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Database: UniProt/TrEMBL
Entry: A0A1D9D1R2_9GAMM
LinkDB: A0A1D9D1R2_9GAMM
Original site: A0A1D9D1R2_9GAMM 
ID   A0A1D9D1R2_9GAMM        Unreviewed;       329 AA.
AC   A0A1D9D1R2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   23-MAY-2018, entry version 15.
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=AOT82_2344 {ECO:0000313|EMBL:AOY44723.1};
OS   Psychrobacter sp. AntiMn-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=1720344 {ECO:0000313|EMBL:AOY44723.1, ECO:0000313|Proteomes:UP000178238};
RN   [1] {ECO:0000313|EMBL:AOY44723.1, ECO:0000313|Proteomes:UP000178238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AntiMn-1 {ECO:0000313|EMBL:AOY44723.1,
RC   ECO:0000313|Proteomes:UP000178238};
RA   Millard Andrew;
RL   Submitted (OCT-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; CP012969; AOY44723.1; -; Genomic_DNA.
DR   KEGG; psya:AOT82_2344; -.
DR   KO; K00024; -.
DR   Proteomes; UP000178238; 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:UP000178238};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU004066};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        8    154       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      158    325       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      13     19       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     131    133       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    189    189       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      94     94       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     107    107       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     114    114       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     133    133       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   329 AA;  35433 MW;  F5D9516C6371345A CRC64;
     MSMKQPLRVA VTGAAGNISY AMLFRIASGE MLGKDQPVIL QLLEITPALD ALKGVVMELE
     DCAFPLLAGI VQTDDANVAF KDADYALLVG ARPRGPGMER KDLLEANAAI FSAQGKALNE
     VASRDVKVLV VGNPANTNAL IAQRNAPDLD PRNFTAMTRL DHNRAMAQLA EKTDSTVNDI
     KNMTIWGNHS STQYPDLTAA TVNGKPALEL VDRDWYENTY IPEVQQRGAA IIKARGASSA
     ASAANAAIAH MRTWALGTDE NDWVSMGVYS NGEYGIAEGL IYSFPCTCKN GDWSIVDGVD
     VSSEFSKEKM AATEQELSEE RDAVAHLLP
//
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