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Q6HSF4 (MDH_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Malate dehydrogenase

EC=1.1.1.37
Gene names
Name:mdh
Ordered Locus Names:BA_4837, GBAA_4837, BAS4486
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113424

Regions

Nucleotide binding12 – 176NAD By similarity
Nucleotide binding123 – 1253NAD By similarity

Sites

Active site1801Proton acceptor By similarity
Binding site361NAD By similarity
Binding site871Substrate By similarity
Binding site931Substrate By similarity
Binding site1001NAD By similarity
Binding site1251Substrate By similarity
Binding site1561Substrate By similarity

Amino acid modifications

Modified residue1491Phosphoserine By similarity

Secondary structure

..................................................... 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6HSF4 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 615A61C61CA217FD

FASTA31233,498
        10         20         30         40         50         60 
MTIKRKKVSV IGAGFTGATT AFLLAQKELA DVVLVDIPQL ENPTKGKALD MLEASPVQGF 

        70         80         90        100        110        120 
DANIIGTSDY ADTADSDVVV ITAGIARKPG MSRDDLVATN SKIMKSITRD IAKHSPNAII 

       130        140        150        160        170        180 
VVLTNPVDAM TYSVFKEAGF PKERVIGQSG VLDTARFRTF IAQELNLSVK DITGFVLGGH 

       190        200        210        220        230        240 
GDDMVPLVRY SYAGGIPLET LIPKERLEAI VERTRKGGGE IVGLLGNGSA YYAPAASLVE 

       250        260        270        280        290        300 
MTEAILKDQR RVLPAIAYLE GEYGYSDLYL GVPVILGGNG IEKIIELELL ADEKEALDRS 

       310 
VESVRNVMKV LV 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP28526.1.
AE017334 Genomic DNA. Translation: AAT33956.1.
AE017225 Genomic DNA. Translation: AAT56784.1.
RefSeqNP_847040.1. NC_003997.3.
YP_021481.1. NC_007530.2.
YP_030734.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TL2X-ray1.70A1-312[»]
ProteinModelPortalQ6HSF4.
SMRQ6HSF4. Positions 5-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198094.BA_4837.

Protocols and materials databases

DNASU1083988.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP28526; AAP28526; BA_4837.
AAT33956; AAT33956; GBAA_4837.
AAT56784; AAT56784; BAS4486.
GeneID1083988.
2819626.
2851560.
KEGGban:BA_4837.
bar:GBAA_4837.
bat:BAS4486.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycANTHRA:MDH-MONOMER.
BANT260799:GJAJ-4544-MONOMER.
BANT261594:GJ7F-4699-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_BACAN
AccessionPrimary (citable) accession number: Q6HSF4
Secondary accession number(s): Q6KLP9, Q81KZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 19, 2004
Last modified: February 19, 2014
This is version 82 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references