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Database: UniProt
Entry: A6Q7S3_SULNB
LinkDB: A6Q7S3_SULNB
Original site: A6Q7S3_SULNB 
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
//
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