ID A6Q7S3_SULNB Unreviewed; 314 AA.
AC A6Q7S3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE SubName: Full=Malate dehydrogenase, NAD-dependent {ECO:0000313|EMBL:BAF71532.1};
DE EC=1.1.1.37 {ECO:0000313|EMBL:BAF71532.1};
GN OrderedLocusNames=SUN_0572 {ECO:0000313|EMBL:BAF71532.1};
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum.
OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF71532.1, ECO:0000313|Proteomes:UP000006378};
RN [1] {ECO:0000313|EMBL:BAF71532.1, ECO:0000313|Proteomes:UP000006378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF71532.1,
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; BAF71532.1; -; Genomic_DNA.
DR RefSeq; WP_011980265.1; NC_009663.1.
DR AlphaFoldDB; A6Q7S3; -.
DR STRING; 387093.SUN_0572; -.
DR KEGG; sun:SUN_0572; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_7; -.
DR OMA; ASCAEYI; -.
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:BAF71532.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 5..144
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 149..305
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 120..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 314 AA; 33792 MW; F14939B7E2D54B0D CRC64;
MHRRKVGIIG AGAVGATAAY SLCMMGTCNE IVLFDIAEGV AKGKAIDIAQ SSHYAPNSTI
VTAAESPADV NDCDIVVITA GVPRKGDMTR EDLLMINAKI MKTVVEDVKT YSPDAVIICV
SNPLDVMTYV IQRMTGWERN RIIGMAGALD GARMAYQIYN KLGYGAGQIG TLVIGDHGQN
MIPLPQKVQV GDVPVNELLS KAEMEEIIER TRTGGAEIVK HLGTSGYYAP GRAIAHMVEA
LLNDSRIVVS SSVLLDGEYG YSDVTVGVPV VLGKNGVEKI IEIDLDSETR EKFKISVDSI
NENIAILKQN KFFD
//