ID Q6BTC6_DEBHA Unreviewed; 340 AA.
AC Q6BTC6;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=L-serine ammonia-lyase {ECO:0000256|ARBA:ARBA00012093};
DE EC=4.3.1.17 {ECO:0000256|ARBA:ARBA00012093};
GN OrderedLocusNames=DEHA2D01738g {ECO:0000313|EMBL:CAG86676.2};
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; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG86676.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG86676.2, 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CR382136; CAG86676.2; -; Genomic_DNA.
DR RefSeq; XP_458544.2; XM_458544.1.
DR AlphaFoldDB; Q6BTC6; -.
DR STRING; 284592.Q6BTC6; -.
DR GeneID; 2901220; -.
DR KEGG; dha:DEHA2D01738g; -.
DR VEuPathDB; FungiDB:DEHA2D01738g; -.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_3_1_1; -.
DR InParanoid; Q6BTC6; -.
DR OMA; CIEAAIG; -.
DR OrthoDB; 8406at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR48078:SF2; CATABOLIC L-SERINE_THREONINE DEHYDRATASE; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT DOMAIN 22..322
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 340 AA; 36798 MW; C98A23292377586D CRC64;
MISQLAKGEP SIDTSLIEVT DKLPNKPPCR IFIKNEYEQP SGSFKLRGMG HLVAKSIERA
HELKKENVET FASSGGNAGL AAAYTSRHYN LSCTVVLPTT AHSGVVEKLE KLGAKVQVHG
AHWGEADSYL REIVMKSVDA SVYPVYCPPF DDPLLWEGHG TIIDEIVNQN QLSPEECGKV
RGIVCSVGGG GLYNGVVAGL SRNAQFKDVP ILAVETFQTP TFSEALKAGK VVTLKSINTL
VSCLASPYIS AQSLANYNKH RTHVQMIDDL EAVKGSIDFY DHFGTLVEPA CGATISMAFD
NTSYLKCFGN LSDEEIIIFI GCGGAAISVD SLNEYRKLFT
//
