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Database: UniProt/TrEMBL
Entry: A0A0G9HF73_9GAMM
LinkDB: A0A0G9HF73_9GAMM
Original site: A0A0G9HF73_9GAMM 
ID   A0A0G9HF73_9GAMM        Unreviewed;       327 AA.
AC   A0A0G9HF73;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 17.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=BJI69_15735 {ECO:0000313|EMBL:APG05205.1}, Y883_05385
GN   {ECO:0000313|EMBL:KLD67829.1};
OS   Luteibacter rhizovicinus DSM 16549.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1440763 {ECO:0000313|EMBL:KLD67829.1, ECO:0000313|Proteomes:UP000035585};
RN   [1] {ECO:0000313|EMBL:KLD67829.1, ECO:0000313|Proteomes:UP000035585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD67829.1,
RC   ECO:0000313|Proteomes:UP000035585};
RX   PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA   Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E.,
RA   Gupta R.S.;
RT   "A phylogenomic and molecular marker based taxonomic framework for the
RT   order Xanthomonadales: proposal to transfer the families Algiphilaceae
RT   and Solimonadaceae to the order Nevskiales ord. nov. and to create a
RT   new family within the order Xanthomonadales, the family
RT   Rhodanobacteraceae fam. nov., containing the genus Rhodanobacter and
RT   its closest relatives.";
RL   Antonie Van Leeuwenhoek 107:467-485(2015).
RN   [2] {ECO:0000313|EMBL:APG05205.1, ECO:0000313|Proteomes:UP000182987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LJ96T {ECO:0000313|EMBL:APG05205.1,
RC   ECO:0000313|Proteomes:UP000182987};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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|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; CP017480; APG05205.1; -; Genomic_DNA.
DR   EMBL; JPLB01000017; KLD67829.1; -; Genomic_DNA.
DR   RefSeq; WP_046966726.1; NZ_JPLB01000017.1.
DR   EnsemblBacteria; KLD67829; KLD67829; Y883_05385.
DR   KEGG; lrz:BJI69_15735; -.
DR   PATRIC; fig|1440763.5.peg.782; -.
DR   KO; K00024; -.
DR   Proteomes; UP000035585; Unassembled WGS sequence.
DR   Proteomes; UP000182987; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000035585,
KW   ECO:0000313|Proteomes:UP000182987};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000313|EMBL:KLD67829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035585};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        5    149       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    319       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     105    105       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   327 AA;  34976 MW;  007F2D0D7D5B320A CRC64;
     MKAPVRVAVT GAAGQIGYAL LFRIAAGDML GPDQPVILHL LEITPALPTL QGVVMELNDC
     AFPTLAGIVA TDDVNVAFKD VDYALLVGAR PRGPGMERKD LLEANGAIFG PQGKALNDHA
     KRDVRVLVVG NPANTNALIA QQNAPDLDPK CFTAMVRLDH NRALSQLAEK TGTHSTDIKK
     LTIWGNHSST QYPDLHQTTV KGKAALEQVD QAWYESDFIP TVQQRGAAII KARGASSAAS
     AASAAIDHMR DWTLGTAEGD WVSMGIPSDG SYGVEKGVIF GYPVTVKNGK YAIVQGLEIN
     AFSQARIDAT EKELREERAG VEHLFAK
//
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