ID   B5RT41_DEBHA            Unreviewed;       393 AA.
AC   B5RT41;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   04-NOV-2026, entry version 81.
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   OrderedLocusNames=DEHA2B04004g {ECO:0000313|EMBL:CAR65446.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR65446.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAR65446.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
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., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382134; CAR65446.1; -; Genomic_DNA.
DR   RefSeq; XP_002770076.1; XM_002770030.1.
DR   AlphaFoldDB; B5RT41; -.
DR   FunCoup; B5RT41; 245.
DR   STRING; 284592.B5RT41; -.
DR   GeneID; 8998177; -.
DR   KEGG; dha:DEHA2B04004g; -.
DR   VEuPathDB; FungiDB:DEHA2B04004g; -.
DR   eggNOG; KOG1481; Eukaryota.
DR   HOGENOM; CLU_021018_1_0_1; -.
DR   InParanoid; B5RT41; -.
DR   OMA; AAFFMIE; -.
DR   OrthoDB; 10259545at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
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   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:UP000000599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          46..361
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   393 AA;  43370 MW;  FDB19566F2DDDDCB CRC64;
     MINWKLILRS SAAIVSALII LQRIHEQLNN NKKRLTTLSP RSRGVESLIG NTPMIEIKSL
     SKLTGCKIYA KLELMNPAGS AKDRVALSII RANEKLGKLK PNHGDVIFEG TSGSTGISFA
     VLANALGYKA HICLPDDTSP EKMQLLKSLG AELEPVKPAS IVDPNQYTNA ARYGAQKINE
     DSSNNKNAIF ADQFENDFNW RIHYSSTGPE IWEQMEENLD VFINGSGTGG TIAGVSKYLK
     EKNDRIKIVL ADPQGSGLAN RVNYGVMYDS VEREGTRRRH QVDTLVEGIG LNRLTWNFQQ
     GEHNIDEAIR VRDEQALKMA KFLCINDGLF WGSSSAINCV AAVKTAFKYG PGQKIVIIAC
     DSGARHLSKF WKDAAELPND ITLQDIIEDI KSP
//