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Database: UniProt/TrEMBL
Entry: I6WQF8_PSEPQ
LinkDB: I6WQF8_PSEPQ
Original site: I6WQF8_PSEPQ 
ID   I6WQF8_PSEPQ            Unreviewed;       340 AA.
AC   I6WQF8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   05-JUL-2017, entry version 37.
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:AFN45346.1};
GN   Synonyms=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   OrderedLocusNames=HMPREF9154_2106 {ECO:0000313|EMBL:AFN45346.1};
OS   Pseudopropionibacterium propionicum (strain F0230a) (Propionibacterium
OS   propionicum).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Pseudopropionibacterium.
OX   NCBI_TaxID=767029 {ECO:0000313|EMBL:AFN45346.1, ECO:0000313|Proteomes:UP000003118};
RN   [1] {ECO:0000313|Proteomes:UP000003118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0230a {ECO:0000313|Proteomes:UP000003118};
RA   Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "The complete genome of chromosome of Propionibacterium propionicum
RT   F0230a.";
RL   Submitted (JUL-2012) 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; CP002734; AFN45346.1; -; Genomic_DNA.
DR   ProteinModelPortal; I6WQF8; -.
DR   EnsemblBacteria; AFN45346; AFN45346; HMPREF9154_2106.
DR   KEGG; ppc:HMPREF9154_2106; -.
DR   PATRIC; fig|767029.3.peg.2048; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000003118; 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:UP000003118};
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:AFN45346.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003118};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN       18    162       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      168    336       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      24     30       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     141    143       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    199    199       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING     104    104       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     110    110       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     117    117       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     124    124       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     143    143       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     174    174       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   340 AA;  36252 MW;  06B73332C6D9C9EE CRC64;
     MDITVERKVR TMSTEAPVKI AVTGAAGQIC YSLLFRIASG SLLGDRPIEL RLLEITPALK
     ALEGVVMELD DCAFPNLKNV VIGDDPKKVF DGVNLAMLVG AMPRKAGMER GDLLSANGAI
     FTAQGKALNE VAADDVRVLV TGNPANTNAL IASSNAPDIP KERFNALTRL DHNRAKSQLA
     QKLGCPVEEI KKMTIWGNHS STQYPDIFHA EVGGKNAAGL VNDEAWIEST FIPTVAKRGA
     AIIEARGLSS AASAANATVE HMRDWVLGTP DGDWVSMAIP SDGSYGVAEG VISSFPCVVK
     NGKYEIVQGL EIDPFSRTKI DASVAELLDE RKAVKELGLI
//
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