ID A0A177DII1_ALTAL Unreviewed; 235 AA.
AC A0A177DII1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=D-lactate dehydratase {ECO:0000256|ARBA:ARBA00013134};
DE EC=4.2.1.130 {ECO:0000256|ARBA:ARBA00013134};
GN ORFNames=CC77DRAFT_992013 {ECO:0000313|EMBL:OAG18842.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG18842.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG18842.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG18842.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylglyoxal = (R)-lactate + H(+);
CC Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130;
CC Evidence={ECO:0000256|ARBA:ARBA00001524};
CC -!- SIMILARITY: Belongs to the peptidase C56 family. HSP31-like subfamily.
CC {ECO:0000256|ARBA:ARBA00038493}.
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DR EMBL; KV441482; OAG18842.1; -; Genomic_DNA.
DR RefSeq; XP_018384263.1; XM_018536372.1.
DR AlphaFoldDB; A0A177DII1; -.
DR STRING; 5599.A0A177DII1; -.
DR GeneID; 29121966; -.
DR KEGG; aalt:CC77DRAFT_992013; -.
DR VEuPathDB; FungiDB:CC77DRAFT_992013; -.
DR OMA; MYDLATD; -.
DR OrthoDB; 4342at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0019172; F:glyoxalase III activity; IEA:UniProt.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03141; GATase1_Hsp31_like; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR PANTHER; PTHR48094:SF11; GLUTATHIONE-INDEPENDENT GLYOXALASE HSP31-RELATED; 1.
DR PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000313|EMBL:OAG18842.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transferase {ECO:0000313|EMBL:OAG18842.1}.
FT DOMAIN 95..230
FT /note="DJ-1/PfpI"
FT /evidence="ECO:0000259|Pfam:PF01965"
SQ SEQUENCE 235 AA; 25621 MW; F2670E2EB91204BE CRC64;
MSNRSKLLIV LTSQDILPTR EGVKTGWYLP ELVHPYNVLN PYVDMVFASP KGGEAPIDPY
SIEDSKDDEE CRRFLRDKEA LWKDTKSLGT IIERADEFLG VFFVGGHGPM FDLADDSISH
SLIRRFYESG KIVSAVCHGP AALVNVKLSD GSYMIQGQNV TGFSNAEEDA NDSTSAMPFL
LEDALKNHGG KYEKAGQLFG AKVVISGKQG NLVTGQNPLS AAAIGKALLE LIQKL
//
