ID A0RKI4_BACAH Unreviewed; 367 AA.
AC A0RKI4;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=ldhB {ECO:0000313|EMBL:ABK87727.1};
GN Synonyms=ldh {ECO:0000256|HAMAP-Rule:MF_00488};
GN OrderedLocusNames=BALH_4532 {ECO:0000313|EMBL:ABK87727.1};
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK87727.1, ECO:0000313|Proteomes:UP000000761};
RN [1] {ECO:0000313|EMBL:ABK87727.1, ECO:0000313|Proteomes:UP000000761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK87727.1,
RC ECO:0000313|Proteomes:UP000000761};
RX PubMed=17337577; DOI=10.1128/JB.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000256|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: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; CP000485; ABK87727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RKI4; -.
DR KEGG; btl:BALH_4532; -.
DR HOGENOM; CLU_045401_1_0_9; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000000761; 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 CDD; cd05291; HicDH_like; 1.
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|HAMAP-Rule:MF_00488, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00488,
KW ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 58..196
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 199..364
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 63..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 88
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 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 172..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 174..177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 202..205
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 207
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 222
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 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ SEQUENCE 367 AA; 40626 MW; 57ECF2E1CB7BCED9 CRC64;
MTKMEYNNSQ KGQKLCSIFH KVSMVSIVGT SIIRSVRNKR NRLYDQLGEI AMKRHTRKIA
IIGTGLVGSS CAYSIVNQGI CEELLLIDIN HERAVGEAMD LSHCINFTNT RTKVYAGSYE
DCKDMDIVII TAGPAPKPGQ SRLDTLGASA KIMESVVGGV MESGFDGIFL LASNPVDIIT
YQVWKLSGLP RNRVIGTGTS LDSSRLRTIL SEMLHVDPRS IHGYSLGEHG DSQMVAWSHV
TVGGKPILQI LEEQKERFGE IDLDEIVEKT AKAGWEIYKR KGTTYYGIGN SLAYIASSIF
NDDHRVIAVS AILDGEYGEY DICTGVPAII TRDGIREIVE LNLTEDEESR FAKSNDILRD
YMKTIGY
//
