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
//