LDH1_BACCR
ID LDH1_BACCR Reviewed; 314 AA.
AC Q81EP4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=L-lactate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE Short=L-LDH 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh1 {ECO:0000255|HAMAP-Rule:MF_00488}; OrderedLocusNames=BC_1924;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RA Malashkevich V.N., Bonanno J.B., Bhosle R., Toro R., Hillerich B.,
RA Gizzi A., Garforth S., Kar A., Chan M.K., Lafluer J., Patel H.,
RA Matikainen B., Chamala S., Lim S., Celikgil A., Villegas G., Evans B.,
RA Love J., Fiser A., Khafizov K., Seidel R., Almo S.C.;
RT "Crystal structure of L-lactate dehydrogenase from Bacillus cereus ATCC
RT 14579 complexed with calcium, NYSGRC Target 029452.";
RL Submitted (JUL-2013) to the PDB data bank.
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 ECO:0000305|Ref.2}.
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}.
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DR EMBL; AE016877; AAP08895.1; -; Genomic_DNA.
DR RefSeq; NP_831694.1; NC_004722.1.
DR RefSeq; WP_000715321.1; NZ_CP034551.1.
DR PDB; 4LMR; X-ray; 2.45 A; A/B=1-314.
DR PDB; 4LN1; X-ray; 1.90 A; A/B/C/D=1-314.
DR PDBsum; 4LMR; -.
DR PDBsum; 4LN1; -.
DR AlphaFoldDB; Q81EP4; -.
DR SMR; Q81EP4; -.
DR STRING; 226900.BC_1924; -.
DR EnsemblBacteria; AAP08895; AAP08895; BC_1924.
DR GeneID; 56651715; -.
DR GeneID; 64202700; -.
DR GeneID; 67506545; -.
DR KEGG; bce:BC1924; -.
DR PATRIC; fig|226900.8.peg.1927; -.
DR HOGENOM; CLU_045401_1_1_9; -.
DR OMA; AFTRHCT; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..314
FT /note="L-lactate dehydrogenase 1"
FT /id="PRO_0000168321"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 82..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 121..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 123..126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 151..154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 156
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 171
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 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT MOD_RES 223
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 268..279
FT /evidence="ECO:0007829|PDB:4LN1"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4LN1"
FT HELIX 293..310
FT /evidence="ECO:0007829|PDB:4LN1"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:4LN1"
SQ SEQUENCE 314 AA; 34789 MW; 19DC3B1C2083AB2B CRC64;
MKKGINRVVL VGTGAVGCSY AYCMINQAVA EEFVLVDVNE AKAEGEAMDL SHAVPFAPAP
TRVWKGSYED CKDADLVVIT AGLPQKPGET RLDLVEKNAK IFKQIVRSIM DSGFDGIFLI
ATNPVDILTY VTWKESGLPK ERVIGSGTTL DSARFRYMLG EYFDIGPHNI HAYIIGEHGD
TELPVWSHVS VGIQKLQTLL EKDNTYNQED LDKIFINVRD AAYHIIERKG ATYYGIGMSL
LRVTKAILND ENSVLTVSAY LEGQYGQKDV YIGVPAVLNR GGVREILEVE LSEDEELKFD
HSVQVLKETM APVL
