ID F8NVE6_SERL9 Unreviewed; 301 AA.
AC F8NVE6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN ORFNames=SERLADRAFT_467018 {ECO:0000313|EMBL:EGO26047.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO26047.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO26047.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) 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 threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; GL945433; EGO26047.1; -; Genomic_DNA.
DR RefSeq; XP_007318169.1; XM_007318107.1.
DR AlphaFoldDB; F8NVE6; -.
DR GeneID; 18819163; -.
DR KEGG; sla:SERLADRAFT_467018; -.
DR HOGENOM; CLU_029381_1_1_1; -.
DR OrthoDB; 178754at2759; -.
DR Proteomes; UP000008064; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 2.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
FT DOMAIN 2..112
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT DOMAIN 132..285
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 301 AA; 33173 MW; 2C16EBAB5286CEDF CRC64;
MFSYAIRSSL GDDVYFEPST AALEEHIAQL AGKEAGIFLP TGTMSNQIAL RTLLEQPPYS
VLCDVRSHVY RFEAGGLAFH SGAHSTPVIP SNGHHLTLED IEDHVILSSD VHVWVFYILF
VVLLYLKSFA SAPTRVITLE NTLNGTIIPQ NEIYMISEFA RSKKIKMHLD GARIWHVAAE
TNTSIRELCS PFDSVSLCLS KGLGAPIGTC LVGTKPFIRK ARWFRKLLGA GMRQTGFLAG
AAAYALANNF QLLPRVHALA KHMQQGLEKL GVGILSPAET CMVFYDPDPI GVEYWEVVEP
L
//