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Database: UniProt/TrEMBL
Entry: R4VM77_9GAMM
LinkDB: R4VM77_9GAMM
Original site: R4VM77_9GAMM 
ID   R4VM77_9GAMM            Unreviewed;       326 AA.
AC   R4VM77;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   05-JUL-2017, entry version 31.
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 {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=SPISAL_07340 {ECO:0000313|EMBL:AGM41562.1};
OS   Spiribacter salinus M19-40.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Spiribacter.
OX   NCBI_TaxID=1260251 {ECO:0000313|EMBL:AGM41562.1, ECO:0000313|Proteomes:UP000017881};
RN   [1] {ECO:0000313|EMBL:AGM41562.1, ECO:0000313|Proteomes:UP000017881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M19-40 {ECO:0000313|EMBL:AGM41562.1};
RX   PubMed=23409269;
RA   Leon M.J., Ghai R., Fernandez A.B., Sanchez-Porro C.,
RA   Rodriguez-Valera F., Ventosa A.;
RT   "Draft Genome of Spiribacter salinus M19-40, an Abundant
RT   Gammaproteobacterium in Aquatic Hypersaline Environments.";
RL   Genome Announc. 1:E00179-12(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: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; CP005963; AGM41562.1; -; Genomic_DNA.
DR   RefSeq; WP_016353869.1; NC_021291.1.
DR   ProteinModelPortal; R4VM77; -.
DR   EnsemblBacteria; AGM41562; AGM41562; SPISAL_07340.
DR   KEGG; ssal:SPISAL_07340; -.
DR   PATRIC; fig|1260251.3.peg.1484; -.
DR   KO; K00024; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000017881; 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:UP000017881};
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:AGM41562.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017881};
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    322       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;  34962 MW;  880C145FA38019D7 CRC64;
     MKAPVRVAVT GAAGQIGYSL LFRIASGDML GPDQPVILQL LEVPPAMDAV QGVVMELDDC
     AFPLVAGLQA TDQAEEAFKD ADYILLVGAK PRGPGMERKD LLEANAAIFS AQGKAMNDVA
     SRNVRVLAVG NPANTNALIA QRNAPDLDPN CFTAMTRLDH NRALAQLANR TGQHVTDIQQ
     LTIWGNHSAT QYPDISHAQV DGKAASDLVD QSWLEESFIP TVQQRGAAII KARGQSSAAS
     AASAAIDHMR DWTLGTPQGD WVSMAIPSDG SYGIAEGIIY SFPVRCANGQ YQIVQGLDIS
     DFSRERMSAT EQELIEERDA VEHLLP
//
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