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Database: UniProt
Entry: A0A1A0TTZ0_9MYCO
LinkDB: A0A1A0TTZ0_9MYCO
Original site: A0A1A0TTZ0_9MYCO 
ID   A0A1A0TTZ0_9MYCO        Unreviewed;       319 AA.
AC   A0A1A0TTZ0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967};
DE            EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967};
GN   ORFNames=A5757_04900 {ECO:0000313|EMBL:OBB62218.1};
OS   Mycobacterium sp. 852013-51886_SCH5428379.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834111 {ECO:0000313|EMBL:OBB62218.1, ECO:0000313|Proteomes:UP000091910};
RN   [1] {ECO:0000313|Proteomes:UP000091910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852013-51886_SCH5428379 {ECO:0000313|Proteomes:UP000091910};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA   Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL   Submitted (JUN-2016) 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:OBB62218.1}.
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DR   EMBL; LZSU01000003; OBB62218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A0TTZ0; -.
DR   STRING; 1834111.A5757_04900; -.
DR   OrthoDB; 9802969at2; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000091910; Unassembled WGS sequence.
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; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091910}.
FT   DOMAIN          10..148
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          151..314
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         15..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         124..126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   319 AA;  32812 MW;  D4B05B82DB8E94EB CRC64;
     MKGILVRGRK VSIVGAGSVG TAIAYACLIR GSAGALALFD TNTAKVRAEI LDLNHGSQFV
     PPCRVDGADD IAVTAGSDVV IVTAGAKQHP GQSRLDLAAA NVLMAQTLTP RLVEQSPNAV
     VLFVTNPVDV VTYAATRAVG AGPGRIFGSG TVLDSSRFRY LVAQRAAVDV GNVHAVVIGE
     HGDSEIALWS TLSVGGVRAD AYRLDGRLIF DEATRTAIGA DVVNAAYEII AGKGATNLAI
     GLATARIVEA VLGDQHRVLP VSRVQDGAHG ITGVALSLPT VVSAGGAGRV LEVELSPAEH
     DGLHRSARTL RDIQESLGI
//
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