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Database: UniProt
Entry: A6Q7S2_SULNB
LinkDB: A6Q7S2_SULNB
Original site: A6Q7S2_SULNB 
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
//
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