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
//