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P48364

- MDH_MORS5

UniProt

P48364 - MDH_MORS5

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Protein

Malate dehydrogenase

Gene
mdh
Organism
Moritella sp. (strain 5710)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate.UniRule annotation

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.1 Publication

pH dependencei

Optimum pH is 9.5-10.0 for malate dehydrogenation, and 7.5-8.0 for oxaloacetate reduction.UniRule annotation

Temperature dependencei

Optimum temperature is 35 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341NAD By similarity
Binding sitei81 – 811Substrate By similarity
Binding sitei87 – 871Substrate By similarity
Binding sitei94 – 941NAD By similarity
Binding sitei119 – 1191Substrate By similarity
Binding sitei153 – 1531Substrate By similarity
Active sitei177 – 1771Proton acceptor By similarity
Binding sitei227 – 2271NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 137NAD By similarity
Nucleotide bindingi117 – 1193NAD By similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. malate metabolic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
OrganismiMoritella sp. (strain 5710)
Taxonomic identifieri246794 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi229 – 2291Q → H: Increases the thermal stability. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Malate dehydrogenaseUniRule annotationPRO_0000113316Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP48364.
SMRiP48364. Positions 1-310.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01516. Malate_dehydrog_1.
InterProiIPR001557. 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.
IPR010097. Malate_DH_type1.
IPR023958. Malate_DH_type1_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48364-1 [UniParc]FASTAAdd to Basket

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MKVAVLGAAG GIGQALALLL KTQLPAGSDL SLYDIAPVTP GVAVDLSHIP    50
TDVTIAGFAG MDPTDALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN 100
LAGKCAEVCP NACIGIITNP VNTTVPIAAE VLKQAGVYDK RKLFGITTLD 150
VIRSETFVSA LKGISLADVE VPVIGGHSGV TILPLLSQVK GVEFTAEEVV 200
ALTARIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR ALQGEKGIVE 250
CTYVDGGSEH ATFFAQPVLL GKNGVEEVLA YGELSEFETN ARDAMLEELK 300
ANITLGEEFV AG 312
Length:312
Mass (Da):31,985
Last modified:February 1, 1996 - v1
Checksum:i2C4A3253E5B5D2E6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78194 Genomic DNA. Translation: BAA11301.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78194 Genomic DNA. Translation: BAA11301.1 .

3D structure databases

ProteinModelPortali P48364.
SMRi P48364. Positions 1-310.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_01516. Malate_dehydrog_1.
InterProi IPR001557. 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.
IPR010097. Malate_DH_type1.
IPR023958. Malate_DH_type1_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene."
    Ohkuma M., Ohtoko K., Takada N., Hamamoto T., Usami R., Kudo T., Horikoshi K.
    FEMS Microbiol. Lett. 137:247-252(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Differences in malate dehydrogenases from the obligately piezophilic deep-sea bacterium Moritella sp. strain 2D2 and the psychrophilic bacterium Moritella sp. strain 5710."
    Saito R., Nakayama A.
    FEMS Microbiol. Lett. 233:165-172(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-229.

Entry informationi

Entry nameiMDH_MORS5
AccessioniPrimary (citable) accession number: P48364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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