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Database: UniProt
Entry: A0A0S8J0S8_9BACT
LinkDB: A0A0S8J0S8_9BACT
Original site: A0A0S8J0S8_9BACT 
ID   A0A0S8J0S8_9BACT        Unreviewed;       224 AA.
AC   A0A0S8J0S8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:KPL03369.1};
DE   Flags: Fragment;
GN   ORFNames=AMK75_01490 {ECO:0000313|EMBL:KPL03369.1};
OS   Planctomycetes bacterium SM23_65.
OC   Bacteria; Planctomycetota.
OX   NCBI_TaxID=1704030 {ECO:0000313|EMBL:KPL03369.1, ECO:0000313|Proteomes:UP000052185};
RN   [1] {ECO:0000313|EMBL:KPL03369.1, ECO:0000313|Proteomes:UP000052185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_65 {ECO:0000313|EMBL:KPL03369.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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:KPL03369.1}.
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DR   EMBL; LJUT01000020; KPL03369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8J0S8; -.
DR   PATRIC; fig|1704030.3.peg.155; -.
DR   Proteomes; UP000052185; Unassembled WGS sequence.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
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; 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   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   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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369}.
FT   DOMAIN          2..53
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          56..221
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPL03369.1"
SQ   SEQUENCE   224 AA;  24606 MW;  AA7FE6BDCBE12FD3 CRC64;
     TLVDRNVRIY KDIVPRLVEV ASGAIIIVVS NPVDVLTYAT IRISGLPWQR VVGSGTILDT
     ARFRHELGRH CGIDPRNVHA YIIGEHGDTE VPVWSLANIA GIGFKPYCRF CGRGCSDDQR
     NGIFEAVKNA AYEIIRLKGA TYFAIALGTT RMIEAILRDQ DTVVTASTLV RGQFDIEDVC
     LSLPVVLGRS GIERVLELPL SPDERRALKH SADTLKNVIK SVGI
//
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