ID   CYSK_EMENI     STANDARD;      PRT;   371 AA.
AC   P50867;
DT   01-OCT-1996 (Rel. 34, Created)
DT   01-OCT-1996 (Rel. 34, Last sequence update)
DT   25-JAN-2005 (Rel. 46, Last annotation update)
DE   Cysteine synthase (EC 2.5.1.47) (O-acetylserine sulfhydrylase) (O-
DE   acetylserine (Thiol)-lyase) (CSase).
GN   Name=cysB;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ANA1 BIA1 PHENA2;
RX   MEDLINE=97263786; PubMed=9108143;
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).
CC   -!- CATALYTIC ACTIVITY: O(3)-acetyl-L-serine + H(2)S = L-cysteine +
CC       acetate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Cysteine biosynthesis.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family.
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DR   EMBL; U19395; AAC06128.1; -.
DR   HSSP; Q9WZD3; 1J6N.
DR   InterPro; IPR001926; B6_enzyme_beta.
DR   InterPro; IPR001216; Cys_synthase_BS.
DR   Pfam; PF00291; PALP; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
KW   Cysteine biosynthesis; Pyridoxal phosphate; Transferase.
FT   BINDING      74     74       Pyridoxal phosphate (By similarity).
SQ   SEQUENCE   371 AA;  39935 MW;  AC94E929AD9A6FD5 CRC64;
     MFRQSVRRFA TAALRSAAES PYNVRVSQAQ GFVNGLTEKA IGNTPLIRLK RLSEETGSNI
     LAKAEFQNPG GSVKDRAALY VVKDAEERGL LKPGGTVVEG TAGNTGIGLA HVCRSKGYKL
     VIYMPNTQSQ GKIDLLRLLG AEVYPVPAVA FDNPENYNHK ARRHAESLDN AVWTNQFDNT
     ANRRAHIETT GPEIWAQTGG KLDAFTCSTG TGGTLAGITY YLKQASGGRV KSFLADPPGS
     VLHSYIQSGG KLVERSGSSI TEGIGQGRIT DNLQPDVGTL DGSLNISDEK TIEMIYRCLD
     EEGLYLGASS ALNVVAAKEV AEKLGKGSTV VTILADGAYR YADRLFSKSW LESKGLRNAI
     PKHLEKYIVL P
//