ID B9KGG0_CAMLR Unreviewed; 298 AA.
AC B9KGG0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE SubName: Full=Malate dehydrogenase, NAD-dependent {ECO:0000313|EMBL:ACM64145.1};
DE EC=1.1.1.37 {ECO:0000313|EMBL:ACM64145.1};
GN Name=mdh {ECO:0000313|EMBL:ACM64145.1};
GN OrderedLocusNames=Cla_0818 {ECO:0000313|EMBL:ACM64145.1};
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM64145.1, ECO:0000313|Proteomes:UP000007727};
RN [1] {ECO:0000313|EMBL:ACM64145.1, ECO:0000313|Proteomes:UP000007727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060
RC {ECO:0000313|Proteomes:UP000007727};
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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DR EMBL; CP000932; ACM64145.1; -; Genomic_DNA.
DR RefSeq; WP_012661528.1; NC_012039.1.
DR AlphaFoldDB; B9KGG0; -.
DR STRING; 306263.Cla_0818; -.
DR GeneID; 7410398; -.
DR KEGG; cla:CLA_0818; -.
DR PATRIC; fig|306263.5.peg.798; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_7; -.
DR OMA; ASCAEYI; -.
DR Proteomes; UP000007727; Chromosome.
DR GO; GO:0030060; F:L-malate 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; 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 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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW ECO:0000313|EMBL:ACM64145.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007727}.
FT DOMAIN 1..140
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 146..294
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 298 AA; 33080 MW; A0F49F2D0C049F86 CRC64;
MKITIIGAGN VGVSTAYALI LRELVDELVL IDINKDLLFA RELELSQSIA AFNFDIKITC
TDDYAHSKDS QVVIFSAGVA RKEGQSRDEL FAINAKIMLE CANNIKKFNN DPLFIIVSNP
VDFLLNALYE SKLFSSKKII AMAGVLDNAR FKYEVGKKLD IKTSYIDTKL IGFHNDSMVL
VKSQSKVQNK ALNKVLNECD LTQIEQEVKT GGAKIIKYLK TSAYLAPASA CVRMIEALKS
GEFLPICAIL DGEYGIKEKA FGVMARISLD GVLEILELKL DNQEQIALEN SLSQYNYK
//