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Database: UniProt/TrEMBL
Entry: A0A089X848_STRGA
LinkDB: A0A089X848_STRGA
Original site: A0A089X848_STRGA 
ID   A0A089X848_STRGA        Unreviewed;       329 AA.
AC   A0A089X848;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   20-JUN-2018, entry version 34.
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   ECO:0000313|EMBL:AIS00103.1};
GN   ORFNames=SGLAU_20745 {ECO:0000313|EMBL:AIS00103.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIS00103.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA.O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces
RT   glaucescens GLA.O (DSM 40922) consisting of a linear chromosome and
RT   one linear plasmid.";
RL   J. Biotechnol. 194:81-83(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: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; CP009438; AIS00103.1; -; Genomic_DNA.
DR   RefSeq; WP_043503481.1; NZ_CP009438.1.
DR   EnsemblBacteria; AIS00103; AIS00103; SGLAU_20745.
DR   GeneID; 33992960; -.
DR   KEGG; sgu:SGLAU_20745; -.
DR   KO; K00024; -.
DR   Proteomes; UP000029482; 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:UP000029482};
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, ECO:0000313|EMBL:AIS00103.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029482};
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    323       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, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
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, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     163    163       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   329 AA;  34708 MW;  2B0058578F0A098F CRC64;
     MTRTPVNVTV TGAAGQIGYA LLFRIASGQL LGADVPVRLR LLEITPALKA AEGTAMELDD
     CAFPLLQGID ITDDPNVAFD GANVALLVGA RPRTKGMERG DLLEANGGIF KPQGQAINAH
     AADDIKVLVV GNPANTNALI AQAAAPDVPA ERFTAMTRLD HNRALTQLAK KTGSTVSDIK
     RLTIWGNHSA TQYPDIFHAT IGGKNAAEVV NDEQWLADDF IPTVAKRGAA IIEARGASSA
     ASAANAAIDH VYSWVNGTPE GDWVSMGIPS DGSYGVPEGL ISSFPVTCKD GKYEIVQGLE
     INEFSRTRID ASVQELAEER EAVRALGLI
//
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