ID A0A2G7G686_9EURO Unreviewed; 420 AA.
AC A0A2G7G686;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:PIG88356.1};
GN ORFNames=AARAC_001375 {ECO:0000313|EMBL:PIG88356.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG88356.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG88356.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG88356.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIG88356.1}.
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DR EMBL; NEXV01000108; PIG88356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7G686; -.
DR STRING; 656916.A0A2G7G686; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR FunFam; 3.20.20.70:FF:000132; FMN dependent dehydrogenase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR PANTHER; PTHR10578:SF75; L-LACTATE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_4G07050); 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR000138-
KW 2}; FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000231358}.
FT DOMAIN 32..410
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 58
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 111..113
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 140
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 162
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 164
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 190
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 199
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 281
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 303
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 305
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 308
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 336..340
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 359..360
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 420 AA; 46856 MW; DADEB5E20849F128 CRC64;
MSDQTNPNIQ KRTTPQWALY QRENFWKLNE GQTPPFNTDP IKLEQLAHEK LSQGGWYYAS
SNAGMSNTHL ANRQAFFRHR IIPRQLVDTN LRDTTTEIFG HRVSAPIGFA PIGINKIYHP
SAEAAVAMVA GELNLPYCLS TAGSTPIEKV AEANGKGPRF YQLYMPHDDE LTLSLLNRAW
KSGFDALILT TDTWQLGWRH DDVANSNYTF YRGTGADLGL TDPVFQKRCR EEGIDLEKDI
VAASAKWIDS VWHGRAWSWE KIPWLIEQWK KISGGRPFAI KGIQSVADAK KCVEYGVDGI
VVSNHAGRQV DGAIASLDAL ENIANAVGDQ IYIMYDSGVR GASDVAKALA LGARFVFVGR
LWIWGLSIMG EEGVRHVMKS LLADFDIFMC VAGFNSVKEL DRSILESYPK GYTLVPDKVL
//
