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Database: UniProt/TrEMBL
Entry: A0A0F7W071_9ACTN
LinkDB: A0A0F7W071_9ACTN
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ID   A0A0F7W071_9ACTN        Unreviewed;       329 AA.
AC   A0A0F7W071;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-SEP-2017, entry version 20.
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=sle_28550 {ECO:0000313|EMBL:CQR62316.1};
GN   Synonyms=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
OS   Streptomyces leeuwenhoekii.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1437453 {ECO:0000313|EMBL:CQR62316.1, ECO:0000313|Proteomes:UP000035016};
RN   [1] {ECO:0000313|EMBL:CQR62316.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C34 {ECO:0000313|EMBL:CQR62316.1};
RA   Gomez-Escribano Juan Pablo;
RL   Submitted (FEB-2015) 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: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; LN831790; CQR62316.1; -; Genomic_DNA.
DR   RefSeq; WP_029385221.1; NZ_LN831790.1.
DR   KEGG; sle:sle_28550; -.
DR   PATRIC; fig|1437453.5.peg.3372; -.
DR   KO; K00024; -.
DR   Proteomes; UP000035016; Chromosome 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; 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:UP000035016};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU004066};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        7    147       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    322       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      12     18       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     130    132       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    188    188       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      93     93       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      99     99       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     106    106       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     113    113       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     132    132       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     163    163       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   329 AA;  34808 MW;  3DB3360226717E5D CRC64;
     MTRTPVNVTV TGAAGQIGYA LLFRIASGQL LGADVPVKLR LLEITPALKA AEGTAMELDD
     CAFPLLQGIE ITDDPNVAFD GANVALLVGA RPRTKGMERG DLLEANGGIF KPQGKAINDH
     AADDIRVLVV GNPANTNALI AQAAAPDVPA ERFTAMTRLD HNRALTQLAK KTGSTVADIK
     RLTIWGNHSA TQYPDIFHAT VAGKNAAEVV NDEKWLAEDF IPTVAKRGAA IIEARGASSA
     ASAANAAIDH VYSWVNGTPE GDWVSMGIPS DGSYGVPEGL ISSFPVTCKD GKYEIVQGLE
     INEFSRTRID ASVKELEEER EAVRGLGLI
//
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