ID A0A0D1CID2_USTMA Unreviewed; 670 AA.
AC A0A0D1CID2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN ORFNames=UMAG_04787 {ECO:0000313|EMBL:KIS66723.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS66723.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS66723.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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 CTAG/PCC1 family.
CC {ECO:0000256|ARBA:ARBA00007073}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; CM003156; KIS66723.1; -; Genomic_DNA.
DR RefSeq; XP_011391652.1; XM_011393350.1.
DR AlphaFoldDB; A0A0D1CID2; -.
DR STRING; 237631.A0A0D1CID2; -.
DR EnsemblFungi; KIS66723; KIS66723; UMAG_04787.
DR GeneID; 23564856; -.
DR KEGG; uma:UMAG_04787; -.
DR VEuPathDB; FungiDB:UMAG_04787; -.
DR eggNOG; KOG1368; Eukaryota.
DR InParanoid; A0A0D1CID2; -.
DR OMA; TRSHIHR; -.
DR OrthoDB; 178754at2759; -.
DR Proteomes; UP000000561; Chromosome 17.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IBA:GO_Central.
DR GO; GO:0006545; P:glycine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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; IPR015419; CTAG/Pcc1.
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 Pfam; PF09341; Pcc1; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000561}.
FT DOMAIN 151..434
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 66..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 72108 MW; B96FD0D1E2A0623B CRC64;
MFVCVSILAT STRSVTRSAA HRLPRLVTSL TTPLSGSNVV PLFRFPLRDP PRACFSLTPT
LASAYSGEGA EDDSSIMSTS YPLQPSEPVD PVHGPSKTQK PINVNANGDA NGAYITDAHS
RQQNKTAPLL PADPLKGKID NAKKQQLLAR DFRSDTITAP TESMIRAMAE ASRGDDVYGE
DDTTNSFQAE IAALTGKESA IFVPSGTLSN QLAFRTHLHQ PPHTVLCDTR SHIHRYEAGG
IAFHCGASTE IVAPSNGHHL RWDQDIKPNL NLSDDIHFSP TRIISLENTL NGTIFPQDEI
VKISTEARKL GLIMHLDGAR VWNVAAETGL SLKELCDPFD TVSLCLSKGL GAPIGSILVG
PSQFIKKVRH FRKLYGAGVR QVGPLVAAAR VGVLENYPKL QATHQLARYA GQELEKLGVR
LTAPVETSMV FLDTSSIGIP ISELVSRAAA LPAPIQLGGG RMVVHYQIEK QAIDDLLDLI
RVMKKEKADG TGPANAAAAD SGAGLYSNNM TGGNTASAAT TKTNGSLSHV RSSSSSENRG
LVFQTIGTCS RRPSDEMRHS VSLVLPFPDR QSALTLQQSI SVDKELKPKE VRKEFTILTR
SSSSATVELG VKIFATTVRQ LRLSVNAFLE DASLVCRTMA EFDPLQKGID ELSKMHLEDE
LEQGSVGVAG
//
