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Database: UniProt/TrEMBL
Entry: A0A1A9J127_9ACTN
LinkDB: A0A1A9J127_9ACTN
Original site: A0A1A9J127_9ACTN 
ID   A0A1A9J127_9ACTN        Unreviewed;       329 AA.
AC   A0A1A9J127;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-NOV-2017, entry version 13.
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=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=A8713_19320 {ECO:0000313|EMBL:ANH93050.1};
OS   Streptomyces sp. SAT1.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1849967 {ECO:0000313|EMBL:ANH93050.1, ECO:0000313|Proteomes:UP000078022};
RN   [1] {ECO:0000313|EMBL:ANH93050.1, ECO:0000313|Proteomes:UP000078022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAT1 {ECO:0000313|EMBL:ANH93050.1,
RC   ECO:0000313|Proteomes:UP000078022};
RA   Dou G.;
RT   "Complete genome of endophytic Streptomyces sp.";
RL   Submitted (MAY-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: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; CP015849; ANH93050.1; -; Genomic_DNA.
DR   RefSeq; WP_064534795.1; NZ_CP015849.1.
DR   EnsemblBacteria; ANH93050; ANH93050; A8713_19320.
DR   GeneID; 32626505; -.
DR   KEGG; strt:A8713_19320; -.
DR   KO; K00024; -.
DR   Proteomes; UP000078022; 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:UP000078022};
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};
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;  34613 MW;  094A2A8E3683E6FB CRC64;
     MTRTPVNVTV TGAAGQIGYA LLFRIASGQL LGADVPVKLR LLEITPALKA AEGTAMELDD
     CAFPLLQGID ISDDPNVAFD GTNVALLVGA RPRTKGMERG DLLEANGGIF KPQGKAINDH
     AADDVKVLVV GNPANTNALI AQAAAPDVPA ERFTAMTRLD HNRALTQLAK KTGTTVADIK
     RLTIWGNHSA TQYPDIFHAT VAGKNAAETV NDEKWLAEDF IPTVAKRGAA IIEARGASSA
     ASAANAAIDH VHTWVNGTAE GDWVSMGIPS DGSYGVPEGL ISSFPVTTKD GAYEIVQGLE
     INEFSRARID ASVQELAEER EAVRALGLI
//
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