CYSD_EMENI
ID CYSD_EMENI Reviewed; 437 AA.
AC P50125; C8V3P9; O13387; Q5ATV3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Homocysteine synthase {ECO:0000303|PubMed:9506902};
DE EC=2.5.1.49 {ECO:0000269|PubMed:6381643, ECO:0000269|Ref.5};
DE AltName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000303|Ref.5};
DE Short=OAH SHL {ECO:0000303|PubMed:8249501};
DE Short=OAH sulfhydrylase {ECO:0000303|Ref.5};
GN Name=cysD {ECO:0000303|PubMed:9506902}; ORFNames=AN8277;
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 / MRNA], AND INDUCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139, and JAM 2006;
RX PubMed=9506902; DOI=10.1007/s002940050319;
RA Sienko 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).
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, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=6381643; DOI=10.1099/00221287-130-5-1113;
RA Paszewski A., Prazmo W., Nadolska J., Regulski M.;
RT "Mutations affecting the sulphur assimilation pathway in Aspergillus
RT nidulans: their effect on sulphur amino acid metabolism.";
RL J. Gen. Microbiol. 130:1113-1121(1984).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX DOI=10.2323/jgam.36.137;
RA Yamagata S., Paszewski A., Lewandowska I.;
RT "Purification and properties of O-acetyl-L-homoserine O-sulfhydrylase from
RT Aspergillus nidulans.";
RL J. Gen. Appl. Microbiol. 36:137-141(1990).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8249501;
RA Brzywczy J., Yamagata S., Paszewski A.;
RT "Comparative studies on O-acetylhomoserine sulfhydrylase: physiological
RT role and characterization of the Aspergillus nidulans enzyme.";
RL Acta Biochim. Pol. 40:421-428(1993).
RN [7]
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-acetyl-L-homoserine (OAH) into
CC homocysteine in the methionine biosynthesis pathway (PubMed:6381643,
CC Ref.5). Has also cysteine synthase (O-acetylserine sulfhydrylase)
CC activity in vitro, but seems only be involved in the alternative
CC pathway of methionine biosynthesis in E.nidulans (PubMed:17482430,
CC PubMed:6381643, PubMed:8249501). {ECO:0000269|PubMed:6381643,
CC ECO:0000269|Ref.5, ECO:0000305|PubMed:17482430,
CC ECO:0000305|PubMed:6381643, ECO:0000305|PubMed:8249501}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-
CC methionine; Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16007, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716,
CC ChEBI:CHEBI:57844; EC=2.5.1.49; Evidence={ECO:0000269|PubMed:6381643,
CC ECO:0000269|Ref.5};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.5};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from O-acetyl-L-homoserine.
CC {ECO:0000305|PubMed:6381643}.
CC -!- SUBUNIT: Oligomer, probably homohexamer. {ECO:0000269|PubMed:8249501,
CC ECO:0000269|Ref.5}.
CC -!- INDUCTION: Up-regulated under sulfur limitation and down-regulated by
CC high methionine concentrations. {ECO:0000269|PubMed:9506902}.
CC -!- MISCELLANEOUS: E.nidulans has another enzyme having cysteine synthase
CC (O-acetylserine sulfhydrylase) activity (cysB) that has been shown to
CC be the enzyme of physiological importance in cysteine biosynthesis.
CC {ECO:0000269|PubMed:17482430, ECO:0000305|PubMed:6381643}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; U19394; AAA61543.1; -; Genomic_DNA.
DR EMBL; AF029318; AAB84201.1; -; mRNA.
DR EMBL; AACD01000145; EAA59015.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF74263.1; -; Genomic_DNA.
DR PIR; T45481; T45481.
DR RefSeq; XP_681546.1; XM_676454.1.
DR AlphaFoldDB; P50125; -.
DR SMR; P50125; -.
DR STRING; 162425.CADANIAP00004337; -.
DR PRIDE; P50125; -.
DR EnsemblFungi; CBF74263; CBF74263; ANIA_08277.
DR EnsemblFungi; EAA59015; EAA59015; AN8277.2.
DR GeneID; 2869162; -.
DR KEGG; ani:AN8277.2; -.
DR VEuPathDB; FungiDB:AN8277; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_4_0_1; -.
DR InParanoid; P50125; -.
DR OMA; TYTLFAH; -.
DR OrthoDB; 572061at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:GOC.
DR GO; GO:0006534; P:cysteine metabolic process; IMP:AspGD.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Methionine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..437
FT /note="Homocysteine synthase"
FT /id="PRO_0000114777"
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
FT VARIANT 170
FT /note="V -> A (in strain: JAM 2006)"
FT VARIANT 231
FT /note="D -> E (in strain: JAM 2006)"
FT VARIANT 330
FT /note="S -> P (in strain: JAM 2006)"
FT VARIANT 333
FT /note="E -> G (in strain: JAM 2006)"
FT VARIANT 436
FT /note="S -> G (in strain: JAM 2006)"
SQ SEQUENCE 437 AA; 47291 MW; 5EC85F12B8E21E28 CRC64;
MSDPSPKRFE TLQLHAGQEP DPATNSRAVP IYATTSYTFN DSAHGARLFG LKEFGNIYSR
IMNPTVDVFE KRIAALEGGV AAVAASSGQA AQFMAISALA HAGDNIVSTS NLYGGTYNQF
KVLFPRLGIT TKFVQGDKAE DIAAAIDDRT KAVYVETIGN PRYNVPDFEV IAKVAHEKGI
PLVVDNTFGA GGYFVRPIEH GADIVVHSAT KWIGGHGTTI GGVVVDSGKF DWGKNAARFP
QFTQPSEGYH GLNFWETFGP IAFAIRVRVE ILRDLGSALN PFAAQQLILG LETLSLRAER
HASNALALAN WLKKNDHVSW VSYVGLEEHS SHEVAKKYLK RGFGGVLSFG VKGEAAVGSQ
VVDNFKLISN LANVGDSKTL AIHPWSTTHE QLTDQERIDS GVTEDAIRIS VGTEHIDDII
ADFEQSFAAT FKVVRSA
