CYSK_NEUCR
ID CYSK_NEUCR Reviewed; 376 AA.
AC Q7RYW6;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Cysteine synthase 1 {ECO:0000305};
DE Short=CS 1;
DE EC=2.5.1.- {ECO:0000250|UniProtKB:O59701};
DE EC=2.5.1.47 {ECO:0000250|UniProtKB:O59701};
DE AltName: Full=O-acetylserine (thiol)-lyase 1;
DE Short=OAS-TL 1;
DE AltName: Full=O-acetylserine sulfhydrylase 1;
DE AltName: Full=O-succinylserine sulfhydrylase {ECO:0000250|UniProtKB:O59701};
DE Flags: Precursor;
GN Name=cys-17; ORFNames=NCU06452;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP PATHWAY.
RX PubMed=15522735; DOI=10.1016/s0065-2660(04)52005-9;
RA Radford A.;
RT "Metabolic highways of Neurospora crassa revisited.";
RL Adv. Genet. 52:165-207(2004).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=21145408; DOI=10.1016/j.fgb.2010.11.011;
RA Keeping A., Deabreu D., Dibernardo M., Collins R.A.;
RT "Gel-based mass spectrometric and computational approaches to the
RT mitochondrial proteome of Neurospora.";
RL Fungal Genet. Biol. 48:526-536(2011).
CC -!- FUNCTION: Catalyzes the conversion of O-succinyl-L-serine into
CC cysteine, the last step in the cysteine biosynthesis pathway. Can also
CC use O-acetyl-L-serine. {ECO:0000250|UniProtKB:O59701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-succinyl-L-serine = L-cysteine +
CC succinate; Xref=Rhea:RHEA:53816, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:136856;
CC Evidence={ECO:0000250|UniProtKB:O59701};
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:0000250|UniProtKB:O59701};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0ABK5};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000305|PubMed:15522735}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21145408}.
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; CM002238; EAA28107.1; -; Genomic_DNA.
DR RefSeq; XP_957343.1; XM_952250.2.
DR AlphaFoldDB; Q7RYW6; -.
DR SMR; Q7RYW6; -.
DR STRING; 5141.EFNCRP00000006251; -.
DR EnsemblFungi; EAA28107; EAA28107; NCU06452.
DR GeneID; 3873512; -.
DR KEGG; ncr:NCU06452; -.
DR VEuPathDB; FungiDB:NCU06452; -.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; Q7RYW6; -.
DR OMA; WMADYGF; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:EnsemblFungi.
DR Gene3D; 3.40.50.1100; -; 2.
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 PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..376
FT /note="Cysteine synthase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436604"
FT BINDING 109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 215..219
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 314
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT MOD_RES 79
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P16703"
SQ SEQUENCE 376 AA; 40711 MW; 8279C41901B9B868 CRC64;
MFRHGVRTFA TTSLRRMAAV APQEPSQYLL NVSKAQGIAK GLTGAIGNTP LIRLNRLSEE
TGCEILGKAE FMNPGGSVKD RAALYVVKDA EERGLLRPGG TVVEGTAGNT GIGLAHVCRS
KGYKLVIYMP NTQSQGKIDL LRLLGAEVYP VPAVAFENPE NYNHQARRHA ERLDNAVWTN
QFDNIANRRA HIETTGPEIW AQTGGKVDAF TCATGTGGTF AGTTRYLKEV SGGRVKAFLA
DPPGSVLHSY FSSGGKLIER SGSSITEGIG QGRITDNLKQ DVDLVDGSMT ISDEKTIEMV
YRCLDEEGLY LGASSTLNVV AAKEVAEKLG KGSTVVTMLC DGAYRYADRL FSRKWLEQKN
LLGAIPEHLQ KYIVLP
