ID G2R806_THETT Unreviewed; 547 AA. AC G2R806; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 24-JAN-2024, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEO68065.1}; GN ORFNames=THITE_2117395 {ECO:0000313|EMBL:AEO68065.1}; OS Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia OS terrestris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides; OC Thermothielavioides terrestris. OX NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO68065.1, ECO:0000313|Proteomes:UP000008181}; RN [1] {ECO:0000313|EMBL:AEO68065.1, ECO:0000313|Proteomes:UP000008181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181}; RX PubMed=21964414; DOI=10.1038/nbt.1976; RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I., RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M., RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P., RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P., RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J., RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S., RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W., RA Tsang A.; RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi RT Myceliophthora thermophila and Thielavia terrestris."; RL Nat. Biotechnol. 29:922-927(2011). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382}; CC -!- SIMILARITY: Belongs to the group II decarboxylase family. CC {ECO:0000256|RuleBase:RU000382}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003011; AEO68065.1; -; Genomic_DNA. DR RefSeq; XP_003654401.1; XM_003654353.1. DR AlphaFoldDB; G2R806; -. DR STRING; 578455.G2R806; -. DR GeneID; 11516424; -. DR KEGG; ttt:THITE_2117395; -. DR eggNOG; KOG0629; Eukaryota. DR HOGENOM; CLU_011856_0_0_1; -. DR OrthoDB; 888358at2759; -. DR Proteomes; UP000008181; Chromosome 3. DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR Gene3D; 3.90.1150.170; -; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR002129; PyrdxlP-dep_de-COase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1. DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1. DR Pfam; PF00282; Pyridoxal_deC; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50, KW ECO:0000256|RuleBase:RU000382}; KW Reference proteome {ECO:0000313|Proteomes:UP000008181}. FT REGION 359..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 359..386 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 324 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 547 AA; 57984 MW; E01A0DD70A19DE35 CRC64; MNGVHDGQPL NRADEVEHLI DAVKALILPF IRAADEAVPS RAAGELLPNK EGVVQNALVN ARKPEDLVRE LSLCLPEGPG LGEDGLLRAI GDILKYSVNT WDQGFMDKLY ASTNPVGVVS ELLLGVLNTN VHVYQVSPAL TVIEKHTAQK LARLFGFTGP RAGGITCQGG SSSNLTSIVI ARNTLYPESK TRGNQCATGS FILFTSEHGH YSVEKAAVTC GLGSSSVWTV PVDDAGRMDP SALRRLVQRA RAEGNTPLYV NATAGTTVLG SYDPIEAVAA VCREFGLWLH VDASWGGPAI FSPRHRHKLA GAHLANSLTV NPHKMLNVPV TCSFLLGPDT AVFHRANTLP AGYLFHSTAS SAPNPPQPAT TITTTTTPTT ATPPTPAENG EEDGPPEEEV WDLADLTLQC GRRADSLKLF LAWTYHGAGG FAAQVDRGFA AAARLAELVA AHPDLAPVSP SPPPCLQVCF YYAPRGELAA DPAENTRRTR AVVHALVGRG FMVDYAPGKR GAFLRVVVNS LTLRGTVEGL VKAVAAVGRE VVGGFLN //