CYSKL_NEUCR
ID CYSKL_NEUCR Reviewed; 456 AA.
AC Q7SHQ1;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Cysteine synthase 2 {ECO:0000305};
DE Short=CS 2;
DE EC=2.5.1.47 {ECO:0000250|UniProtKB:P0ABK5};
DE AltName: Full=Cysteine synthase-like protein;
DE Short=CSl;
DE AltName: Full=O-acetylserine (thiol)-lyase 2;
DE Short=OAS-TL 2;
DE AltName: Full=O-acetylserine sulfhydrylase 2;
GN Name=cys-12 {ECO:0000303|PubMed:15522735}; ORFNames=NCU02564;
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=16294304; DOI=10.1002/pmic.200402084;
RA Schmitt S., Prokisch H., Schlunck T., Camp D.G. II, Ahting U.,
RA Waizenegger T., Scharfe C., Meitinger T., Imhof A., Neupert W.,
RA Oefner P.J., Rapaport D.;
RT "Proteome analysis of mitochondrial outer membrane from Neurospora
RT crassa.";
RL Proteomics 6:72-80(2006).
CC -!- FUNCTION: Putative cysteine synthase that catalyzes the conversion of
CC O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine
CC biosynthesis pathway. However, in contrast to cysteine synthase cys-17,
CC this CS-like protein may not function in cysteine biosynthesis.
CC {ECO:0000250|UniProtKB:Q5BD67}.
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:P0ABK5};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0ABK5};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16294304}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; CM002236; EAA36459.1; -; Genomic_DNA.
DR RefSeq; XP_965695.1; XM_960602.2.
DR AlphaFoldDB; Q7SHQ1; -.
DR SMR; Q7SHQ1; -.
DR STRING; 5141.EFNCRP00000002220; -.
DR EnsemblFungi; EAA36459; EAA36459; NCU02564.
DR GeneID; 3881813; -.
DR KEGG; ncr:NCU02564; -.
DR VEuPathDB; FungiDB:NCU02564; -.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; Q7SHQ1; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
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; 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 Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..456
FT /note="Cysteine synthase 2"
FT /id="PRO_0000436605"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 49854 MW; BE875B27CB0A7710 CRC64;
MSISDHPRVY GTVALTAAFA AGILVTLGFK DCYPELENRY QRRRNRNLSR SNGDYGVVVP
TANRVHRESL IFGPVRLEDH EEVTSNINSS FDWVEGIEGC IGNTPLVMIR SLSEATGCVI
LAKAELLNGA GGSPKDRVAL NMIQDAEERG LLVPGRGDTI YEGTVGSTGI SLATLARAKG
YKCHICMPND MAIEKSQLLH HLGATVERVD PAPITSPDHF VNLARRRARE HEAVHADGSV
GFFADQFEST ANYQAHVKTT GPEIYRQTGG QLDAFVAGAG TGGTIAGVAK YLKEEKNLWE
TRVVLADPQG SGLFNKIRHG VMYSSTEREG TRRRQQVDTM VEGIGINRIT ENFESGRVLI
DDAVRVTDEQ ACRMARWLVE HDGIFCGSST AVNCVAAVVT AMKLPRGSRV VTLLCDSGNR
HLSKFWKHIG DMGLENDTQA QAEDLFAELG LEELKR
