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Database: UniProt
Entry: B6BK81_SULGG
LinkDB: B6BK81_SULGG
Original site: B6BK81_SULGG 
ID   B6BK81_SULGG            Unreviewed;       314 AA.
AC   B6BK81; H1FSQ7;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Malate dehydrogenase, NAD-dependent {ECO:0000313|EMBL:EHP31175.1};
DE            EC=1.1.1.37 {ECO:0000313|EMBL:EHP31175.1};
GN   Name=mdh2 {ECO:0000313|EMBL:EHP31175.1};
GN   ORFNames=SMGD1_2653 {ECO:0000313|EMBL:EHP31175.1};
OS   Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP31175.1, ECO:0000313|Proteomes:UP000006431};
RN   [1] {ECO:0000313|EMBL:EHP31175.1, ECO:0000313|Proteomes:UP000006431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD1 {ECO:0000313|EMBL:EHP31175.1,
RC   ECO:0000313|Proteomes:UP000006431};
RX   PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA   Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA   Labrenz M., Jurgens K.;
RT   "Genome and physiology of a model Epsilonproteobacterium responsible for
RT   sulfide detoxification in marine oxygen depletion zones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHP31175.1}.
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DR   EMBL; AFRZ01000001; EHP31175.1; -; Genomic_DNA.
DR   RefSeq; WP_008337263.1; NZ_DS995287.1.
DR   AlphaFoldDB; B6BK81; -.
DR   STRING; 929558.SMGD1_2653; -.
DR   PATRIC; fig|929558.5.peg.2642; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_7; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000006431; Unassembled WGS sequence.
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:EHP31175.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006431};
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;  33804 MW;  9E56E73BD5C04AC0 CRC64;
     MVGRRVGIVG AGFVGATAAY SLTMTGRCHE VVLYDINSDL AKGKAIDIGQ STSYSVRGTI
     VTAAEDAKDL KDCDIIVVTA GVPRKSDMTR ADLLMINAKI MKDVVGNIMK YSPNAIIICV
     SNPLDIMTYV IHKMTGWNRN RIIGMAGALD GARMAYQINQ KVGYGSGQTR AMLIGDHGQN
     MIPLPEISAV GGVPLDQIVT KEDMEDIIAR TKDGGAEIVK YLGTSAYYAP GRAISVMVEA
     ILDDSRIVMP SSVMLDGEYG YRDITVGVPV VLGANGVEKI IELELDEETK AKFKISVDSI
     QDGIDILKEN DFFV
//
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