ID D4MA05_9BACT Unreviewed; 319 AA.
AC D4MA05;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Malate/lactate dehydrogenases {ECO:0000313|EMBL:CBL28700.1};
DE EC=1.1.1.27 {ECO:0000313|EMBL:CBL28700.1};
GN ORFNames=SY1_18390 {ECO:0000313|EMBL:CBL28700.1};
OS Fretibacterium fastidiosum.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=651822 {ECO:0000313|EMBL:CBL28700.1, ECO:0000313|Proteomes:UP000008957};
RN [1] {ECO:0000313|EMBL:CBL28700.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL28700.1,
RC ECO:0000313|Proteomes:UP000008957};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Wade W., Vartoukian S.;
RT "The genome sequence of Synergistetes sp. SGP1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL28700.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL28700.1,
RC ECO:0000313|Proteomes:UP000008957};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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DR EMBL; FP929056; CBL28700.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MA05; -.
DR KEGG; sbr:SY1_18390; -.
DR PATRIC; fig|651822.3.peg.1101; -.
DR HOGENOM; CLU_045401_1_2_0; -.
DR BioCyc; FFAS651822:G13GF-1113-MONOMER; -.
DR Proteomes; UP000008957; Chromosome.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd05291; HicDH_like; 1.
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; 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:SF31; 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|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW ECO:0000313|EMBL:CBL28700.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008957}.
FT DOMAIN 8..148
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 151..316
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 12..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 37
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; 34697 MW; 82359577FBB02CCB CRC64;
MQGKKRTVGI IGIGHVGAHV AYSLAVQGIA DEIILVDRER KKADCEAQDV MDSVCYLPHR
VEVRSGDFPD LKDCDVLVNS AGHIQLLATG NKSRLEEMDF TIRAVNGYVD RVMESGFDGV
VINVTNPCDV VAWRFAELSG LPRGRVFGTG TGLDTARLRS ALARQTGVDH KSICAYVMGE
HGASQMVPWS SVSFGGRPLA EWERTDERFR FDREAIRKEA RDAGWVVFSG KQCTEYGICS
TAARMASVVL LDEKQILPVT TRLEGEYGES GIFIGVPAVV GAGGAEQVVE VPMSAEELAE
FKGCCDDVRA NMAHALEVR
//