CYSKL_EMENI
ID CYSKL_EMENI Reviewed; 428 AA.
AC Q5BD67; C8VMP5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 {ECO:0000303|PubMed:17482430};
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=cysF {ECO:0000303|PubMed:17482430}; ORFNames=AN1513;
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 [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 [2]
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 [3]
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: 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 cysB,
CC this CS-like protein seems not to function in cysteine biosynthesis.
CC {ECO:0000305|PubMed:17482430}.
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:0000250|UniProtKB:Q7SHQ1}; 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; BN001307; CBF85019.1; -; Genomic_DNA.
DR EMBL; AACD01000023; EAA63826.1; -; Genomic_DNA.
DR RefSeq; XP_659117.1; XM_654025.1.
DR AlphaFoldDB; Q5BD67; -.
DR SMR; Q5BD67; -.
DR STRING; 162425.CADANIAP00008139; -.
DR EnsemblFungi; CBF85019; CBF85019; ANIA_01513.
DR EnsemblFungi; EAA63826; EAA63826; AN1513.2.
DR GeneID; 2874711; -.
DR KEGG; ani:AN1513.2; -.
DR VEuPathDB; FungiDB:AN1513; -.
DR eggNOG; KOG1481; Eukaryota.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; Q5BD67; -.
DR OMA; FWDSGER; -.
DR OrthoDB; 1016546at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Cysteine synthase 2"
FT /id="PRO_0000436603"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 260..264
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT BINDING 367
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P16703"
FT MOD_RES 106
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P16703"
SQ SEQUENCE 428 AA; 45859 MW; 632FBDD157F6D1FD CRC64;
MPDHSHIYIG SAFVAGVVLT IAFKDLFYPE IEERIRDYRA RHSSKSYQNA SVDSLAVRHG
PPAIVDGIEG CIGNTPLLRI KSLSEATGCE ILAKAEFLNG AGQSSKDRVA LSMIELAEER
GLMTPHSGDT IYEGTSGSTG ISLATLARAK GYLAHICMPS DQAIEKSNLL LKLGAIVDRV
PPAPIVEKDN FVNRARALAQ AHTNSTASES SVGTASQRGR GYFADQFENE ANWRAHYNGT
GPEIYAQCNG SLDAFVAGAG TGGTISGVAL YLKPRIPNMT VVVADPQGSG LYNRVRYGVM
FDTKEKEGTR RRRQVDTIVE GIGINRVTAN FEAGRELVDD AVRVTDAQAL AMARWLVEKD
GIFAGSSSAV NCFAAVKTAL KLGPGHRIVT MLSDSGSRHL SRFWAKAGNV GGAVDTKLED
VLNAKEDQ
