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Database: UniProt/TrEMBL
Entry: A0A0K0XXD3_9GAMM
LinkDB: A0A0K0XXD3_9GAMM
Original site: A0A0K0XXD3_9GAMM 
ID   A0A0K0XXD3_9GAMM        Unreviewed;       327 AA.
AC   A0A0K0XXD3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 18.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=WM2015_1977 {ECO:0000313|EMBL:AKS42343.1};
OS   Wenzhouxiangella marina.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Wenzhouxiangellaceae; Wenzhouxiangella.
OX   NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS42343.1, ECO:0000313|Proteomes:UP000066624};
RN   [1] {ECO:0000313|EMBL:AKS42343.1, ECO:0000313|Proteomes:UP000066624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS42343.1,
RC   ECO:0000313|Proteomes:UP000066624};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01517,
CC       ECO:0000256|SAAS:SAAS00755561}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066,
CC       ECO:0000256|SAAS:SAAS00369698}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP012154; AKS42343.1; -; Genomic_DNA.
DR   RefSeq; WP_049725912.1; NZ_CP012154.1.
DR   EnsemblBacteria; AKS42343; AKS42343; WM2015_1977.
DR   KEGG; wma:WM2015_1977; -.
DR   PATRIC; fig|1579979.3.peg.2022; -.
DR   KO; K00024; -.
DR   Proteomes; UP000066624; 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:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000066624};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066624};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        6    152       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      156    322       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     105    105       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   327 AA;  34867 MW;  4F9D166C92DDF776 CRC64;
     MNRPKRVAIT GAAGQIGYQL CFRIASGDLL GPNQPVILQL IEIAPALDAL KGVVMELEDA
     AFPLLAGVEA TADLETGFKD ADYAILVGAK PRGPGMERAD LLSENGKIFG PQGRALNAVA
     SRDVKVLVVG NPANTNALIA QANAPDLPKE NFTAMTRLDH NRALAQLAAR TGIHHTSIRQ
     MTIWGNHSST QYPDLHHTLV AGKPAMEAEG VDASWYESDF IPTVQQRGAA IIKARGASSA
     ASAASAAIDH IRDWALGTDG DDWVSMAVPS DGSYGIEPGV IYSFPCTCEN GQWSIVQGLE
     INEFSRARMD ATDQELREER AAVESLL
//
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