ID   TOXG_COCCA              Reviewed;         389 AA.
AC   Q9UW18;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Alanine racemase TOXG;
DE            EC=5.1.1.1;
GN   Name=TOXG;
OS   Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5017 {ECO:0000312|EMBL:AAD47837.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 90305 / SB111 / 2R15;
RX   PubMed=10671527; DOI=10.1074/jbc.275.7.4906;
RA   Cheng Y.-Q., Walton J.D.;
RT   "A eukaryotic alanine racemase gene involved in cyclic peptide
RT   biosynthesis.";
RL   J. Biol. Chem. 275:4906-4911(2000).
CC   -!- FUNCTION: Essential role in the production of the major forms of HC-
CC       toxin, all of which contain D-alanine. The absence of this enzyme
CC       reduces pathogenicity of the fungus on maize. Synthesizes D-alanine
CC       from L-alanine. {ECO:0000269|PubMed:10671527}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000269|PubMed:10671527};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305};
CC   -!- PATHWAY: Mycotoxin biosynthesis; HC-toxin biosynthesis.
CC   -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR   EMBL; AF169478; AAD47837.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UW18; -.
DR   SMR; Q9UW18; -.
DR   BRENDA; 5.1.1.1; 1551.
DR   UniPathway; UPA00874; -.
DR   PHI-base; PHI:469; -.
DR   GO; GO:0008784; F:alanine racemase activity; IDA:UniProtKB.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009403; P:toxin biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097:SF9; PTHR48097:SF9; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..389
FT                   /note="Alanine racemase TOXG"
FT                   /id="PRO_0000121573"
FT   MOD_RES         235
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  42697 MW;  A2F7A64D3B34B307 CRC64;
     MSNMVLNGNI DKSDRNSILD ILQSLENIAW GQPGSARCDF RSDVITRPSL RMLSAVLKTT
     LGDDVFREDL TTAHFEAHVA EISGREEGMF VITGTMANQL CLHALVSTRP CGILLSSESH
     AIHYEAGGSS MLSGAMLQPV QPSNGKYLRV EDLEEHAILT DDVHKCPTSI VSMENTAGGA
     VVPVHELRRI RDWAKQNNVR THLDGARLFE AVATGAGTLK EYCSLIDLVS VDFSKNLGAP
     MGAMILGDKK LIQQMRRTRK GIGGGMRQGG VITAAAREAL FENFGLGAEI ESQTLLQVHK
     VAKRLGEEWT RKGGKLSKEI ETNIIWLDLD AVGIKKSQFI DKGREYGVIL DGCRIVCHHQ
     IDIYAVEALI DVFHDILKAD PIKNKNSDR