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A4SFT4 (MDH_PROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

malate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000081364

Regions

Nucleotide binding7 – 126NAD By similarity
Nucleotide binding117 – 1193NAD By similarity

Sites

Active site1741Proton acceptor By similarity
Binding site321NAD By similarity
Binding site811Substrate By similarity
Binding site871Substrate By similarity
Binding site941NAD By similarity
Binding site1191Substrate By similarity
Binding site1501Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SFT4 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: F637E23B541A2A27

FASTA30932,966
        10         20         30         40         50         60 
MKITVIGAGH VGATAALRIA EKQLAREVVL IDIIEGIPQG KALDMYESGP VALFDTMVKG 

        70         80         90        100        110        120 
SNDYADSADS DIVLITAGLA RKPGMSREDL LMKNTAIIKD VTTQVMRYSV NPILIMVSNP 

       130        140        150        160        170        180 
LDVMTFVAHT VSGLKPERVI GMAGVLDTAR FRSFIAEALN VSMQDINAFV LGGHGDSMVP 

       190        200        210        220        230        240 
VVKYTNVAGI PLTELLPKET IDAIVERTKN GGIEIVNHLK TGSAFYAPAA SAVEMIESIV 

       250        260        270        280        290        300 
KDRKRILPCT TCLGGQYGIN NVFCGVPVKL GKEGVEQILE INLDDNELKA LQASAAIVEK 


NCKSLASAI 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37343.1.
RefSeqYP_001130845.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SFT4.
SMRA4SFT4. Positions 1-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290318.Cvib_1331.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP37343; ABP37343; Cvib_1331.
GeneID4971185.
KEGGpvi:Cvib_1331.
PATRIC21397156. VBIChlPha132153_1404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAGANSYEA.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycCPHA290318:GHNQ-1369-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00487. Malate_dehydrog_3.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01763. MalateDH_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_PROVI
AccessionPrimary (citable) accession number: A4SFT4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families