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P19446

- MDHG_CITLA

UniProt

P19446 - MDHG_CITLA

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Protein

Malate dehydrogenase, glyoxysomal

Gene
N/A
Organism
Citrullus lanatus (Watermelon) (Citrullus vulgaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.PROSITE-ProRule annotation

Kineticsi

  1. KM=146 µM for NADH
  2. KM=76 mM for oxaloacetate

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771NADBy similarity
Binding sitei124 – 1241Substrate
Binding sitei130 – 1301Substrate
Binding sitei137 – 1371NADBy similarity
Binding sitei162 – 1621Substrate
Binding sitei196 – 1961Substrate
Active sitei220 – 2201Proton acceptor
Binding sitei271 – 2711NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi51 – 577NADBy similarity
Nucleotide bindingi160 – 1623NADBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-KW
  2. malate metabolic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, glyoxysomal (EC:1.1.1.37)
OrganismiCitrullus lanatus (Watermelon) (Citrullus vulgaris)
Taxonomic identifieri3654 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCitrullus

Subcellular locationi

GO - Cellular componenti

  1. glyoxysome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636Glyoxysome2 PublicationsAdd
BLAST
Chaini37 – 356320Malate dehydrogenase, glyoxysomalPRO_0000018638Add
BLAST

Proteomic databases

PRIDEiP19446.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 517Combined sources
Helixi57 – 6610Combined sources
Beta strandi70 – 8011Combined sources
Helixi81 – 899Combined sources
Beta strandi96 – 1027Combined sources
Helixi103 – 1108Combined sources
Beta strandi114 – 1185Combined sources
Helixi132 – 15120Combined sources
Beta strandi155 – 1595Combined sources
Helixi164 – 17815Combined sources
Beta strandi185 – 1884Combined sources
Helixi191 – 20515Combined sources
Helixi209 – 2113Combined sources
Beta strandi216 – 2183Combined sources
Helixi222 – 2243Combined sources
Beta strandi225 – 2273Combined sources
Helixi229 – 2313Combined sources
Helixi240 – 26021Combined sources
Turni261 – 2633Combined sources
Helixi269 – 28719Combined sources
Beta strandi292 – 2998Combined sources
Beta strandi302 – 31514Combined sources
Beta strandi318 – 3225Combined sources
Helixi330 – 35425Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SEVX-ray2.55A/B1-356[»]
1SMKX-ray2.50A/B/C/D/E/F/G/H37-356[»]
ProteinModelPortaliP19446.
SMRiP19446. Positions 44-356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19446.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
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.
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.

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

P19446-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQPIPDVNQR IARISAHLHP PKSQMEESSA LRRANCRAKG GAPGFKVAIL
60 70 80 90 100
GAAGGIGQPL AMLMKMNPLV SVLHLYDVVN APGVTADISH MDTGAVVRGF
110 120 130 140 150
LGQQQLEAAL TGMDLIIVPA GVPRKPGMTR DDLFKINAGI VKTLCEGIAK
160 170 180 190 200
CCPRAIVNLI SNPVNSTVPI AAEVFKKAGT YDPKRLLGVT MLDVVRANTF
210 220 230 240 250
VAEVLGLDPR DVDVPVVGGH AGVTILPLLS QVKPPSSFTQ EEISYLTDRI
260 270 280 290 300
QNGGTEVVEA KAGAGSATLS MAYAAVKFAD ACLRGLRGDA GVIECAFVSS
310 320 330 340 350
QVTELPFFAS KVRLGRNGIE EVYSLGPLNE YERIGLEKAK KELAGSIEKG

VSFIRS
Length:356
Mass (Da):37,637
Last modified:February 1, 1991 - v1
Checksum:i4B0C8101DC11FC7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33148 mRNA. Translation: AAA33041.1.
PIRiA35957. DEPUGW.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33148 mRNA. Translation: AAA33041.1 .
PIRi A35957. DEPUGW.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SEV X-ray 2.55 A/B 1-356 [» ]
1SMK X-ray 2.50 A/B/C/D/E/F/G/H 37-356 [» ]
ProteinModelPortali P19446.
SMRi P19446. Positions 44-356.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P19446.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P19446.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
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.
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. "Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide."
    Gietl C.
    Proc. Natl. Acad. Sci. U.S.A. 87:5773-5777(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Sugar Baby.
  2. "Sequence homologies between glyoxysomal and mitochondrial malate dehydrogenase."
    Gietl C., Lottspeich F., Hock B.
    Planta 169:555-558(1986)
    Cited for: PROTEIN SEQUENCE OF 37-65.
  3. "Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence."
    Cox B., Chit M.M., Weaver T., Gietl C., Bailey J., Bell E., Banaszak L.
    FEBS J. 272:643-654(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMDHG_CITLA
AccessioniPrimary (citable) accession number: P19446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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