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D3PQL0 (D3PQL0_MEIRD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. SAAS SAAS010945 RuleBase RU000422 HAMAP-Rule MF_01517

Subunit structure

Homodimer By similarity. SAAS SAAS010945 HAMAP-Rule MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family. RuleBase RU000421 HAMAP-Rule MF_01517

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding11 – 177NAD By similarity HAMAP-Rule MF_01517
Nucleotide binding129 – 1313NAD By similarity HAMAP-Rule MF_01517

Sites

Active site1871Proton acceptor By similarity HAMAP-Rule MF_01517
Binding site921Substrate By similarity HAMAP-Rule MF_01517
Binding site981Substrate By similarity HAMAP-Rule MF_01517
Binding site1051NAD By similarity HAMAP-Rule MF_01517
Binding site1121NAD By similarity HAMAP-Rule MF_01517
Binding site1311Substrate By similarity HAMAP-Rule MF_01517
Binding site1621Substrate By similarity HAMAP-Rule MF_01517

Sequences

Sequence LengthMass (Da)Tools
D3PQL0 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: C57E56BF6A0CC7DB

FASTA32935,340
        10         20         30         40         50         60 
MKPPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPVILQL LEITPALKAL GGVIMELEDC 

        70         80         90        100        110        120 
AFPTLAGIVA TDDPNIAFGD ADYALLVGAM PRKQGMERAD LLQANGAIFT AQGRALSENA 

       130        140        150        160        170        180 
RKHVKVLVVG NPANTNALIT YKNAPNLSPR QIHAMTRLDH NRAISQLAAR LKVPVSEIKK 

       190        200        210        220        230        240 
MTIWGNHSLT QYPDLFHCEV GGRNAYELVG DHDWYANTYI PKVAKRGAEI IEARGASSAA 

       250        260        270        280        290        300 
SAASAAIDHM RDWALGTPAG DWVSMAIPSD GSYGIPEGLV YSYPCVCKDG DFEIVQGLEI 

       310        320 
NEFSRSKMDA SAKELADERD AVLQLGLIK 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Meiothermus ruber type strain (21)."
Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A., Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Fahnrich R., Goodwin L. expand/collapse author list , Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.
Stand. Genomic Sci. 3:26-36(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35948 / DSM 1279 / VKM B-1258 / 21.
[2]"Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT Sequencing Data."
Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J., Eichler E., Turner S.W.
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 1279 EMBL AGK04208.1.
[3]Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 1279 EMBL AGK04208.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001743 Genomic DNA. Translation: ADD27743.1.
CP005385 Genomic DNA. Translation: AGK04208.1.
RefSeqYP_003506763.1. NC_013946.1.
YP_007879705.1. NC_021081.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADD27743; ADD27743; Mrub_0978.
AGK04208; AGK04208; K649_04530.
GeneID15335518.
8879066.
KEGGmrb:Mrub_0978.
mre:K649_04530.
PATRIC35358092. VBIMeiRub128672_0983.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000220953.
KOK00024.
OMANICLYDP.

Enzyme and pathway databases

BioCycMRUB504728:GI6U-1000-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD3PQL0_MEIRD
AccessionPrimary (citable) accession number: D3PQL0
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)