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Database: UniProt
Entry: L2G106_COLFN
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Original site: L2G106_COLFN 
ID   L2G106_COLFN            Unreviewed;       911 AA.
AC   L2G106;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Tryptophanase {ECO:0000313|EMBL:ELA32282.1};
GN   Name=tnaA {ECO:0000313|EMBL:KAF4479466.1};
GN   ORFNames=CGGC5_7658 {ECO:0000313|EMBL:ELA32282.1}, CGGC5_v012017
GN   {ECO:0000313|EMBL:KAF4479466.1};
OS   Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS   (Colletotrichum gloeosporioides (strain Nara gc5)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA32282.1};
RN   [1] {ECO:0000313|EMBL:ELA32282.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA32282.1};
RA   Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   fructicola.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF4479466.1, ECO:0000313|Proteomes:UP000011096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4479466.1,
RC   ECO:0000313|Proteomes:UP000011096};
RA   Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF4479466.1, ECO:0000313|Proteomes:UP000011096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4479466.1,
RC   ECO:0000313|Proteomes:UP000011096};
RA   Gan P., Shirasu K.;
RT   "Genome sequencing and assembly of multiple isolates from the
RT   Colletotrichum gloeosporioides species complex.";
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000256|ARBA:ARBA00009721}.
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DR   EMBL; KB020713; ELA32282.1; -; Genomic_DNA.
DR   EMBL; ANPB02000007; KAF4479466.1; -; Genomic_DNA.
DR   RefSeq; XP_007278693.1; XM_007278631.1.
DR   AlphaFoldDB; L2G106; -.
DR   STRING; 1213859.L2G106; -.
DR   EnsemblFungi; ELA32282; ELA32282; CGGC5_7658.
DR   HOGENOM; CLU_319817_0_0_1; -.
DR   InParanoid; L2G106; -.
DR   OrthoDB; 2251964at2759; -.
DR   Proteomes; UP000011096; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd13930; PT-Tnase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR32325; BETA-ELIMINATING LYASE-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32325:SF4; TRYPTOPHANASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   SFLD; SFLDG01162; I; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011096};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          47..497
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   911 AA;  100087 MW;  AA25EF63A8984CA9 CRC64;
     MSPLIVPSHN TLVVRPHIAI TPEEREEVLR SVEYNVFAFP AAILTCDYLS DSGTSAMTDV
     QWAAMLRGDE SYGRNSGYYC LLEAFRDVFE RGEDRRSVFK DVLAGTADST FYREVFLKEI
     FGGFVNGGPL QLIRPNFFIL PQGRCAEGLL FSTLSDILCN IDTDPRNVSN PPALISNGFF
     DTTGANATAA GFQLHTFTQP GLTDPFPVEQ VGVTNPFKGN LDIEKASAFL GAGGNASRVA
     MLLLTITNKW AGAQPVSMGN IKAAAELAKR HSLPLFFDAC RFAENAKFIQ VFEAGYQDRS
     IPQIVQEMFA YADGFTISLK KDGLANMGGA LCFRDQGIFP TKFGADIGIR LKERQIMCYG
     NDSYGGMSGR DVMAAAVGLY EGTKETYLAD RIGQVKKFAE GLAAKGVPVL LPPGGHAIYL
     DMDGFFADCG RSYGEFASVG FTLELLKDYG IRACEAGPFG WEWDKKESIT QDRDNIPNLV
     RFAVPRYVMS DRHIEYTIAA VSQLHQRRHS IPGVRITRGK ELRMRVFQSG LQPVPILSGL
     SSPADVGTFK SEAWHDIQKL CDALHLDDQA LKMFHHAFDV SMQGWGHLPA SEPPFGWKSD
     ASLNLCPFEY SVAIEKTTGK AQLRFLIENQ ADEATLEAHQ RSALQLNNEI QRIYPNAVSL
     DRFNHIKDTF FPSGAEAQGT FAGWHSFVAE EGPRPGWKIY LNANAQGESR APAIFHEALN
     KLCMPQAWAP LEKVLLPGNK LMYLSLDLCP GSQARVKIYV QHCGATAADI SQAASIVAPD
     IVGASDPEIL HFCTVLSGGS EGPYEGKGPM TCFSFTADGE DVKSEVAVYF PVHDYANDDA
     DIRNRIETYL GSADEKAVKT YQRALDAVAH RPLQNGRGIH AWVGLKMTRS RGSVVTFYLA
     SEMFGVLPKR L
//
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