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Database: UniProt
Entry: A0A0F8XGQ3_9EURO
LinkDB: A0A0F8XGQ3_9EURO
Original site: A0A0F8XGQ3_9EURO 
ID   A0A0F8XGQ3_9EURO        Unreviewed;       413 AA.
AC   A0A0F8XGQ3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=ARAM_006563 {ECO:0000313|EMBL:KKK22747.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK22747.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK22747.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK22747.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) 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}.
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:KKK22747.1}.
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DR   EMBL; JZBS01001442; KKK22747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8XGQ3; -.
DR   STRING; 308745.A0A0F8XGQ3; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_like; 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; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          58..350
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         254
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   413 AA;  44799 MW;  1557B304AF8D5459 CRC64;
     MKHIVGPLFR PRTFLRPTSS LPRSRLGPRL AMASTMTSPN GANGKPSTWQ GAGAAEFDLR
     SDTMTKPTPS MLEAICQTTL LDDVFEEDPV TNDLQSYVAQ RTNHEASLLV MSGTMGNQVA
     IRTHLVEPPY SIVCDYRAHI ICYEAGGVSM WTGATVIPVM PKNGSYLTLE EIKKHTVLSD
     DVHACPTKLI SLENTLGGAI MPLEETRKIS EWAHQNGIKV HLDGARLWEA VAAGAGSLTD
     FTSLFDSVSL CFSKGLGAPI GSIVIGSKAF IKKARWFRKS IGGGTRQAGV IAAAARVALD
     ETFGTDPYGQ QGKLRETHSK ANRIAEMWTS RGGKLDFAVE TNMVWLDVEA AGLGPNDLSE
     IGSEKGLKLL GNRIVVHYQV SEEALNRLEQ VFDVAMKGQY QRSADTSKAY GSR
//
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