ID A5DNW5_PICGU Unreviewed; 355 AA.
AC A5DNW5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=L-serine ammonia-lyase {ECO:0000256|ARBA:ARBA00012093};
DE EC=4.3.1.17 {ECO:0000256|ARBA:ARBA00012093};
GN ORFNames=PGUG_04966 {ECO:0000313|EMBL:EDK40868.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40868.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK40868.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CH408160; EDK40868.2; -; Genomic_DNA.
DR RefSeq; XP_001483011.1; XM_001482961.1.
DR AlphaFoldDB; A5DNW5; -.
DR STRING; 294746.A5DNW5; -.
DR GeneID; 5125050; -.
DR KEGG; pgu:PGUG_04966; -.
DR VEuPathDB; FungiDB:PGUG_04966; -.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_3_1_1; -.
DR InParanoid; A5DNW5; -.
DR OMA; AEQGCEH; -.
DR OrthoDB; 8406at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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:UP000001997}.
FT DOMAIN 31..332
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 355 AA; 38753 MW; 654D1C6DE875680F CRC64;
MSLEPQNFSS SQPLSQPFVK SSLVEVTDTL AVKPPCRIFF KNEYEQPSGS FKLRGIGNLV
SKSYKEAKTK FPHKEIHVYA SSGGNAGLAA AYAARYYKVN CTVVLPVVSK PEVIEKLKTY
GAKTVIHGAN IYEADQYLQG ILRNVNVSKY HPIYCHPFEN PLIWDGHSTL VDEIFQSQLP
EQDKPKVKGF VCSVGGGGLY NGIHKGIIRN KSSSDVFLVE TNQAPTLHET IKAGKVITLK
SVNSLATSLA CSSLSIQSLA NYNDQSKVKT HIASIDDLEA VKGSVNFYRN YGIAVEPACG
ASLSVLYNQL PFLTSKFPNL GSDDIIVVVV CGGSCTNVEG IKKFETLVER QAHKL
//
