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Database: UniProt/TrEMBL
Entry: A0A167A2T2_9GAMM
LinkDB: A0A167A2T2_9GAMM
Original site: A0A167A2T2_9GAMM 
ID   A0A167A2T2_9GAMM        Unreviewed;       326 AA.
AC   A0A167A2T2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-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=ECTOBSL9_0512 {ECO:0000313|EMBL:ANB01407.1};
OS   Ectothiorhodospira sp. BSL-9.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=1442136 {ECO:0000313|EMBL:ANB01407.1, ECO:0000313|Proteomes:UP000076772};
RN   [1] {ECO:0000313|EMBL:ANB01407.1, ECO:0000313|Proteomes:UP000076772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSL-9 {ECO:0000313|EMBL:ANB01407.1,
RC   ECO:0000313|Proteomes:UP000076772};
RA   Saltikov C., Conrad A., Hernandez J., Stoneburner B., Oremland R.,
RA   Rosen M., Miller L., McCann-Hoeft S., Pourmand N., Bernick D.;
RT   "The arx anaerobic arsenite-oxidization pathway is conserved in
RT   Halomonas and Ectothiorhodospira strains isolated from Big Soda Lake,
RT   Nevada.";
RL   Submitted (JUN-2015) 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; CP011994; ANB01407.1; -; Genomic_DNA.
DR   RefSeq; WP_063463742.1; NZ_CP011994.1.
DR   EnsemblBacteria; ANB01407; ANB01407; ECTOBSL9_0512.
DR   KEGG; ebs:ECTOBSL9_0512; -.
DR   PATRIC; fig|1442136.6.peg.514; -.
DR   KO; K00024; -.
DR   Proteomes; UP000076772; 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   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:UP000076772};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU004066, ECO:0000313|EMBL:ANB01407.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    152       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      156    320       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   326 AA;  34927 MW;  7AD671D916C4220C CRC64;
     MKNPMRVAVT GAAGQISYSL LFRIASGDML GKDQPVILQL LEITPAMDAL RGVVMELEDC
     AFPLVAGITT SDKPEVAFDK ADVALLVGAR PRGPGMERKD LLEANAAIFS EQGKALNAVA
     SRDVKVLVVG NPANTNSLIA QRNAPDLNPR NFTAMTRLDH NRALAQLAGK TGASTTDIKK
     MIIWGNHSAT QYPDISQAMV KGDAASGLVP RDWYESDFIP TVQQRGAAII KARGASSAAS
     AGSSAVDHIR DWVMGTPDGD WVSMAVPSDG SYGIEKGLIY SFPVTCKGGD YSIVQGLEID
     DFSRERMQVT EQELREERDG VAHLLP
//
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