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Database: UniProt/TrEMBL
Entry: S4YWF6_9GAMM
LinkDB: S4YWF6_9GAMM
Original site: S4YWF6_9GAMM 
ID   S4YWF6_9GAMM            Unreviewed;       329 AA.
AC   S4YWF6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   31-JAN-2018, entry version 34.
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=PSYCG_11080 {ECO:0000313|EMBL:AGP49694.1};
OS   Psychrobacter sp. G.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=571800 {ECO:0000313|EMBL:AGP49694.1, ECO:0000313|Proteomes:UP000014806};
RN   [1] {ECO:0000313|EMBL:AGP49694.1, ECO:0000313|Proteomes:UP000014806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G {ECO:0000313|EMBL:AGP49694.1};
RX   PubMed=24051316;
RA   Che S., Song L., Song W., Yang M., Liu G., Lin X.;
RT   "Complete Genome Sequence of Antarctic Bacterium Psychrobacter sp.
RT   Strain G.";
RL   Genome Announc. 1:e00725-13(2013).
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; CP006265; AGP49694.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGP49694; AGP49694; PSYCG_11080.
DR   KEGG; pso:PSYCG_11080; -.
DR   PATRIC; fig|571800.3.peg.2181; -.
DR   KO; K00024; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000014806; 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:UP000014806};
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, ECO:0000313|EMBL:AGP49694.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        7    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;  35171 MW;  A75216D5B30C1CBC CRC64;
     MSMKQPVRVA VTGAAGNISY AMLFRIASGE MLGKDQPVIL QLLEIAPALD ALKGVVMELE
     DCAFPLLAGV VQTDDATVAF KDVDYALLVG SRPRGPGMER KDLLEANAAI FSAQGKALND
     VASRDVKVLV VGNPANTNAV IAQRNAPDLD PRNFTAMTRL DHNRAMAQLA GKTDSTVNDL
     KKMIIWGNHS STQYPDLTAS TVNGKPALDL VDRAWYEGTY IPEVQQRGAA IIKARGASSA
     ASAANAAIAH VRTWVMGTDE NDWVSMGVYS NGEYGIAKGL IYSFPVTCAN GDWSIVDGVD
     VSSDFSKEKM AATEQELSEE RDAVAHLLP
//
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