ID A0A0J8RXS6_COCIT Unreviewed; 411 AA.
AC A0A0J8RXS6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KMU88994.1};
GN ORFNames=CIHG_06795 {ECO:0000313|EMBL:KMU88994.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU88994.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS017009; KMU88994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RXS6; -.
DR STRING; 396776.A0A0J8RXS6; -.
DR VEuPathDB; FungiDB:CIHG_06795; -.
DR eggNOG; KOG1368; Eukaryota.
DR Proteomes; UP000054563; 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:UP000054563}.
FT DOMAIN 66..340
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 252
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 411 AA; 44342 MW; E30B910688D658C6 CRC64;
MTGVLARSVS TPRRPTCSLR KKKLHMISAR MSSRHRREYD AGNYEKKSIP WETQSRASES
PGAIIDATFA DDVFDEGGDP SVTALEQKLV ELTGKEAALW VLSGTMGNQI CLRTHLTQPP
HSVLLDHRAH IYTWESGALP VMSQASVTPV HPANGIHLTL EDVKKNMIPE ENFHFPPTRV
VALENTLNGT VLPLKHAKEI SDYVRSYPVS PGQKRVAMPL DGARVFDAAA GEGIDIKDYC
ACFDSISVCL AKGVGAPIGS VILGSKPFIA RAKWFKKMFG GGTRQPGMMA AAAHAALTNS
IPQLPRVHSL TKSTAARLSA LGYTFSSPVQ TNMILLDLEA AGIPVAAFVD YLTEAGVQVF
PTPRLVFHYQ TAQEAADKLV DGLGLLIQDK KAGKDLVARK MTGGYAKGGS E
//
