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Database: UniProt/TrEMBL
Entry: A0A1D9LKH7_9NEIS
LinkDB: A0A1D9LKH7_9NEIS
Original site: A0A1D9LKH7_9NEIS 
ID   A0A1D9LKH7_9NEIS        Unreviewed;       326 AA.
AC   A0A1D9LKH7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-SEP-2017, entry version 6.
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   ORFNames=BKX93_18380 {ECO:0000313|EMBL:AOZ51766.1};
OS   Chromobacterium vaccinii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=1108595 {ECO:0000313|EMBL:AOZ51766.1, ECO:0000313|Proteomes:UP000178776};
RN   [1] {ECO:0000313|EMBL:AOZ51766.1, ECO:0000313|Proteomes:UP000178776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21-1 {ECO:0000313|EMBL:AOZ51766.1,
RC   ECO:0000313|Proteomes:UP000178776};
RA   Sparks M.E., Blackburn M.B., Gundersen-Rindal D.E., Mitchell A.,
RA   Farrar R., Kuhar D.;
RT   "Chromobacterium muskegensis sp. nov., an insecticidal bacterium
RT   isolated from Sphagnum bogs.";
RL   Submitted (OCT-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; CP017707; AOZ51766.1; -; Genomic_DNA.
DR   RefSeq; WP_046155359.1; NZ_JZJL01000002.1.
DR   KEGG; cvc:BKX93_18380; -.
DR   KO; K00024; -.
DR   Proteomes; UP000178776; 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   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; IPR016040; NAD(P)-bd_dom.
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   Complete proteome {ECO:0000313|Proteomes:UP000178776};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        5    152       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    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}.
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}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   326 AA;  35014 MW;  7630B009B5F2606F CRC64;
     MKAPVRVAVT GAAGQIGYSL LFRIASGEML GKDQPVILHL LDLPQAQTAL KGVMMELEDC
     AFPLLAGMVA TDDPNVAFKD VKVALLVGAR PRSKGMERKD LLEANGAIFT VQGKALNDHA
     ARDVKVLVVG NPANTNAWIA MKSAPDLDPK NFTAMLRLDH NRALSQIAAK TGKPVAAIEK
     LAVWGNHSPT MYADYRFATI DGQSVKTLIN DDVWNRDVFL PTVGKRGAAI IEARGLSSAA
     SAANAAIDHI HDWVLGSNGK WVTMGIPSDG SYGIPEGVMY GVPVVCENGE YKRVEGLEID
     AFSRERMDLT LAELEEERAA IAHLFG
//
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