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UniProtKB - P16100 (IDH_AZOVI)
Protein
Isocitrate dehydrogenase [NADP]
Gene
icd
Organism
Azotobacter vinelandii
Status
Functioni
Catalytic activityi
- EC:1.1.1.42
Cofactori
Activity regulationi
Inhibition of this enzyme by phosphorylation regulates the branch point between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth. The phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK).
Temperature dependencei
Optimum temperature is above 40 degrees Celsius.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 135 | NADP | 1 | |
Binding sitei | 145 | Substrate | 1 | |
Sitei | 255 | Critical for catalysisBy similarity | 1 | |
Metal bindingi | 350 | Magnesium or manganese | 1 | |
Sitei | 420 | Critical for catalysisBy similarity | 1 | |
Binding sitei | 547 | Substrate | 1 | |
Metal bindingi | 548 | Magnesium or manganese | 1 | |
Metal bindingi | 552 | Magnesium or manganeseBy similarity | 1 | |
Binding sitei | 589 | NADP | 1 | |
Binding sitei | 649 | NADP | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 82 – 87 | NADP | 6 | |
Nucleotide bindingi | 584 – 585 | NADP | 2 | |
Nucleotide bindingi | 600 – 602 | NADP | 3 |
GO - Molecular functioni
- isocitrate dehydrogenase (NADP+) activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- glyoxylate cycle Source: UniProtKB-KW
- tricarboxylic acid cycle Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Glyoxylate bypass, Tricarboxylic acid cycle |
Ligand | Magnesium, Manganese, Metal-binding, NADP |
Names & Taxonomyi
Protein namesi | Recommended name: Isocitrate dehydrogenase [NADP] (EC:1.1.1.42)Short name: IDH Alternative name(s): Oxalosuccinate decarboxylase |
Gene namesi | Name:icd |
Organismi | Azotobacter vinelandii |
Taxonomic identifieri | 354 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter |
Subcellular locationi
Cytoplasm and Cytosol
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Chemistry databases
DrugBanki | DB01727, Isocitric Acid DB03461, Nicotinamide adenine dinucleotide phosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000083593 | 2 – 741 | Isocitrate dehydrogenase [NADP]Add BLAST | 740 |
Keywords - PTMi
PhosphoproteinProteomic databases
PRIDEi | P16100 |
Interactioni
Subunit structurei
Monomer.
1 PublicationStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P16100 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P16100 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 132 – 139 | Substrate binding | 8 |
Domaini
This molecule consists of two distinct domains, a small domain and a large domain. The structure of the large domain repeats a motif observed in the dimeric IDH. Such a fusional structure by domain duplication enables a single polypeptide chain to form a structure at the catalytic site that is homologous to the dimeric IDH, the catalytic site of which is located at the interface of two identical subunits.
Sequence similaritiesi
Belongs to the monomeric-type IDH family.Curated
Family and domain databases
InterProi | View protein in InterPro IPR004436, Isocitrate_DH_NADP_mono |
PANTHERi | PTHR36999, PTHR36999, 1 hit |
Pfami | View protein in Pfam PF03971, IDH, 1 hit |
PIRSFi | PIRSF009407, IDH_monmr, 1 hit |
TIGRFAMsi | TIGR00178, monomer_idh, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P16100-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTPKIIYTL TDEAPALATY SLLPIIKAFT GSSGIAVETR DISLAGRLIA
60 70 80 90 100
TFPEYLTDTQ KISDDLAELG KLATTPDANI IKLPNISASV PQLKAAIKEL
110 120 130 140 150
QQQGYKLPDY PEEPKTDTEK DVKARYDKIK GSAVNPVLRE GNSDRRAPLS
160 170 180 190 200
VKNYARKHPH KMGAWSADSK SHVAHMDNGD FYGSEKAALI GAPGSVKIEL
210 220 230 240 250
IAKDGSSTVL KAKTSVQAGE IIDSSVMSKN ALRNFIAAEI EDAKKQGVLL
260 270 280 290 300
SVHLKATMMK VSDPIMFGQI VSEFYKDALT KHAEVLKQIG FDVNNGIGDL
310 320 330 340 350
YARIKTLPEA KQKEIEADIQ AVYAQRPQLA MVNSDKGITN LHVPSDVIVD
360 370 380 390 400
ASMPAMIRDS GKMWGPDGKL HDTKAVIPDR CYAGVYQVVI EDCKQHGAFD
410 420 430 440 450
PTTMGSVPNV GLMAQKAEEY GSHDKTFQIP ADGVVRVTDE SGKLLLEQSV
460 470 480 490 500
EAGDIWRMCQ AKDAPIQDWV KLAVNRARAT NTPAVFWLDP ARAHDAQVIA
510 520 530 540 550
KVERYLKDYD TSGLDIRILS PVEATRFSLA RIREGKDTIS VTGNVLRDYL
560 570 580 590 600
TDLFPIMELG TSAKMLSIVP LMSGGGLFET GAGGSAPKHV QQFLEEGYLR
610 620 630 640 650
WDSLGEFLAL AASLEHLGNA YKNPKALVLA STLDQATGKI LDNNKSPARK
660 670 680 690 700
VGEIDNRGSH FYLALYWAQA LAAQTEDKEL QAQFTGIAKA LTDNETKIVG
710 720 730 740
ELAAAQGKPV DIAGYYHPNT DLTSKAIRPS ATFNAALAPL A
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D73443 Genomic DNA Translation: BAA11169.1 |
PIRi | A10759 JC7822 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D73443 Genomic DNA Translation: BAA11169.1 |
PIRi | A10759 JC7822 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ITW | X-ray | 1.95 | A/B/C/D | 1-741 | [»] | |
1J1W | X-ray | 3.20 | A/B/C/D | 1-741 | [»] | |
SMRi | P16100 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB01727, Isocitric Acid DB03461, Nicotinamide adenine dinucleotide phosphate |
Proteomic databases
PRIDEi | P16100 |
Miscellaneous databases
EvolutionaryTracei | P16100 |
Family and domain databases
InterProi | View protein in InterPro IPR004436, Isocitrate_DH_NADP_mono |
PANTHERi | PTHR36999, PTHR36999, 1 hit |
Pfami | View protein in Pfam PF03971, IDH, 1 hit |
PIRSFi | PIRSF009407, IDH_monmr, 1 hit |
TIGRFAMsi | TIGR00178, monomer_idh, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | IDH_AZOVI | |
Accessioni | P16100Primary (citable) accession number: P16100 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 122 of the entry and version 5 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families