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Database: UniProt/TrEMBL
Entry: A0A1P8PMP7_9GAMM
LinkDB: A0A1P8PMP7_9GAMM
Original site: A0A1P8PMP7_9GAMM 
ID   A0A1P8PMP7_9GAMM        Unreviewed;       328 AA.
AC   A0A1P8PMP7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   25-OCT-2017, entry version 5.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517,
GN   ECO:0000313|EMBL:APX63793.1};
GN   ORFNames=AsACE_CH02435 {ECO:0000313|EMBL:APX63793.1};
OS   Acinetobacter schindleri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=108981 {ECO:0000313|EMBL:APX63793.1};
RN   [1] {ECO:0000313|EMBL:APX63793.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ACE {ECO:0000313|EMBL:APX63793.1};
RA   Sigala J.C., Suarez B.P., Lara A., Le Borgne S., Bustos P.,
RA   Santamaria R.I., Gonzalez V., Martinez A.;
RT   "Genomic and physiological characterization of an Acinetobacter
RT   schindleri strain isolated from the laboratory that catabolizes
RT   acetate fast and efficiently.";
RL   Submitted (MAY-2016) 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|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; CP015615; APX63793.1; -; Genomic_DNA.
DR   RefSeq; WP_004809714.1; NZ_CP015615.1.
DR   GeneID; 25067987; -.
DR   KEGG; asj:AsACE_CH02435; -.
DR   KO; K00024; -.
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; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000313|EMBL:APX63793.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        5    154       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      159    322       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       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}.
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}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   328 AA;  35338 MW;  39A1B4324146A3F0 CRC64;
     MKQPVRVAVT GAAGQIGYSL LFRIASGEML GKDQPVILQL LEIPVEKAQQ ALKGVMMELD
     DCAFPLLAGM IGTDDPKVAF KDADYALLVG SRPRGPGMER ADLLKVNGEI FIGQGQALNE
     VASRDVKVLV VGNPANTNAY IAMKSAPDLP AKNFTAMLRL DHNRALTQLA QKAGVAVSDI
     ENMTVWGNHS PTMYADYRFA NVNGESLKDK INDAAWNKDV FLPTVGKRGA AIIEARGLSS
     AASAANAAID HMRDWALGTN GKWVTMGIPS DGSYGIPEGV MFGFPVTTEN GEYKIVQGLE
     IDEFSRERIN VTLNELEEER AAVADMLN
//
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