CYSK_EMENI
ID CYSK_EMENI Reviewed; 370 AA.
AC P50867; C8V672; Q5AUH3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cysteine synthase 1 {ECO:0000303|PubMed:9108143};
DE Short=CS 1 {ECO:0000303|PubMed:17482430};
DE EC=2.5.1.- {ECO:0000250|UniProtKB:O59701};
DE EC=2.5.1.47 {ECO:0000269|PubMed:17482430};
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=cysB {ECO:0000303|PubMed:17482430, ECO:0000303|PubMed:9108143};
GN Synonyms=cysE {ECO:0000303|PubMed:17482430}; ORFNames=AN8057;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ANA1 BIA1 PHENA2;
RX PubMed=9108143; DOI=10.1007/s002940050215;
RA Topczewski J., Sienko M., Paszewski A.;
RT "Cloning and characterization of the Aspergillus nidulans cysB gene
RT encoding cysteine synthase.";
RL Curr. Genet. 31:348-356(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION.
RX PubMed=17482430; DOI=10.1016/j.resmic.2007.03.002;
RA Brzywczy J., Natorff R., Sienko M., Paszewski A.;
RT "Multiple fungal enzymes possess cysteine synthase activity in vitro.";
RL Res. Microbiol. 158:428-436(2007).
CC -!- FUNCTION: Catalyzes the conversion of O-succinyl-L-serine into
CC cysteine, the last step in the cysteine biosynthesis pathway (By
CC similarity). Can also use O-acetyl-L-serine (PubMed:17482430).
CC {ECO:0000250|UniProtKB:O59701, ECO:0000305|PubMed:17482430}.
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:0000269|PubMed:17482430};
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:17482430}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P53206}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; U19395; AAC06128.1; -; Genomic_DNA.
DR EMBL; AACD01000139; EAA59679.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF73799.1; -; Genomic_DNA.
DR RefSeq; XP_681326.1; XM_676234.1.
DR AlphaFoldDB; P50867; -.
DR SMR; P50867; -.
DR STRING; 162425.CADANIAP00004083; -.
DR EnsemblFungi; CBF73799; CBF73799; ANIA_08057.
DR EnsemblFungi; EAA59679; EAA59679; AN8057.2.
DR GeneID; 2869229; -.
DR KEGG; ani:AN8057.2; -.
DR VEuPathDB; FungiDB:AN8057; -.
DR eggNOG; KOG1481; Eukaryota.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; P50867; -.
DR OMA; WMADYGF; -.
DR OrthoDB; 1016546at2759; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:0008652; P:cellular amino acid biosynthetic process; IMP:AspGD.
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..370
FT /note="Cysteine synthase 1"
FT /id="PRO_0000167127"
FT BINDING 103
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 209..213
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 308
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT MOD_RES 73
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT CONFLICT 38
FT /note="E -> EK (in Ref. 1; AAC06128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 39807 MW; 5672B5C43656C30A CRC64;
MFRQSVRRFA TAALRSAAES PYNVRVSQAQ GFVNGLTEAI GNTPLIRLKR LSEETGSNIL
AKAEFQNPGG SVKDRAALYV VKDAEERGLL KPGGTVVEGT AGNTGIGLAH VCRSKGYKLV
IYMPNTQSQG KIDLLRLLGA EVYPVPAVAF DNPENYNHKA RRHAESLDNA VWTNQFDNTA
NRRAHIETTG PEIWAQTGGK LDAFTCSTGT GGTLAGITYY LKQASGGRVK SFLADPPGSV
LHSYIQSGGK LVERSGSSIT EGIGQGRITD NLQPDVGTLD GSLNISDEKT IEMIYRCLDE
EGLYLGASSA LNVVAAKEVA EKLGKGSTVV TILADGAYRY ADRLFSKSWL ESKGLRNAIP
KHLEKYIVLP
