ID E8RU32_ASTEC Unreviewed; 396 AA.
AC E8RU32;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=Astex_3370 {ECO:0000313|EMBL:ADU15003.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU15003.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 2 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01559}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC 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}.
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DR EMBL; CP002396; ADU15003.1; -; Genomic_DNA.
DR AlphaFoldDB; E8RU32; -.
DR STRING; 573065.Astex_3370; -.
DR KEGG; aex:Astex_3370; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_0_0_5; -.
DR Proteomes; UP000001492; Chromosome 2.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01559};
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:UP000001492}.
FT DOMAIN 15..396
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559,
FT ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 41
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 94..96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 123
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 144
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 146
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 172
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 181
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 268
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 290
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 292
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 295
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 323..347
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01559"
FT BINDING 323..327
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 346..347
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 396 AA; 42990 MW; DA6B297BB8138783 CRC64;
MLEHRHSFSN SLNRWVAMII SASTDYREAA RRRLPPFLFH YIDGGAYAER TLARNMSDLG
DVALRQRVLK DVSSLSLETE LLGEKLSMPI ALAPVGLTGM YARRGEVQAA RAAQKAGINL
TLSTVSVCPI EEVQGKCDKP IWFQLYVLKD RGFMKNALER AWAAGIRTLV FTVDMPVPGA
RYRDAHSGMS GPNAEMRRLW QAVTHPHWAF DVGLMGTPHD LGNVSKYLGK ATGLADYIGW
LGANFDPSIS WKDLEWIRDF WKGPMVIKGI LDPEDAKDAV SFGADGIVVS NHGGRQLDGV
LSSARALPAI AEAVKGDLTI LADSGIRTGL DVVRMIALGA DGVLLGRAFI YALAAGGEAG
VSNLLTLFEK EMRVAMALTG VKSIREIGPQ CLVQGA
//
