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UniProtKB - O34295 (TTUC5_AGRVI)
Protein
Probable tartrate dehydrogenase/decarboxylase TtuC'
Gene
ttuC'
Organism
Agrobacterium vitis (Rhizobium vitis)
Status
Functioni
Has multiple catalytic activities. Apart from catalyzing the oxidation of (+)-tartrate to oxaloglycolate, also converts meso-tartrate to D-glycerate and catalyzes the oxidative decarboxylation of D-malate to pyruvate.
By similarityCatalytic activityi
- EC:1.1.1.93By similarity
- EC:1.1.1.93By similarity
- EC:1.1.1.93By similarity
- EC:4.1.1.73By similarity
- EC:1.1.1.83By similarity
Cofactori
Protein has several cofactor binding sites:- Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity
- K+By similarity
: tartrate degradation Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 2-hydroxy-3-oxosuccinate from L-tartrate. This subpathway is part of the pathway tartrate degradation, which is itself part of Carbohydrate acid metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-hydroxy-3-oxosuccinate from L-tartrate, the pathway tartrate degradation and in Carbohydrate acid metabolism.
Pathwayi: tartrate degradation
This protein is involved in step 1 of the subpathway that synthesizes 2-hydroxy-3-oxosuccinate from meso-tartrate. This subpathway is part of the pathway tartrate degradation, which is itself part of Carbohydrate acid metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-hydroxy-3-oxosuccinate from meso-tartrate, the pathway tartrate degradation and in Carbohydrate acid metabolism.
Pathwayi: tartrate degradation
This protein is involved in step 1 of the subpathway that synthesizes D-glycerate from L-tartrate. This subpathway is part of the pathway tartrate degradation, which is itself part of Carbohydrate acid metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glycerate from L-tartrate, the pathway tartrate degradation and in Carbohydrate acid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 222 | ManganeseBy similarity | 1 | |
Metal bindingi | 246 | ManganeseBy similarity | 1 | |
Metal bindingi | 250 | ManganeseBy similarity | 1 |
GO - Molecular functioni
- D-malate dehydrogenase (decarboxylating) activity Source: UniProtKB-EC
- magnesium ion binding Source: InterPro
- NAD binding Source: InterPro
- tartrate decarboxylase activity Source: UniProtKB-EC
- tartrate dehydrogenase activity Source: UniProtKB-EC
Keywordsi
Molecular function | Lyase, Oxidoreductase |
Ligand | Manganese, Metal-binding, NAD |
Enzyme and pathway databases
UniPathwayi | UPA00839;UER00800 UPA00839;UER00801 UPA00839;UER00803 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ttuC' |
Encoded oni | Plasmid pTrAB4 |
Organismi | Agrobacterium vitis (Rhizobium vitis) |
Taxonomic identifieri | 373 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Hyphomicrobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000083817 | 1 – 358 | Probable tartrate dehydrogenase/decarboxylase TtuC'Add BLAST | 358 |
Expressioni
Inductioni
By tartrate.
Family & Domainsi
Sequence similaritiesi
Belongs to the isocitrate and isopropylmalate dehydrogenases family.Curated
Family and domain databases
InterProi | View protein in InterPro IPR019818, IsoCit/isopropylmalate_DH_CS IPR024084, IsoPropMal-DH-like_dom IPR011829, TTC_DH |
Pfami | View protein in Pfam PF00180, Iso_dh, 1 hit |
SMARTi | View protein in SMART SM01329, Iso_dh, 1 hit |
TIGRFAMsi | TIGR02089, TTC, 1 hit |
PROSITEi | View protein in PROSITE PS00470, IDH_IMDH, 1 hit |
i Sequence
Sequence statusi: Complete.
O34295-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MREYKIAAIP ADGIGPEVIA AGLQVLEALE QRSGDFKIHT ETFDWGSDYY
60 70 80 90 100
KKHGVMMPAD GLDKLKKFDA IFFGAVGAPD VPDHITLWGL RLPICQGFDQ
110 120 130 140 150
YANVRPTKIL PGITPPLRNC GPGDLDWVIV RENSEGEYSG HGGRAHRGLP
160 170 180 190 200
EEVGTEVAIF TRVGVTRIMR YAFKLAQARP RKLLTVVTKS NAQRHGMVMW
210 220 230 240 250
DEIAAEVATE FPDVTWDKML VDAMTVRMTL KPETLDTIVA TNLHADILSD
260 270 280 290 300
LAGALAGSLG VAPTANIDPE RRFPSMFEPI HGSAFDITGK GIANPIATFW
310 320 330 340 350
TAAQMLEHLG ERDAAARLMG AVERVTEAGI LTPDVGGTAN TSQVTEAVCN
AIAGSNII
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF010261 Genomic DNA Translation: AAB65746.1 |
RefSeqi | WP_032489006.1, NZ_WPID01000009.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF010261 Genomic DNA Translation: AAB65746.1 |
RefSeqi | WP_032489006.1, NZ_WPID01000009.1 |
3D structure databases
AlphaFoldDBi | O34295 |
SMRi | O34295 |
ModBasei | Search... |
Enzyme and pathway databases
UniPathwayi | UPA00839;UER00800 UPA00839;UER00801 UPA00839;UER00803 |
Family and domain databases
InterProi | View protein in InterPro IPR019818, IsoCit/isopropylmalate_DH_CS IPR024084, IsoPropMal-DH-like_dom IPR011829, TTC_DH |
Pfami | View protein in Pfam PF00180, Iso_dh, 1 hit |
SMARTi | View protein in SMART SM01329, Iso_dh, 1 hit |
TIGRFAMsi | TIGR02089, TTC, 1 hit |
PROSITEi | View protein in PROSITE PS00470, IDH_IMDH, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TTUC5_AGRVI | |
Accessioni | O34295Primary (citable) accession number: O34295 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1999 |
Last sequence update: | January 1, 1998 | |
Last modified: | May 25, 2022 | |
This is version 96 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
PlasmidDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families