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-MAY-2013, entry version 46.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
GN Name=mdh; 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
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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; AINDHAA; -.
DR ProtClustDB; PRK05442; -.
DR BioCyc; CTRA471473:GHJK-628-MONOMER; -.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:HAMAP.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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: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; Lactate_DH/Glyco_hydro_4_C; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR PROSITE; PS00068; MDH; FALSE_NEG.
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 (By similarity).
FT NP_BIND 130 132 NAD (By similarity).
FT ACT_SITE 188 188 Proton acceptor (By similarity).
FT BINDING 93 93 Substrate (By similarity).
FT BINDING 99 99 Substrate (By similarity).
FT BINDING 106 106 NAD (By similarity).
FT BINDING 113 113 NAD (By similarity).
FT BINDING 132 132 Substrate (By similarity).
FT BINDING 163 163 Substrate (By similarity).
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
//
