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Database: UniProt
Entry: L8K2S3_9BACT
LinkDB: L8K2S3_9BACT
Original site: L8K2S3_9BACT 
ID   L8K2S3_9BACT            Unreviewed;       306 AA.
AC   L8K2S3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967};
DE            EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967};
GN   ORFNames=C900_01347 {ECO:0000313|EMBL:ELR73737.1};
OS   Fulvivirga imtechensis AK7.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Fulvivirga.
OX   NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR73737.1, ECO:0000313|Proteomes:UP000011135};
RN   [1] {ECO:0000313|EMBL:ELR73737.1, ECO:0000313|Proteomes:UP000011135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK7 {ECO:0000313|EMBL:ELR73737.1,
RC   ECO:0000313|Proteomes:UP000011135};
RA   Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Fulvivirga imtechensis AK7.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELR73737.1}.
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DR   EMBL; AMZN01000002; ELR73737.1; -; Genomic_DNA.
DR   RefSeq; WP_009577547.1; NZ_AMZN01000002.1.
DR   AlphaFoldDB; L8K2S3; -.
DR   STRING; 1237149.C900_01347; -.
DR   PATRIC; fig|1237149.3.peg.110; -.
DR   eggNOG; COG0039; Bacteria.
DR   OrthoDB; 9802969at2; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000011135; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011135};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..140
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          143..303
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         116..118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   306 AA;  33212 MW;  8ABAF62F78DE8BE7 CRC64;
     MGGKSIGIIG MGWVGSSVAI SVLYSGIANE LLLYDIKTGI AEGEAMDLSH GSSFYPTARV
     AATTVEEMMR TDAIVVAAGR GGKPGETRLQ LLNENVLIAK NIAEKLRGYE GIIIVVSNPV
     DVLTYFIQKF SGLPTSRVIG TGTMLDTARL KEILGQSLLL DPRSIHAQVI GEHGDSEVVL
     WSSAMVGGMN LRNWKGWVRE KELVISERVR TAAQEIIKRK GATNHAIGLV TATLIKWMLR
     GERRIINVSR VQEGAMGYMD VAISLPTIVG IDGATEVLIP NMSDEEHEKF HKSVEVIKKA
     IVSVKY
//
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