ID   A3LRL7_PICST            Unreviewed;       392 AA.
AC   A3LRL7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
DE   AltName: Full=Cysteine synthase-like protein {ECO:0000256|ARBA:ARBA00078545};
GN   Name=CYK2 {ECO:0000313|EMBL:ABN65759.2};
GN   ORFNames=PICST_30734 {ECO:0000313|EMBL:ABN65759.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65759.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN65759.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate;
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:0000256|ARBA:ARBA00047931};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004572}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR   EMBL; CP000497; ABN65759.2; -; Genomic_DNA.
DR   RefSeq; XP_001383788.2; XM_001383751.1.
DR   AlphaFoldDB; A3LRL7; -.
DR   FunCoup; A3LRL7; 247.
DR   STRING; 322104.A3LRL7; -.
DR   GeneID; 4837877; -.
DR   KEGG; pic:PICST_30734; -.
DR   eggNOG; KOG1481; Eukaryota.
DR   HOGENOM; CLU_021018_1_0_1; -.
DR   InParanoid; A3LRL7; -.
DR   OMA; WMADYGF; -.
DR   OrthoDB; 10259545at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd01561; CBS_like; 1.
DR   FunFam; 3.40.50.1100:FF:000096; Related to cysteine synthase; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR050214; Cys_Synth/Cystath_Beta-Synth.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ABN65759.2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..392
FT                   /note="cysteine synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002654986"
FT   DOMAIN          50..365
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   392 AA;  42951 MW;  540D08FAF634CD06 CRC64;
     MSFNWKIILQ SSASIVSALI ILRELHRQLS QSNNSSTKLT SLPPRSRGVE SLIGNTPLIE
     IKSLSKLTGC KIYAKLELAN PAGSAKDRVA LAIIRANEKL GHLRPHSGDV IFEGTSGSTG
     ISFAVLANAL GYDAHICLPD DTSPEKLQLL KSLGATIHPV KPASIVDPQQ YTNAARCGSQ
     QINEDPNDRR RAIFADQFEN DFNWRIHYET TGPEIWRQME QDVDVFINGS GTGGTIAGVS
     KYLHEQNREI KIILADPQGS GLANRVNYGV MYDTVEKEGT RRRHQVDTLV EGIGLNRLTW
     NFKQAEAHIT EAIRVSDNQA LRMAKFLCIN DGLFWGSSAA INCVAAVKTA LKNGPGQKIV
     VIACDSGARH LSKFWKSAAE VPNDITLDEV LQ
//