ID   A0A165MZP8_EXIGL        Unreviewed;       360 AA.
AC   A0A165MZP8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Pyridoxal phosphate-dependent enzyme, beta subunit {ECO:0000313|EMBL:KZV99992.1};
GN   ORFNames=EXIGLDRAFT_723157 {ECO:0000313|EMBL:KZV99992.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV99992.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV99992.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV99992.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-homocysteine and L-serine: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005003}.
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DR   EMBL; KV425904; KZV99992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165MZP8; -.
DR   STRING; 1314781.A0A165MZP8; -.
DR   InParanoid; A0A165MZP8; -.
DR   OrthoDB; 5487987at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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   PANTHER; PTHR10314:SF194; 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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          15..327
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   360 AA;  37821 MW;  1348BBFCE9DD75E2 CRC64;
     MPPSLAPQVL DTALDAVGNT PLIRLDKIAG AEGLKCNLLG KVEFFSAGGS VKDRIAKRMV
     EEAEKDGTLV PGKSVIIEPT SGNTGIGLAL AGAIKGYPVI ITLPEKMSLE KEATLRALGA
     EVVRTPTAAT WDSEESHIGV AKKLQRNIPH AVILDQYSNP NNPLAHELGT GPEILAAVAT
     LDNSSKTVDV CVAGAGTGGT VTGVSRALKA SNKDCVIVAV DPKGSILAVP DTLNDDARGE
     MYVVEGIGYD FVPEVLDRDK PTVDVWVKMD DSAAFTAAHR LMRLEGLLVG GSSGTALAGA
     LQYLKSEEGW ARFGNVEGKN VVVILPDGLR NYIGKPWFLD ATLRAPATPL ANQISQILRS
//