ID A0A1S8CLU3_9GAMM Unreviewed; 380 AA.
AC A0A1S8CLU3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 08-OCT-2025, entry version 41.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01559};
DE EC=1.1.-.- {ECO:0000256|HAMAP-Rule:MF_01559};
GN Name=lldD {ECO:0000256|HAMAP-Rule:MF_01559,
GN ECO:0000313|EMBL:OMQ23724.1};
GN ORFNames=BMI79_09450 {ECO:0000313|EMBL:OMQ23724.1};
OS Serratia oryzae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Yersiniaceae; Serratia.
OX NCBI_TaxID=2034155 {ECO:0000313|EMBL:OMQ23724.1, ECO:0000313|Proteomes:UP000216021};
RN [1] {ECO:0000313|EMBL:OMQ23724.1, ECO:0000313|Proteomes:UP000216021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J11-6 {ECO:0000313|EMBL:OMQ23724.1,
RC ECO:0000313|Proteomes:UP000216021};
RA Zhang X.-X., Zhang J.;
RT "Rahnella oryzae sp. nov., isolated from rice root.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of L-lactate to pyruvate. Is coupled
CC to the respiratory chain. {ECO:0000256|HAMAP-Rule:MF_01559}.
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|HAMAP-Rule:MF_01559};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|HAMAP-Rule:MF_01559};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01559};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01559}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042,
CC ECO:0000256|HAMAP-Rule:MF_01559}.
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:OMQ23724.1}.
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DR EMBL; MOXD01000004; OMQ23724.1; -; Genomic_DNA.
DR RefSeq; WP_076941928.1; NZ_MOXD01000004.1.
DR AlphaFoldDB; A0A1S8CLU3; -.
DR STRING; 2034155.BMI79_09450; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000216021; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter.
DR GO; GO:0006089; P:lactate metabolic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01559; L_lact_dehydr; 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 InterPro; IPR020920; LldD.
DR NCBIfam; NF033901; L_lactate_LldD; 1.
DR NCBIfam; NF008398; PRK11197.1; 1.
DR PANTHER; PTHR10578:SF85; L-LACTATE DEHYDROGENASE; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01559};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01559};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01559};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01559};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01559}; Reference proteome {ECO:0000313|Proteomes:UP000216021}.
FT DOMAIN 1..380
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559,
FT ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 24
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 77..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559,
FT ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559,
FT ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 129
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 155
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559,
FT 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 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 251
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559,
FT ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 273
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 275
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 278
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 306..330
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 306..310
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 329..330
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 380 AA; 41277 MW; 49F45AC9713C49BD CRC64;
MIISAASDYR AAAQRKLPPF LFHYIDGGAY AEHTLRRNVE DLAQVALRQR VLKNMSALSL
ETKLFNETLS MPVALGPVGL CGMYARRGEV QAARAAERNG IPFTLSTVSV CPIEEVTSAI
KRPMWFQLYV LKDRGFMRNA LERAKAAGCT TLVFTVDMPT PGARYRDAHS GMSGPHAALR
RYWQAVTHPA WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLGANFDP SISWSDLEWI
RDFWQGPMVI KGILDADDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PSIADAVKGD
ITILADSGVR SGLDVVRMIA LGADSVLLGR AYLYALATAG QAGVENLLDL IRKEMCVAMT
LTGAKSIAEI SRDLLVQEGF
//
