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Database: UniProt
Entry: B0BC10
LinkDB: B0BC10
Original site: B0BC10 
ID   MDH_CHLTB               Reviewed;         326 AA.
AC   B0BC10;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   01-OCT-2014, entry version 52.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517};
GN   OrderedLocusNames=CTLon_0628;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J.,
RA   Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H.,
RA   Harris B., Ormond D., Rance R., Quail M.A., Parkhill J.,
RA   Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR   EMBL; AM884177; CAP07025.1; -; Genomic_DNA.
DR   RefSeq; YP_001653716.1; NC_010280.2.
DR   ProteinModelPortal; B0BC10; -.
DR   STRING; 471473.CTLon_0628; -.
DR   EnsemblBacteria; CAP07025; CAP07025; CTLon_0628.
DR   GeneID; 5859030; -.
DR   KEGG; ctl:CTLon_0628; -.
DR   PATRIC; 20382909; VBIChlTra68089_0682.
DR   eggNOG; COG0039; -.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; AFSQECI; -.
DR   OrthoDB; EOG6PP9Q2; -.
DR   BioCyc; CTRA471473:GHJK-660-MONOMER; -.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044262; P:cellular 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   Gene3D; 3.40.50.720; -; 1.
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; 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; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    326       Malate dehydrogenase.
FT                                /FTId=PRO_1000191617.
FT   NP_BIND      12     18       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   NP_BIND     130    132       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    188    188       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      93     93       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      99     99       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     106    106       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     113    113       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     132    132       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     163    163       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
SQ   SEQUENCE   326 AA;  35561 MW;  20EE90A99BBF351F CRC64;
     MVSQTVSVAV TGGTGQIAYS FLFSLAHGDV FGLDCGIDLR IYDIPGTERA LSGVRMELDD
     GAFPLLQRVQ VTTSLHDAFD GIDAAFLIGS VPRGPGMERR DLLKKNGEIV ATQGKALNTT
     AKRDAKIFVV GNPVNTNCWI AMNHAPRLLR KNFHAMLRLD QNRMHSMLSH RAEVPLSAVS
     QVVVWGNHSA KQVPDFTQAL INDRPIAETI ADRDWLENIM VPSVQSRGSA VIEARGKSSA
     ASAARALAEA ARSIYQPKEG EWFSSGVCSD HNPYGLPEDL IFGFPCRMLA TGEYEVIPGL
     PWDAFIRGKM QISLDEILQE KASVSL
//
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