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Database: UniProt
Entry: A0A0D5NI40_9BACL
LinkDB: A0A0D5NI40_9BACL
Original site: A0A0D5NI40_9BACL 
ID   A0A0D5NI40_9BACL        Unreviewed;       317 AA.
AC   A0A0D5NI40;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:AJY74622.1};
GN   ORFNames=VN24_08570 {ECO:0000313|EMBL:AJY74622.1};
OS   Paenibacillus beijingensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY74622.1, ECO:0000313|Proteomes:UP000032633};
RN   [1] {ECO:0000313|EMBL:AJY74622.1, ECO:0000313|Proteomes:UP000032633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY74622.1,
RC   ECO:0000313|Proteomes:UP000032633};
RX   PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA   Kwak Y., Shin J.H.;
RT   "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT   24997(T)), a novel rhizobacterium from jujube garden soil.";
RL   J. Biotechnol. 206:75-76(2015).
RN   [2] {ECO:0000313|Proteomes:UP000032633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA   Kwak Y., Shin J.-H.;
RT   "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; CP011058; AJY74622.1; -; Genomic_DNA.
DR   RefSeq; WP_045670055.1; NZ_CP011058.1.
DR   AlphaFoldDB; A0A0D5NI40; -.
DR   STRING; 1126833.VN24_08570; -.
DR   KEGG; pbj:VN24_08570; -.
DR   PATRIC; fig|1126833.4.peg.1890; -.
DR   HOGENOM; CLU_045401_1_2_9; -.
DR   OrthoDB; 9802969at2; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000032633; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00488};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00488,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032633}.
FT   DOMAIN          7..145
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..311
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         12..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         68
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         121..123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         123..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         146
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         151..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ   SEQUENCE   317 AA;  34468 MW;  9D03C7A4BAF1CB89 CRC64;
     MGSKVRKVAI VGVGHVGSSC AYAMVNQSVC DEMMLIGRTP QRARAHALDL SHCVDFTHSR
     TKVYAGTYAD CKDMDIVMLC AGGNPVPGGT RLDLLDSAYE IHRDIIGPIM DSGFDGIFIA
     ASNPVDIVTY MVWKLSGLPR GRVIGSGTSI DSSRLKTLLS EYLPVDPRSV QGYVLGEHGE
     SQFPAWSHVT IGGKPILDIV KQHPVRFAHM KLDEIALRTR NSGWEILQGK GSTHFGVAGA
     LTAIARSILN DDHRIMAVSA ILDGEYGQRE IGIGVPAILS REGIEEVLEL NLTEAEKEQF
     ESSCRVIRQA MSRLPQL
//
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