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Database: UniProt
Entry: U7PSS7_SPOS1
LinkDB: U7PSS7_SPOS1
Original site: U7PSS7_SPOS1 
ID   U7PSS7_SPOS1            Unreviewed;       384 AA.
AC   U7PSS7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=HMPREF1624_06148 {ECO:0000313|EMBL:ERS97976.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS97976.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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; KI440847; ERS97976.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PSS7; -.
DR   STRING; 1391915.U7PSS7; -.
DR   eggNOG; KOG1368; Eukaryota.
DR   HOGENOM; CLU_029381_1_0_1; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000018087; 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; 3.90.1150.10; 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:UP000018087}.
FT   DOMAIN          19..310
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   384 AA;  41000 MW;  917DDA191CC80AAE CRC64;
     MAAQPETRWV GSAGAGSLDL RSDVMTTPTA NMLAAIQNCT LLDDVFREDT TTIDLEKHCA
     KLAGKEAGLL VLSGTMGNQV ALRTLLKQPP YSVLCDRASH IFKYEAGGVS SLTGAMVHTV
     VPKNGIYLTL EDVQANAVTG TDVHDCTTRV ISLENTINGV LMPLAEVRRI AEWARAHGIK
     MHCDGARLWE AAASGAGSLV DFAACFDTVT LCFSKGLGAP IGSVLLGSAD DIRHATWIRK
     SIGGGLRQAG VIAAPARVAV DETFGTGPNG EGGLLRHTHT LAKEMSKLWT DRGGKLLYPV
     DTNMMWVDLE ASGIGYDDIS KQAEAEGLRM LGNRMVFHYQ IYQNREVVVP KLERIFTKVL
     AGKAAAPGVS ASAGAKSMYQ TQQQ
//
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