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Database: UniProt
Entry: L0K5P2_HALHC
LinkDB: L0K5P2_HALHC
Original site: L0K5P2_HALHC 
ID   L0K5P2_HALHC            Unreviewed;       310 AA.
AC   L0K5P2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967};
DE            EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967};
GN   OrderedLocusNames=Halha_0300 {ECO:0000313|EMBL:AGB40311.1};
OS   Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Halobacteroides.
OX   NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB40311.1, ECO:0000313|Proteomes:UP000010880};
RN   [1] {ECO:0000313|Proteomes:UP000010880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC   {ECO:0000313|Proteomes:UP000010880};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Halobacteroides halobius DSM 5150.";
RL   Submitted (FEB-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}.
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DR   EMBL; CP003359; AGB40311.1; -; Genomic_DNA.
DR   RefSeq; WP_015326037.1; NC_019978.1.
DR   AlphaFoldDB; L0K5P2; -.
DR   STRING; 748449.Halha_0300; -.
DR   KEGG; hhl:Halha_0300; -.
DR   PATRIC; fig|748449.3.peg.279; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_1_1_9; -.
DR   OMA; HHANIIS; -.
DR   OrthoDB; 9802969at2; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000010880; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010880}.
FT   DOMAIN          1..140
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          143..308
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         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   310 AA;  33964 MW;  F3DDCE0855E08DA4 CRC64;
     MKVVVIGAGM VGSDVTGRLL AQGSISEIVL VDINQDKAEG EVMDYSHTTS YNYNPSASLE
     VGDYSDCQGA DLIVLTAGPS IKEGQSRRDL ALQNAQVTKE IMEQIIKYTT DALIIPVTNP
     VDVVTYTAVK SGYDRDKVIG TGTIVDSARL MRIIGNKYQL DPKNIFGYIL GEHGKVSFVP
     WSIAGICGYD FETFAQIRGL DVELNKKKIT KQVQQIGFDI WKKKGYTNHG IAAGVARIVK
     AISLDEEAVL PVSVYLDREY EIEGVALSVP CIIGEQGIEK ILEFPLTKEE LKKLEDAAKS
     LENTIKEIKV
//
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