ID A0A0B2B7A9_9ACTN Unreviewed; 409 AA.
AC A0A0B2B7A9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 18-JUN-2025, entry version 40.
DE RecName: Full=Putative L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00071405};
GN ORFNames=CLV56_1820 {ECO:0000313|EMBL:PJJ57585.1};
OS Mumia flava.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Mumia.
OX NCBI_TaxID=1348852 {ECO:0000313|EMBL:PJJ57585.1, ECO:0000313|Proteomes:UP000230842};
RN [1] {ECO:0000313|EMBL:PJJ57585.1, ECO:0000313|Proteomes:UP000230842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27763 {ECO:0000313|EMBL:PJJ57585.1,
RC ECO:0000313|Proteomes:UP000230842};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + A = pyruvate + AH2; Xref=Rhea:RHEA:45816,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16651,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000256|ARBA:ARBA00050153};
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:PJJ57585.1}.
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DR EMBL; PGEZ01000001; PJJ57585.1; -; Genomic_DNA.
DR RefSeq; WP_039358510.1; NZ_PGEZ01000001.1.
DR AlphaFoldDB; A0A0B2B7A9; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000230842; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000261; L-lactate dehydrogenase (Cytochrome); 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 InterPro; IPR008259; FMN_hydac_DH_AS.
DR PANTHER; PTHR10578:SF107; 2-HYDROXYACID OXIDASE 1; 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; PS00557; FMN_HYDROXY_ACID_DH_1; 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:UP000230842}.
FT DOMAIN 27..404
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 299
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 53
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 106..108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 157
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 159
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 185
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 194
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 299
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 302
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 353..354
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 409 AA; 44685 MW; 1A0A7A8665E65E72 CRC64;
MRRRVPRWHD LGPLMKFKRP VLSPRRRRLA SALTIADLRA VAKRRTPKAA FDYTDGAAEE
ELSLARARQA FRDVELNPAI LRDVSKVDVS ASPLGVRSEL PFGIAPTGFT RLMQTEGEYA
GAGAAQAAGI PYTLSTMGTA SIEDVAATAP HGRNWFQLYM WKDRDRSMAL VDRAAKAGYE
ALVVTVDVPV AGARRRDTRN GMTIPPTLTP RNVVDAIPRP AWWFNLLTTE PLAFASLDSW
SGTVGQLLDT MFDPTVTYED LAWIRTQWEG KLVVKGVQTV ADAARLAEAG VDAIILSNHG
GRQLDRAPVP FHLLPSVVSE VGDGCEVWLD TGIMSGADVV ASLAHGADFT LIGRAYLYGL
MAGGRPGVDR TIEILRSEIE RTMRLLGVGS TAELEPGHVT QLQRLIPRR
//
