CYSD_KLULA
ID CYSD_KLULA Reviewed; 444 AA.
AC Q92441;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Homocysteine/cysteine synthase;
DE EC=2.5.1.47;
DE EC=2.5.1.49;
DE AltName: Full=O-acetylserine/O-acetylhomoserine sulfhydrylase;
DE Short=OAS-OAH SHLase;
DE Short=OAS-OAH sulfhydrylase;
GN Name=MET17; OrderedLocusNames=KLLA0D04037g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WM27 / NRRL Y-17066;
RX PubMed=10509022;
RX DOI=10.1002/(sici)1097-0061(19990930)15:13<1403::aid-yea467>3.0.co;2-5;
RA Brzywczy J., Paszewski A.;
RT "Cloning and characterization of the Kluyveromyces lactis homocysteine
RT synthase gene.";
RL Yeast 15:1403-1409(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into
CC homocysteine in the methionine biosynthesis pathway. Also catalyzes the
CC conversion of O-acetylserine (OAS) into cysteine, the last step in the
CC cysteine biosynthesis pathway. {ECO:0000250|UniProtKB:P06106}.
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:0000250|UniProtKB:P06106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000250|UniProtKB:P06106};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P06106};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from O-acetyl-L-homoserine.
CC {ECO:0000250|UniProtKB:P06106}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P06106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06106}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; U72486; AAB17387.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00339.1; -; Genomic_DNA.
DR RefSeq; XP_453243.1; XM_453243.1.
DR AlphaFoldDB; Q92441; -.
DR SMR; Q92441; -.
DR STRING; 28985.XP_453243.1; -.
DR EnsemblFungi; CAH00339; CAH00339; KLLA0_D04037g.
DR GeneID; 2892931; -.
DR KEGG; kla:KLLA0_D04037g; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_4_0_1; -.
DR InParanoid; Q92441; -.
DR OMA; TYTLFAH; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
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: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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Multifunctional enzyme; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06106"
FT CHAIN 2..444
FT /note="Homocysteine/cysteine synthase"
FT /id="PRO_0000114775"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
SQ SEQUENCE 444 AA; 48106 MW; C1183F66411BF79A CRC64;
MPSHFDTLQL HAGQEKTADA HNPRAVPIYA TTSYVFNDSK HGAQLFGLET PGYIYSRIMN
PTLDVLEKRL AALEGGIAAL ATSSGQAAQT LAVTGLAHTG DNIVSTSFLY GGTYNQFKVA
FKRLGIEARF VDGDKPEDFE KLFDEKTKAL YLESIGNPKY NVPDFEKIVA VAHKHGIPVV
VDNTFGAGGF FCQPIKYGAD IVTHSATKWI GGHGVTVGGV IIDSGKFPWK DYPEKFPQFS
QPSEGYHGLI FNDAFGPAAF IGHVRTELLR DLGPVLSPFA GFLLLQGLET LSLRGERHGS
NALKLAQYLE SSPYVSWVSY PGLPSHSHHE NAKKYLENGF GGVLSFGVKD LPNASEESDP
FKASGAQVVD NLKLASNLAN VGDSKTLVIA PYFTTHQQLT DEEKLASGVT KDLIRVSVGT
EFIDDIIADF EASFATVFNG QKPE
