LDH_PETMO
ID LDH_PETMO Reviewed; 307 AA.
AC A9BGZ9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488}; OrderedLocusNames=Pmob_1893;
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00488};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000255|HAMAP-Rule:MF_00488}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000879; ABX32580.1; -; Genomic_DNA.
DR RefSeq; WP_012209677.1; NC_010003.1.
DR PDB; 6H9S; X-ray; 1.90 A; A/B=1-307.
DR PDBsum; 6H9S; -.
DR AlphaFoldDB; A9BGZ9; -.
DR SMR; A9BGZ9; -.
DR STRING; 403833.Pmob_1893; -.
DR EnsemblBacteria; ABX32580; ABX32580; Pmob_1893.
DR KEGG; pmo:Pmob_1893; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_1_1_0; -.
DR OMA; CYIIVLT; -.
DR OrthoDB; 870724at2; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000000789; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00488; Lactate_dehydrog; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR011304; L-lactate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase;
KW Phosphoprotein.
FT CHAIN 1..307
FT /note="L-lactate dehydrogenase"
FT /id="PRO_1000081367"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 76..77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 115..117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 117..120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 145..148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 150
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 165
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 85..106
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 207..225
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6H9S"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6H9S"
FT HELIX 283..302
FT /evidence="ECO:0007829|PDB:6H9S"
SQ SEQUENCE 307 AA; 33346 MW; A753D3295EF5596D CRC64;
MKISIIGTGR VGSSTAFALI NAAVADEIVL YDLNKEMAEG EALDLLHATT FHKRMIIRAG
EYSDIEGSDI VLITAGAAQK PGETRLDLTI KNAKIIKGIS ENIKKYAPNT LIINITNPVD
VMSYVVWKVT GFESNRVIGT GTILDTARLR ALIGKNCGVS PMSVHAYIIG EHGDSELAAW
SSAMIGGVPI KGFCRNCPYK DNCNKDLSKI FDDVKNSAYT IISKKGATNY GIASATTALV
ESIIKNEGRV YTPSVLLDDV YIGYPAVINK DGVERTIDIT LNDEETEKFE SSKSIIKEYL
ESIKNLL
