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Database: UniProt/TrEMBL
Entry: A0A120JVP0_9GAMM
LinkDB: A0A120JVP0_9GAMM
Original site: A0A120JVP0_9GAMM 
ID   A0A120JVP0_9GAMM        Unreviewed;       324 AA.
AC   A0A120JVP0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUL-2017, entry version 13.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh_1 {ECO:0000313|EMBL:AMC99780.1};
GN   Synonyms=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=LOKO_00699 {ECO:0000313|EMBL:AMC99780.1};
OS   Halomonas chromatireducens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=507626 {ECO:0000313|EMBL:AMC99780.1, ECO:0000313|Proteomes:UP000063387};
RN   [1] {ECO:0000313|EMBL:AMC99780.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMC99780.1,
RC   ECO:0000313|Proteomes:UP000063387};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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|RuleBase:RU000422,
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; CP014226; AMC99780.1; -; Genomic_DNA.
DR   RefSeq; WP_066445074.1; NZ_CP014226.1.
DR   EnsemblBacteria; AMC99780; AMC99780; LOKO_00699.
DR   KEGG; hco:LOKO_00699; -.
DR   PATRIC; fig|507626.3.peg.689; -.
DR   KO; K00024; -.
DR   Proteomes; UP000063387; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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; 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.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000063387};
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, ECO:0000313|EMBL:AMC99780.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063387};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    145       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}.
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   324 AA;  35019 MW;  DDD900277A0D451A CRC64;
     MKDPVRIAIT GGAGQISYSL IFRIAAGDML GPDQPVILQL LEITPAMDAL NGVVMEVNDC
     AFPLVQDIVA TDDPNVAFKD ADFALLVGAR PRGPGMERKD LLEANAAIFS VQGKALNDNA
     SRDVRVLVVG NPANTNALIA SCNAPDLSPR HFTAMTRLDH NRALTQLAQK TGKRVTDVEN
     MIIWGNHSAT QYPDLAHTKV DGKPAFDLVE RDWYENTFIP DVQQRGAAII KARGASSAAS
     AASSAIDHMR DWALGTDGVV SMAIPSDGSY GIEKGIIYSY PVRCQNGDYE IVQGLEVDDF
     SRGRMKATED ELREERAAVE HLLG
//
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