ID   CYSD_EMENI     STANDARD;      PRT;   437 AA.
AC   P50125;
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   O-acetylhomoserine (Thiol)-lyase (EC 2.5.1.49) (O-acetylhomoserine
DE   sulfhydrylase) (OAH sulfhydrylase) (Homocysteine synthase).
GN   Name=cysD;
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=JAM 2006;
RX   MEDLINE=98173633; PubMed=9506902;
RA   Sie'nko M., Topczewski J., Paszewski A.;
RT   "Structure and regulation of cysD, the homocysteine synthase gene of
RT   Aspergillus nidulans.";
RL   Curr. Genet. 33:136-144(1998).
CC   -!- FUNCTION: Transforms O-acetylhomoserine into homocysteine.
CC   -!- CATALYTIC ACTIVITY: O-acetyl-L-homoserine + methanethiol = L-
CC       methionine + acetate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U19394; AAA61543.1; -.
DR   HSSP; P13254; 1GC0.
DR   InterPro; IPR000277; Cys_Met_Meta_PP.
DR   InterPro; IPR006235; OAH_OAS_sulfhy.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
KW   Cysteine biosynthesis; Pyridoxal phosphate; Transferase.
FT   BINDING     211    211       Pyridoxal phosphate (By similarity).
SQ   SEQUENCE   437 AA;  47185 MW;  7621E2FC82E09628 CRC64;
     MSDPSPKRFE TLQLHAGQEP DPATNSRAVP IYATTSYTFN DSAHGARLFG LKEFGNIYSR
     IMNPTVDVFE KRIAALEGGV AAVAASSGQA AQFMAISALA HAGDNIVSTS NLYGGTYNQF
     KVLFPRLGIT TKFVQGDKAE DIAAAIDDRT KAVYVETIGN PRYNVPDFEA IAKVAHEKGI
     PLVVDNTFGA GGYFVRPIEH GADIVVHSAT KWIGGHGTTI GGVVVDSGKF EWGKNAARFP
     QFTQPSEGYH GLNFWETFGP IAFAIRVRVE ILRDLGSALN PFAAQQLILG LETLSLRAER
     HASNALALAN WLKKNDHVSW VSYVGLEEHP SHGVAKKYLK RGFGGVLSFG VKGEAAVGSQ
     VVDNFKLISN LANVGDSKTL AIHPWSTTHE QLTDQERIDS GVTEDAIRIS VGTEHIDDII
     ADFEQSFAAT FKVVRGA
//