CYSD_SCHPO
ID CYSD_SCHPO Reviewed; 429 AA.
AC O13326;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Homocysteine synthase {ECO:0000303|PubMed:11754480};
DE EC=2.5.1.49 {ECO:0000269|PubMed:11754480, ECO:0000269|PubMed:6526818};
DE AltName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000303|PubMed:11754480, ECO:0000303|PubMed:6526818};
DE Short=OAH SHL {ECO:0000303|PubMed:11754480};
DE Short=OAH sulfhydrylase {ECO:0000303|PubMed:6526818};
GN Name=met17 {ECO:0000250|UniProtKB:P06106};
GN Synonyms=cys2 {ECO:0000303|PubMed:17482430};
GN ORFNames=SPBC428.11 {ECO:0000312|PomBase:SPBC428.11};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=11754480; DOI=10.1002/yea.798;
RA Brzywczy J., Sienko M., Kucharska A., Paszewski A.;
RT "Sulphur amino acid synthesis in Schizosaccharomyces pombe represents a
RT specific variant of sulphur metabolism in fungi.";
RL Yeast 19:29-35(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RX PubMed=6526818; DOI=10.1093/oxfordjournals.jbchem.a134980;
RA Yamagata S.;
RT "O-acetylhomoserine sulfhydrylase of the fission yeast Schizosaccharomyces
RT pombe: partial purification, characterization, and its probable role in
RT homocysteine biosynthesis.";
RL J. Biochem. 96:1511-1523(1984).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP MUTAGENESIS OF GLY-411.
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:11754480,
CC PubMed:6526818). Can also use O-succinyl-L-homoserine and L-homoserine
CC as substrates (PubMed:6526818). Has also cysteine synthase (O-
CC acetylserine sulfhydrylase) activity in vitro, but in S.pombe, it seems
CC only to be involved in the alternative pathway of methionine
CC biosynthesis under cysteine deficiency conditions (PubMed:11754480).
CC {ECO:0000269|PubMed:11754480, ECO:0000269|PubMed:6526818,
CC ECO:0000305|PubMed:11754480}.
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;
CC Evidence={ECO:0000269|PubMed:11754480, ECO:0000269|PubMed:6526818};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:6526818};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.5 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:6526818};
CC KM=11.1 mM for O-succinyl-L-homoserine {ECO:0000269|PubMed:6526818};
CC KM=10.4 mM for L-homoserine {ECO:0000269|PubMed:6526818};
CC KM=0.053 mM for H(2)S {ECO:0000269|PubMed:6526818};
CC Vmax=15.5 umol/min/mg enzyme for O-acetyl-L-homoserine
CC {ECO:0000269|PubMed:6526818};
CC Vmax=6.2 umol/min/mg enzyme for O-succinyl-L-homoserinee
CC {ECO:0000269|PubMed:6526818};
CC Vmax=2.5 umol/min/mg enzyme for L-homoserine
CC {ECO:0000269|PubMed:6526818};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:6526818};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from O-acetyl-L-homoserine.
CC {ECO:0000305|PubMed:11754480}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:6526818}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Repressed by cysteine. {ECO:0000269|PubMed:11754480}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AF012876; AAB66879.1; -; mRNA.
DR EMBL; CU329671; CAA22286.1; -; Genomic_DNA.
DR PIR; T40463; T40463.
DR RefSeq; NP_595189.1; NM_001021096.2.
DR AlphaFoldDB; O13326; -.
DR SMR; O13326; -.
DR BioGRID; 277366; 9.
DR STRING; 4896.SPBC428.11.1; -.
DR iPTMnet; O13326; -.
DR MaxQB; O13326; -.
DR PaxDb; O13326; -.
DR PRIDE; O13326; -.
DR EnsemblFungi; SPBC428.11.1; SPBC428.11.1:pep; SPBC428.11.
DR GeneID; 2540849; -.
DR KEGG; spo:SPBC428.11; -.
DR PomBase; SPBC428.11; met17.
DR VEuPathDB; FungiDB:SPBC428.11; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_4_0_1; -.
DR InParanoid; O13326; -.
DR OMA; TYTLFAH; -.
DR PhylomeDB; O13326; -.
DR PRO; PR:O13326; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004124; F:cysteine synthase activity; IMP:PomBase.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IDA:PomBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IMP:PomBase.
DR GO; GO:0071269; P:L-homocysteine biosynthetic process; IDA:PomBase.
DR GO; GO:0006555; P:methionine metabolic process; NAS:PomBase.
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; Cytoplasm; Methionine biosynthesis; Nucleus;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..429
FT /note="Homocysteine synthase"
FT /id="PRO_0000114778"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
FT MUTAGEN 411
FT /note="G->D: In cys2-1: Impairs homocysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:17482430"
SQ SEQUENCE 429 AA; 46409 MW; 18C717E55087B223 CRC64;
MPVESEHFET LQLHAGQEPD AATSSRAVPI YATTSYVFRD CDHGGRLFGL QEPGYIYSRM
MNPTADVFEK RIAALEHGAA AIATSSGTSA LFMALTTLAK AGDNIVSTSY LYGGTYNLFK
VTLPRLGITT KFVNGDDPND LAAQIDENTK AVYVESIGNP MYNVPDFERI AEVAHAAGVP
LMVDNTFGGG GYLVRPIDHG ADIVTHSATK WIGGHGTTIG GVIVDSGKFD WKKNSKRFPE
FNEPHPGYHG MVFTETFGNL AYAFACRTQT LRDVGGNANP FGVFLLLQGL ETLSLRMERH
VQNAFALAKY LEKHPKVNWV SYPGLESHVS HKLAKKYLKN GYGAVLSFGA KGGPDQSRKV
VNALKLASQL ANVGDAKTLV IAPAYTTHLQ LTDEEQISAG VTKDLIRVAV GIEHIDDIIA
DFAQALEVA
