ID A5DNQ5_PICGU Unreviewed; 319 AA.
AC A5DNQ5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=L-serine ammonia-lyase {ECO:0000256|ARBA:ARBA00012093};
DE EC=4.3.1.17 {ECO:0000256|ARBA:ARBA00012093};
GN ORFNames=PGUG_04906 {ECO:0000313|EMBL:EDK40808.2};
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:EDK40808.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK40808.2, 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; EDK40808.2; -; Genomic_DNA.
DR RefSeq; XP_001482951.1; XM_001482901.1.
DR AlphaFoldDB; A5DNQ5; -.
DR STRING; 294746.A5DNQ5; -.
DR GeneID; 5124934; -.
DR KEGG; pgu:PGUG_04906; -.
DR VEuPathDB; FungiDB:PGUG_04906; -.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_3_1_1; -.
DR InParanoid; A5DNQ5; -.
DR OMA; KCTIFLP; -.
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 8..311
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 319 AA; 34111 MW; 85AAF1FD39F727BE CRC64;
MARVSVTTTL VEVTDQLDDT PCRVFFKNEL EQPSGSFKLR GIGHLISKQL AQKEPGKTKV
HVYSSSGGNA GLAAAYASRE LGVPCTVVLP KWSSAVVGNL EKLGATVIMF GEHWGIADDH
LRNVIMKSAP SDVQTVYVHP FDNPVIWDGH ATLVDEIKSQ LRPNDAKAIK GVVCSVGGGG
LYNGVVEGLK RNKMDETSVL AIETFQTPTF SSAVEEGKVV NLPTIKTTTT SLASPYLSQQ
SLENYREGKT VVKMVDDSEA KSAAEKYHKL FGKKVEASCG AALTAVLDSK VFLKDLGNLT
KDDIVVVVVC GGIVGLGMD
//
