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ID A4AWN8_MARSH Unreviewed; 308 AA.
AC A4AWN8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 08-MAY-2019, entry version 86.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487};
DE EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487};
GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487};
GN OrderedLocusNames=FB2170_01791 {ECO:0000313|EMBL:EAQ99652.1};
OS Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99652.1, ECO:0000313|Proteomes:UP000001602};
RN [1] {ECO:0000313|EMBL:EAQ99652.1, ECO:0000313|Proteomes:UP000001602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX PubMed=21037013; DOI=10.1128/JB.01207-10;
RA Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2170, a novel member of the
RT genus Maribacter in the family Flavobacteriaceae.";
RL J. Bacteriol. 193:303-304(2011).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_00487,
CC ECO:0000256|SAAS:SAAS01087531}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.37; Evidence={ECO:0000256|HAMAP-Rule:MF_00487};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000256|HAMAP-Rule:MF_00487}.
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DR EMBL; CP002157; EAQ99652.1; -; Genomic_DNA.
DR RefSeq; WP_013305051.1; NC_014472.1.
DR STRING; 313603.FB2170_01791; -.
DR EnsemblBacteria; EAQ99652; EAQ99652; FB2170_01791.
DR KEGG; fbc:FB2170_01791; -.
DR eggNOG; ENOG4105C80; Bacteria.
DR eggNOG; COG0039; LUCA.
DR HOGENOM; HOG000213794; -.
DR KO; K00024; -.
DR OMA; MDLMQTA; -.
DR OrthoDB; 870724at2; -.
DR BioCyc; MSP313603:G1GNS-619-MONOMER; -.
DR Proteomes; UP000001602; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd01339; LDH-like_MDH; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00487; Malate_dehydrog_3; 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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
PE 3: Inferred from homology;
DR PRODOM; A4AWN8.
DR SWISS-2DPAGE; A4AWN8.
KW Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00487, ECO:0000256|SAAS:SAAS01087535};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487,
KW ECO:0000256|RuleBase:RU003369, ECO:0000256|SAAS:SAAS01087526};
KW Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00487,
KW ECO:0000256|SAAS:SAAS01087533}.
FT DOMAIN 1 142 Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT DOMAIN 147 301 Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT NP_BIND 7 12 NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT NP_BIND 118 120 NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT ACT_SITE 175 175 Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT 1}.
FT BINDING 32 32 NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT BINDING 82 82 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_00487}.
FT BINDING 88 88 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT 2}.
FT BINDING 95 95 NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT BINDING 120 120 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT 2}.
FT BINDING 151 151 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT 2}.
SQ SEQUENCE 308 AA; 32285 MW; A90192EC534698D1 CRC64;
MKVTVVGAGA VGASCAEYIA IKDFASEVVV LDIKEGYAEG KAMDLMQTAS LNGFDTKITG
TTNDYSKTAG SDIAVITSGI PRKPGMTREE LIGINAGIVK TVSANLIEHS PNVILIVVSN
PMDTMTYLVH KTTGLPKNKI IGMGGALDSA RFKYRLAEAM EAPISDIDGM VIGGHSDTGM
VPLASHATRN SINVSEYLSE DRLNQVVEDT KVGGATLTKL LGTSAWYAPG AAVSSLVQAI
ACDQKKMFPC STLLEGEYGL NDICIGVPVI LGKNGIEKVV DVPLSDAEKT KMQESAAGVT
KTNGLLEV
//
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