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L-lactate dehydrogenase (L-LDH) (EC 1.1.1.27)

 LDH_LACCA               Reviewed;         326 AA.
P00343;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 137.
RecName: Full=L-lactate dehydrogenase;
Short=L-LDH;
EC=1.1.1.27;
Name=ldh;
Lactobacillus casei.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
Lactobacillus.
NCBI_TaxID=1582;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 /
NCDO 161;
PubMed=1768113;
Kim S.F., Baek S.J., Pack M.Y.;
"Cloning and nucleotide sequence of the Lactobacillus casei lactate
dehydrogenase gene.";
Appl. Environ. Microbiol. 57:2413-2417(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 /
NCDO 161;
Taguchi H., Ohta T.;
Submitted (NOV-1991) to the PIR data bank.
[3]
PROTEIN SEQUENCE OF 2-326.
PubMed=6411465; DOI=10.1111/j.1432-1033.1983.tb07595.x;
Hensel R., Mayr U., Yang C.;
"The complete primary structure of the allosteric L-lactate
dehydrogenase from Lactobacillus casei.";
Eur. J. Biochem. 134:503-511(1983).
[4]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Buehner M., Hecht H.J.;
"Structure determination of the allosteric L-lactate dehydrogenase
from Lactobacillus-casei at 3A resolution.";
Acta Crystallogr. A 40:32-34(1984).
-!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
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EMBL; D12591; BAA02133.1; -; Genomic_DNA.
EMBL; M76708; AAA25245.2; -; Genomic_DNA.
PIR; A43944; DELBLA.
RefSeq; WP_003567646.1; NZ_MWVD01000024.1.
PDB; 1LLC; X-ray; 3.00 A; A=2-326.
PDB; 2ZQY; X-ray; 2.60 A; A/B/C/D=1-326.
PDB; 2ZQZ; X-ray; 2.50 A; A/B/C/D/E/F=1-326.
PDB; 3VKU; X-ray; 1.96 A; A/B/C/D/E/F=1-326.
PDB; 3VKV; X-ray; 2.70 A; A/B/C/D/E/F=1-326.
PDB; 3VPF; X-ray; 2.79 A; A/B/C/D/E/F=1-326.
PDBsum; 1LLC; -.
PDBsum; 2ZQY; -.
PDBsum; 2ZQZ; -.
PDBsum; 3VKU; -.
PDBsum; 3VKV; -.
PDBsum; 3VPF; -.
ProteinModelPortal; P00343; -.
SMR; P00343; -.
PRIDE; P00343; -.
GeneID; 31583240; -.
eggNOG; ENOG4105C80; Bacteria.
eggNOG; COG0039; LUCA.
BioCyc; MetaCyc:MONOMER-8681; -.
SABIO-RK; P00343; -.
UniPathway; UPA00554; UER00611.
EvolutionaryTrace; P00343; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
Gene3D; 3.90.110.10; -; 1.
HAMAP; MF_00488; Lactate_dehydrog; 1.
InterPro; IPR001557; L-lactate/malate_DH.
InterPro; IPR011304; L-lactate_DH.
InterPro; IPR018177; L-lactate_DH_AS.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
PIRSF; PIRSF000102; Lac_mal_DH; 1.
PRINTS; PR00086; LLDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
PROSITE; PS00064; L_LDH; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Direct protein sequencing; NAD;
Oxidoreductase; Phosphoprotein.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6411465}.
CHAIN 2 326 L-lactate dehydrogenase.
/FTId=PRO_0000168347.
NP_BIND 18 46 NAD. {ECO:0000250}.
ACT_SITE 181 181 Proton acceptor. {ECO:0000250}.
BINDING 94 94 Substrate. {ECO:0000250}.
BINDING 126 126 NAD or substrate. {ECO:0000250}.
BINDING 157 157 Substrate. {ECO:0000250}.
BINDING 235 235 Substrate. {ECO:0000250}.
MOD_RES 226 226 Phosphotyrosine. {ECO:0000250}.
CONFLICT 26 26 Y -> F (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 52 52 I -> T (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 88 89 QK -> KQ (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 119 119 G -> L (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 270 270 L -> I (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 273 273 I -> L (in Ref. 3; AA sequence).
{ECO:0000305}.
HELIX 4 6 {ECO:0000244|PDB:3VKU}.
STRAND 11 15 {ECO:0000244|PDB:3VKU}.
HELIX 19 31 {ECO:0000244|PDB:3VKU}.
STRAND 35 40 {ECO:0000244|PDB:3VKU}.
HELIX 44 55 {ECO:0000244|PDB:3VKU}.
HELIX 56 60 {ECO:0000244|PDB:3VKU}.
STRAND 65 68 {ECO:0000244|PDB:3VKU}.
HELIX 71 74 {ECO:0000244|PDB:3VKU}.
STRAND 78 82 {ECO:0000244|PDB:3VKU}.
STRAND 91 93 {ECO:0000244|PDB:1LLC}.
HELIX 94 103 {ECO:0000244|PDB:3VKU}.
HELIX 105 113 {ECO:0000244|PDB:3VKU}.
TURN 114 116 {ECO:0000244|PDB:3VKU}.
STRAND 119 123 {ECO:0000244|PDB:3VKU}.
STRAND 125 127 {ECO:0000244|PDB:3VKU}.
HELIX 128 139 {ECO:0000244|PDB:3VKU}.
HELIX 143 145 {ECO:0000244|PDB:3VKU}.
STRAND 146 148 {ECO:0000244|PDB:3VKU}.
HELIX 152 166 {ECO:0000244|PDB:3VKU}.
HELIX 170 172 {ECO:0000244|PDB:3VKU}.
STRAND 177 182 {ECO:0000244|PDB:3VKU}.
HELIX 189 191 {ECO:0000244|PDB:3VKU}.
HELIX 199 205 {ECO:0000244|PDB:3VKU}.
HELIX 211 232 {ECO:0000244|PDB:3VKU}.
HELIX 237 251 {ECO:0000244|PDB:3VKU}.
STRAND 256 266 {ECO:0000244|PDB:3VKU}.
HELIX 267 269 {ECO:0000244|PDB:3VKU}.
STRAND 270 282 {ECO:0000244|PDB:3VKU}.
STRAND 285 289 {ECO:0000244|PDB:3VKU}.
HELIX 296 310 {ECO:0000244|PDB:3VKU}.
HELIX 313 316 {ECO:0000244|PDB:3VKU}.
HELIX 318 323 {ECO:0000244|PDB:2ZQY}.
SEQUENCE 326 AA; 35531 MW; 934905641592AF8A CRC64;
MASITDKDHQ KVILVGDGAV GSSYAYAMVL QGIAQEIGIV DIFKDKTKGD AIDLSNALPF
TSPKKIYSAE YSDAKDADLV VITAGAPQKP GETRLDLVNK NLKILKSIVD PIVDSGFNGI
FLVAANPVDI LTYATWKLSG FPKNRVVGSG TSLDTARFRQ SIAEMVNVDA RSVHAYIMGE
HGDTEFPVWS HANIGGVTIA EWVKAHPEIK EDKLVKMFED VRDAAYEIIK LKGATFYGIA
TALARISKAI LNDENAVLPL SVYMDGQYGL NDIYIGTPAV INRNGIQNIL EIPLTDHEEE
SMQKSASQLK KVLTDAFAKN DIETRQ


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