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Protein

Malate dehydrogenase

Gene

mdh

Organism
Aquaspirillum arcticum
Status
Reviewed-Annotation score: Annotation score: 4 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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei95SubstrateUniRule annotation1
Binding sitei101SubstrateUniRule annotation1
Binding sitei108NADUniRule annotation1
Binding sitei115NADUniRule annotation1 Publication1
Binding sitei134SubstrateUniRule annotation1
Binding sitei165SubstrateUniRule annotation1 Publication1
Active sitei190Proton acceptorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 18NADUniRule annotation1 Publication7
Nucleotide bindingi132 – 134NADUniRule annotation1 Publication3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.37. 395.
SABIO-RKQ9ZF99.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenaseUniRule annotation (EC:1.1.1.37UniRule annotation)
Gene namesi
Name:mdhUniRule annotation
OrganismiAquaspirillum arcticum
Taxonomic identifieri87645 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceae

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001133462 – 329Malate dehydrogenaseAdd BLAST328

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Helixi16 – 26Combined sources11
Turni27 – 31Combined sources5
Beta strandi37 – 42Combined sources6
Helixi47 – 61Combined sources15
Turni62 – 64Combined sources3
Beta strandi68 – 76Combined sources9
Helixi77 – 80Combined sources4
Turni81 – 83Combined sources3
Beta strandi85 – 89Combined sources5
Helixi101 – 122Combined sources22
Beta strandi128 – 131Combined sources4
Beta strandi133 – 135Combined sources3
Helixi136 – 145Combined sources10
Helixi152 – 154Combined sources3
Beta strandi155 – 157Combined sources3
Helixi160 – 174Combined sources15
Helixi178 – 180Combined sources3
Beta strandi181 – 183Combined sources3
Beta strandi185 – 188Combined sources4
Beta strandi195 – 197Combined sources3
Helixi208 – 212Combined sources5
Helixi215 – 220Combined sources6
Helixi222 – 227Combined sources6
Helixi229 – 237Combined sources9
Helixi242 – 258Combined sources17
Beta strandi265 – 270Combined sources6
Helixi274 – 276Combined sources3
Beta strandi282 – 290Combined sources9
Beta strandi293 – 296Combined sources4
Helixi304 – 324Combined sources21
Helixi325 – 328Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8PX-ray1.90A1-329[»]
1B8UX-ray2.50A1-329[»]
1B8VX-ray2.10A1-329[»]
ProteinModelPortaliQ9ZF99.
SMRiQ9ZF99.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZF99.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 2 family.UniRule annotationCurated

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ZF99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTPMRVAV TGAAGQICYS LLFRIANGDM LGKDQPVILQ LLEIPNEKAQ
60 70 80 90 100
KALQGVMMEI DDCAFPLLAG MTAHADPMTA FKDADVALLV GARPRGPGME
110 120 130 140 150
RKDLLEANAQ IFTVQGKAID AVASRNIKVL VVGNPANTNA YIAMKSAPSL
160 170 180 190 200
PAKNFTAMLR LDHNRALSQI AAKTGKPVSS IEKLFVWGNH SPTMYADYRY
210 220 230 240 250
AQIDGASVKD MINDDAWNRD TFLPTVGKRG AAIIDARGVS SAASAANAAI
260 270 280 290 300
DHIHDWVLGT AGKWTTMGIP SDGSYGIPEG VIFGFPVTTE NGEYKIVQGL
310 320
SIDAFSQERI NVTLNELLEE QNGVQHLLG
Length:329
Mass (Da):35,251
Last modified:January 23, 2007 - v3
Checksum:iF02E2826E5028F27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF109682 Genomic DNA. Translation: AAD13225.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF109682 Genomic DNA. Translation: AAD13225.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8PX-ray1.90A1-329[»]
1B8UX-ray2.50A1-329[»]
1B8VX-ray2.10A1-329[»]
ProteinModelPortaliQ9ZF99.
SMRiQ9ZF99.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.1.37. 395.
SABIO-RKQ9ZF99.

Miscellaneous databases

EvolutionaryTraceiQ9ZF99.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMDH_AQUAR
AccessioniPrimary (citable) accession number: Q9ZF99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.