ID A0A508U194_9BRAD Unreviewed; 405 AA.
AC A0A508U194;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE SubName: Full=(S)-mandelate dehydrogenase {ECO:0000313|EMBL:VIO80218.1};
DE EC=1.1.99.31 {ECO:0000313|EMBL:VIO80218.1};
GN Name=mdlB {ECO:0000313|EMBL:VIO80218.1};
GN ORFNames=CI1B_83200 {ECO:0000313|EMBL:VIO80218.1};
OS Bradyrhizobium ivorense.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=2511166 {ECO:0000313|EMBL:VIO80218.1, ECO:0000313|Proteomes:UP000328092};
RN [1] {ECO:0000313|EMBL:VIO80218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CI-1B {ECO:0000313|EMBL:VIO80218.1};
RA Pothier F.J.;
RL Submitted (FEB-2019) 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:VIO80218.1}.
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DR EMBL; CAADFC020000034; VIO80218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A508U194; -.
DR Proteomes; UP000328092; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0033720; F:(S)-mandelate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:TreeGrafter.
DR GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000029; L-lactate 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 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 ECO:0000313|EMBL:VIO80218.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000328092}.
FT DOMAIN 24..405
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 50
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 103..105
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 132
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 152
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 154
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 180
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 189
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 279
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 301
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 303
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 306
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 333..337
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 356..357
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 405 AA; 44553 MW; 6BDB5B6DB51882F4 CRC64;
MHDRTAAPSP PPATVNRAAS AVPRRLRRYL TLDDFEPQAR RMLPKFLYGY ISGGAETDAA
RTDNRKAFDE YGFVPRVLND VSGRDQSTML FGKSYAAPFG IPPMGSSALC AYRGDIVLTR
AAAAANIPMI LSASSLITLE DVRANNQDAW YQAYLAGIDA RIEPLVDRVA AAGYDTFVVT
ADVPVPPNRE NNIRNGFQVP LAITPRVFWD TITHPDWLLN TWARTVFNHG MPHFENMDAK
QGPPVLSKNL MRNIGSRDQL AWKHVELIRK RWKGKLVVKG LISPEDARLA REHGCDGVMV
SNHGGRQLDY TVSALRTLPE IAAQKGGMTV MMDGGVRRGT DVIKALALGA DFVWVGRPFL
YAAVVAGEAG VARAISLLYD EIDRDLALLG IRSPSEITPD LVRKF
//
