ID F3KLW7_9ARCH Unreviewed; 300 AA.
AC F3KLW7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Lactate/malate dehydrogenase {ECO:0000313|EMBL:EGG41701.1};
GN ORFNames=Nlim_1500 {ECO:0000313|EMBL:EGG41701.1};
OS Candidatus Nitrosarchaeum limnium SFB1.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=886738 {ECO:0000313|EMBL:EGG41701.1};
RN [1] {ECO:0000313|EMBL:EGG41701.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB1 {ECO:0000313|EMBL:EGG41701.1};
RX PubMed=21364937; DOI=10.1371/journal.pone.0016626;
RA Blainey P.C., Mosier A.C., Potanina A., Francis C.A., Quake S.R.;
RT "Genome of a low-salinity ammonia-oxidizing archaeon determined by single-
RT cell and metagenomic analysis.";
RL PLoS ONE 6:E16626-E16626(2011).
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|ARBA:ARBA00008104, 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:EGG41701.1}.
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DR EMBL; AEGP01000050; EGG41701.1; -; Genomic_DNA.
DR AlphaFoldDB; F3KLW7; -.
DR STRING; 886738.Nlim_1500; -.
DR PATRIC; fig|886738.10.peg.1637; -.
DR HOGENOM; CLU_045401_2_2_2; -.
DR Proteomes; UP000004348; Chromosome.
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:SF34; 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 NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 2..137
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 141..298
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 6..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 113..115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 300 AA; 33197 MW; 8EC40D24A9C7ECAD CRC64;
MISIIGSGKV GTAIAFLCIT NSLDDILFVN RTKSKAIGEA LDISNAVPAN SNITIHGTDD
FSKISGSNIV VITASTGTYL KSRTEMMDAQ VKMIKEIANK IKKYCPSAIV LVVSNPLDVL
TFIFQKETQF SRNKVIGIAS SLDSSRFRYL LSEKFGIKQS QITDTLVMGE HGDSMVPIFS
RVKINGKNVS EMLNDLDKKT ITTETQNYWR SLRLLKTRSE FGIAKNTFDV IRAIINNDEL
VIPASIVLNG EYGEKDVALG IPVKINKNGV KEIIEIKLNE QENKLLKISA QTIRNYIKSL
//
