ID A0A1T0CH89_9GAMM Unreviewed; 384 AA.
AC A0A1T0CH89;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:OOS21663.1};
GN ORFNames=B0682_03135 {ECO:0000313|EMBL:OOS21663.1};
OS Moraxella lincolnii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=90241 {ECO:0000313|EMBL:OOS21663.1, ECO:0000313|Proteomes:UP000191094};
RN [1] {ECO:0000313|EMBL:OOS21663.1, ECO:0000313|Proteomes:UP000191094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 9405 {ECO:0000313|EMBL:OOS21663.1,
RC ECO:0000313|Proteomes:UP000191094};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Moraxella lincolnii CCUG 9405T type strain.";
RL Submitted (FEB-2017) 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 = AH2 + pyruvate; 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:OOS21663.1}.
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DR EMBL; MUYT01000004; OOS21663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0CH89; -.
DR STRING; 90241.B0682_03135; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000191094; 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:0004457; F:lactate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0019516; P:lactate oxidation; IEA:UniProtKB-UniRule.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 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 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|HAMAP-Rule:MF_01559,
KW ECO:0000256|PIRSR:PIRSR000138-2};
KW FMN {ECO:0000256|HAMAP-Rule:MF_01559, ECO:0000256|PIRSR:PIRSR000138-2};
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:UP000191094}.
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 384 AA; 42061 MW; B000FE1261055699 CRC64;
MIISSGNDYK EAARRRLPRF LFDYIDGGAY AEYTLKRNVS DLSEVALRQR VLKDMSSLDL
STEIFGERLS MPLALSPVGL TGMYAKRGEV QAAKAADKKG LPFTLSTVSV CPIEEVVPAI
NRPMWFQLYV LKDRGFMQNV LERAKAAGCT TLIFTVDMPV PGARYRDAHS GMSGPNAAMR
RYLQATWHPH WAINVGLLGR PHDLGNISKY MGKTIGLEDY IGYLTANFDP SISWKDLQWI
RDFWDGPMVI KGILDPKDAK DAVSFGADGI VVSNHGGRQL DGVLSTARAL PAIADAVKGD
IKILADSGIR NGLDVVRMLA MGADLCMIGR AFVYALAAEG EAGVTNLLDL FEKEMQVAMT
LTSSASIKDI NHECLLDFLK SSNS
//
