ID A0A167FD59_9HYPO Unreviewed; 339 AA.
AC A0A167FD59;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=L-serine ammonia-lyase {ECO:0000256|ARBA:ARBA00012093};
DE EC=4.3.1.17 {ECO:0000256|ARBA:ARBA00012093};
GN ORFNames=BBO_03683 {ECO:0000313|EMBL:OAA45105.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA45105.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA45105.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA45105.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA45105.1}.
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DR EMBL; AZHA01000009; OAA45105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167FD59; -.
DR OrthoDB; 8406at2759; -.
DR Proteomes; UP000076863; 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 CDD; cd06448; L-Ser-dehyd; 1.
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;
FT DOMAIN 13..315
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 339 AA; 35732 MW; 487FD2CFC4B82ECF CRC64;
MGSLGGESTL PWVKTPCVYS TAVSRAVGCN IYLKLDNLQP SGSFKSRGIG NLMTRAVAHH
PGNVHFYCAS GGNAGLACAT SALALDRPCT VVVPLTTSEF MRNKLVALGA HVQQYGKNLF
AAEQYVKQEL VAHDPDGVFV PPFDHPDIWD GAASLIPELR DQMDVPMDAI VCSVGGGGLF
NGLMQGIETF PWSGNKPHVV GVETAGADSL NASLAANEHL TLAEITSIAV SLGCSRVSAQ
TWKWAHYPNT HSMVVSDADA AMACVRFADD ARLLVEVSCG AALAAAYRGD LRASLGKGLS
DAEWAQKNVV LIVCGGSGVS LQLLDRYVQE YGPQSAIKV
//
