA AVWSALQLAK QPENEGKLIV VLLPSYGERY
LSTPLFADLA
