ID A6Q7S2_SULNB Unreviewed; 320 AA.
AC A6Q7S2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE SubName: Full=Malate dehydrogenase, NAD-dependent {ECO:0000313|EMBL:BAF71531.1};
DE EC=1.1.1.37 {ECO:0000313|EMBL:BAF71531.1};
GN OrderedLocusNames=SUN_0571 {ECO:0000313|EMBL:BAF71531.1};
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum.
OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF71531.1, ECO:0000313|Proteomes:UP000006378};
RN [1] {ECO:0000313|EMBL:BAF71531.1, ECO:0000313|Proteomes:UP000006378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF71531.1,
RC ECO:0000313|Proteomes:UP000006378};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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DR EMBL; AP009179; BAF71531.1; -; Genomic_DNA.
DR RefSeq; WP_011980264.1; NC_009663.1.
DR AlphaFoldDB; A6Q7S2; -.
DR STRING; 387093.SUN_0571; -.
DR KEGG; sun:SUN_0571; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_7; -.
DR OMA; MGWTSQA; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000006378; 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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01339; LDH-like_MDH; 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; IPR011275; Malate_DH_type3.
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:BAF71531.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 6..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 150..307
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 121..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 320 AA; 34458 MW; 8F21C1D2CD80376A CRC64;
MAKGKKVTVI GTGNFGSTVA FILAMNGSCH HVMLRGRNYD VAKGKALDMS QAANAARQHT
IVKAAKGPED MEGSDVVIIT AGAPRTPGMS RDDLLFKNAD IVKCYSREIK EYAPDAIVIV
VSNPLDVMTY VALKETGFPR QRVLGMAGIL DAARMAHFIY EKLEYGAGQI RATVMGGHGD
TMVPLPKFTT VAGVPIEDLL DSEEIGEIVR KTRNGGAEIV NLLGDGSAYY APAKSTTVMV
EAILKDTNQI HSCAIMLKND YGYSDIVSGV PVMIGAGGAE KVINMTLKPL QQTRFKNSVA
SVQEMVDTLY EANFFDDDKK
//