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Database: UniProt/TrEMBL
Entry: A0A0D5LZU6_9GAMM
LinkDB: A0A0D5LZU6_9GAMM
Original site: A0A0D5LZU6_9GAMM 
ID   A0A0D5LZU6_9GAMM        Unreviewed;       324 AA.
AC   A0A0D5LZU6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-NOV-2017, entry version 25.
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=KO116_00954 {ECO:0000313|EMBL:AJY49451.1};
OS   Halomonas sp. KO116.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY49451.1, ECO:0000313|Proteomes:UP000028645};
RN   [1] {ECO:0000313|EMBL:AJY49451.1, ECO:0000313|Proteomes:UP000028645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KO116 {ECO:0000313|EMBL:AJY49451.1,
RC   ECO:0000313|Proteomes:UP000028645};
RX   PubMed=25953187;
RA   O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D.,
RA   Hazen T.C.;
RT   "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-
RT   Tolerant Marine Bacterium Isolated from a Lignin-Enriched Seawater
RT   Microcosm.";
RL   Genome Announc. 3:0-0(2015).
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; CP011052; AJY49451.1; -; Genomic_DNA.
DR   RefSeq; WP_022519687.1; NZ_CP011052.1.
DR   EnsemblBacteria; AJY49451; AJY49451; KO116_00954.
DR   KEGG; hak:KO116_00954; -.
DR   KO; K00024; -.
DR   Proteomes; UP000028645; 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:UP000028645};
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   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    143       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      156    319       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   324 AA;  34911 MW;  BA670C24FE2AD643 CRC64;
     MKDPVRIAIT GGAGQISYSL IFRIAAGDML GPDQPVILQL LEIPQAMDAL NGVVMEVNDC
     AFPLVQDIVA TDDPNVAFKD ADFALLVGAR PRGPGMERKD LLEANAAIFS VQGKALNDHA
     SRDVKVLVVG NPANTNALIA SCNAPDLDAG QFTAMTRLDH NRALTQLAQK TGKHVTDVEN
     MIIWGNHSAT QYPDLAQCKV DGKAAFDLVE RDWYENDFIP TVQQRGAAII KARGASSAAS
     AASSAIDHMH DWALGSKGIV SMAIPSDGSY GIDEGIIYSY PVRCQGGKYE IVQGFEIDEF
     SQEKMKATEK ELREERAAVE HLLG
//
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