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Database: UniProt/TrEMBL
Entry: A0A1B1YWB8_9GAMM
LinkDB: A0A1B1YWB8_9GAMM
Original site: A0A1B1YWB8_9GAMM 
ID   A0A1B1YWB8_9GAMM        Unreviewed;       325 AA.
AC   A0A1B1YWB8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
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=PG2T_13255 {ECO:0000313|EMBL:ANX05046.1};
OS   Immundisolibacter cernigliae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Immundisolibacterales;
OC   Immundisolibacteraceae; Immundisolibacter.
OX   NCBI_TaxID=1810504 {ECO:0000313|EMBL:ANX05046.1, ECO:0000313|Proteomes:UP000092952};
RN   [1] {ECO:0000313|Proteomes:UP000092952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TR3.2 {ECO:0000313|Proteomes:UP000092952};
RA   Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.;
RT   "Complete genome sequence of Solimmundus cernigliae, representing a
RT   novel lineage of polycyclic aromatic hydrocarbon degraders within the
RT   Gammaproteobacteria.";
RL   Submitted (MAR-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP014671; ANX05046.1; -; Genomic_DNA.
DR   RefSeq; WP_068806447.1; NZ_CP014671.1.
DR   EnsemblBacteria; ANX05046; ANX05046; PG2T_13255.
DR   KEGG; gbi:PG2T_13255; -.
DR   KO; K00024; -.
DR   Proteomes; UP000092952; 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; 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:UP000092952};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092952};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        5    145       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    321       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
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   325 AA;  34763 MW;  0E3211AF2DB6337C CRC64;
     MNKPVRIAVT GCAGNIGYAL LFRIAAGDML GPDQPVILHL LEVTPALKAL EGVSMELRDC
     AFPLLADIVA TDDPAVGFKD ADYAILVGAR PRGPGMERKD LLEANGAIFT VQGKALNDHA
     SRGVKVLVVG NPANTNALIA MRSAPDLDPR QFTAMMRLDH NRAISQLAAK TGSTVPAIRR
     MTVWGNHSST QYPDISHTLV DGRPAPELVD QAWLETDFIP TVQQRGAAII AARGASSAAS
     AASAAIDHMR TWALGTADGD WVSMGIPSDG SYGIPEGIIY SYPVTCRDGR YEIVQNLPVS
     AFSRARMDAT ARELLEEREA VQHLL
//
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