(data stored in ACNUC16935 zone)

SWISSPROT: 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   05-JUL-2017, entry version 91.
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community 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
RT   vitro.";
RL   Res. Microbiol. 158:428-436(2007).
CC   -!- FUNCTION: Putative cysteine synthase that catalyzes the conversion
CC       of O-acetyl-L-serine (OAS) into cysteine, the last step in the
CC       cysteine biosynthesis pathway. However, in contrast to cysteine
CC       synthase cysB, this CS-like protein seems not to function in
CC       cysteine biosynthesis. {ECO:0000305|PubMed:17482430}.
CC   -!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L-
CC       cysteine + acetate. {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}.
DR   EMBL; BN001307; CBF85019.1; -; Genomic_DNA.
DR   EMBL; AACD01000023; EAA63826.1; -; Genomic_DNA.
DR   RefSeq; XP_659117.1; XM_654025.1.
DR   ProteinModelPortal; Q5BD67; -.
DR   SMR; Q5BD67; -.
DR   STRING; 162425.CADANIAP00008139; -.
DR   EnsemblFungi; CADANIAT00008139; CADANIAP00008139; CADANIAG00008139.
DR   EnsemblFungi; EAA63826; EAA63826; AN1513.2.
DR   GeneID; 2874711; -.
DR   KEGG; ani:AN1513.2; -.
DR   HOGENOM; HOG000217393; -.
DR   KO; K01738; -.
DR   OMA; GIRRWPE; -.
DR   OrthoDB; EOG092C33M9; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled 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:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5BD67.
DR   SWISS-2DPAGE; Q5BD67.
KW   Complete proteome; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    428       Cysteine synthase 2.
FT                                /FTId=PRO_0000436603.
FT   TRANSMEM      7     27       Helical. {ECO:0000255}.
FT   REGION      260    264       Pyridoxal phosphate binding.
FT                                {ECO:0000250|UniProtKB:P16703}.
FT   BINDING     367    367       Pyridoxal phosphate.
FT                                {ECO:0000250|UniProtKB:P16703}.
FT   MOD_RES     106    106       N6-(pyridoxal phosphate)lysine.
FT                                {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
//

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