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Q9ZF99

- MDH_AQUAR

UniProt

Q9ZF99 - MDH_AQUAR

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Protein

Malate dehydrogenase

Gene

mdh

Organism
Aquaspirillum arcticum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951SubstrateBy similarity
Binding sitei101 – 1011SubstrateBy similarity
Binding sitei108 – 1081NADBy similarity
Binding sitei115 – 1151NAD1 Publication
Binding sitei134 – 1341SubstrateBy similarity
Binding sitei165 – 1651Substrate
Active sitei190 – 1901Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 187NAD1 Publication
Nucleotide bindingi132 – 1343NAD1 Publication

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

Enzyme and pathway databases

SABIO-RKQ9ZF99.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
OrganismiAquaspirillum arcticum
Taxonomic identifieri87645 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceae

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 329328Malate dehydrogenasePRO_0000113346Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127
Helixi16 – 2611
Turni27 – 315
Beta strandi37 – 426
Helixi47 – 6115
Turni62 – 643
Beta strandi68 – 769
Helixi77 – 804
Turni81 – 833
Beta strandi85 – 895
Helixi101 – 12222
Beta strandi128 – 1314
Beta strandi133 – 1353
Helixi136 – 14510
Helixi152 – 1543
Beta strandi155 – 1573
Helixi160 – 17415
Helixi178 – 1803
Beta strandi181 – 1833
Beta strandi185 – 1884
Beta strandi195 – 1973
Helixi208 – 2125
Helixi215 – 2206
Helixi222 – 2276
Helixi229 – 2379
Helixi242 – 25817
Beta strandi265 – 2706
Helixi274 – 2763
Beta strandi282 – 2909
Beta strandi293 – 2964
Helixi304 – 32421
Helixi325 – 3284

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8PX-ray1.90A1-329[»]
1B8UX-ray2.50A1-329[»]
1B8VX-ray2.10A1-329[»]
ProteinModelPortaliQ9ZF99.
SMRiQ9ZF99. Positions 3-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZF99.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 2 family.Curated

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
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.
SUPFAMiSSF56327. 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:
EMBL
GenBank
DDBJ
Links Updated
AF109682 Genomic DNA. Translation: AAD13225.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF109682 Genomic DNA. Translation: AAD13225.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B8P X-ray 1.90 A 1-329 [» ]
1B8U X-ray 2.50 A 1-329 [» ]
1B8V X-ray 2.10 A 1-329 [» ]
ProteinModelPortali Q9ZF99.
SMRi Q9ZF99. Positions 3-329.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q9ZF99.

Miscellaneous databases

EvolutionaryTracei Q9ZF99.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_01517. Malate_dehydrog_2.
InterProi IPR001557. 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 ]
PANTHERi PTHR23382. PTHR23382. 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 TIGR01759. MalateDH-SF1. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum."
    Kim S.-Y., Hwang K.Y., Kim S.-H., Sung H.-C., Han Y.S., Cho Y.
    J. Biol. Chem. 274:11761-11767(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 103-123, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

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: October 1, 2014
This is version 96 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

External Data

Dasty 3