ID D5APZ5_RHOCB Unreviewed; 309 AA.
AC D5APZ5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
DE Short=L-LDH {ECO:0000256|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
GN Name=ldh {ECO:0000256|HAMAP-Rule:MF_00488,
GN ECO:0000313|EMBL:ADE84582.1};
GN OrderedLocusNames=RCAP_rcc00817 {ECO:0000313|EMBL:ADE84582.1};
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE84582.1, ECO:0000313|Proteomes:UP000002361};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB1003;
RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADE84582.1, ECO:0000313|Proteomes:UP000002361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC {ECO:0000313|Proteomes:UP000002361};
RX PubMed=20418398; DOI=10.1128/JB.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966}.
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:0000256|ARBA:ARBA00001763, ECO:0000256|HAMAP-
CC Rule:MF_00488};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate (FBP). {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000256|ARBA:ARBA00006054, ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00488}.
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DR EMBL; CP001312; ADE84582.1; -; Genomic_DNA.
DR RefSeq; WP_013066561.1; NC_014034.1.
DR AlphaFoldDB; D5APZ5; -.
DR STRING; 272942.RCAP_rcc00817; -.
DR GeneID; 31489759; -.
DR KEGG; rcp:RCAP_rcc00817; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_1_1_5; -.
DR OMA; CYIIVLT; -.
DR OrthoDB; 9802969at2; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000002361; 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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
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; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00488};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00488};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00488}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00488};
KW Reference proteome {ECO:0000313|Proteomes:UP000002361}.
FT DOMAIN 1..139
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 142..305
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 76..77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 115..117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 117..120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 145..148
FT /ligand="substrate"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00488"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ SEQUENCE 309 AA; 31558 MW; 820A86A0954E528E CRC64;
MKVGIVGAGM VGSAAGFAIA MRGGASEVVF VDRNAALAQA QAEDIGHAVP FAHPVKLGAG
DYEVLAGAGI VILAAGVAQK PGESRLSLLS RNAAVFSEVI AKVRAQAPEA LLIVASNPVD
IMTEVAQRAS GLPAERVIGT GTLLDSARFR ALLAGHLGVA AHSVHGFVLG EHGDSEVLAW
SSARVGAEPL DRIASQLGVA ITEEVRAKID AGVRQAAYRI IAGKGATWYG IGAGLARLVQ
AIRDDQRAVM SVSIRSPEVA GIADVALSLP RVIGAAGVVS TLIPSLDEGE WAALHRSAAV
LKESAEGLW
//