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UniProtKB - Q5JI38 (SPEBH_THEKO)
Protein
N(1)-aminopropylagmatine ureohydrolase
Gene
TK0882
Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Functioni
Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the decarboxylation of N1-(3-aminopropyl)agmatine to yield spermidine and urea. It can also use agmatine to yield putrescine.
1 PublicationMiscellaneous
In T.kodakarensis, two kinds of synthetic pathways from agmatine to spermidine are predicted. One is the pathway via putrescine (pathway I), and the other is that via N1-aminopropylagmatine (pathway II) (PubMed:20675472).1 Publication
Catalytic activityi
Cofactori
Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation
Kineticsi
kcat is 1.86 sec(-1) for ureohydrolase activity with agmatine as substrate (at pH 7.5 and 70 degrees Celsius). kcat is 1.01 sec(-1) for ureohydrolase activity with N1-aminopropylagmatine as substrate (at pH 7.5 and 70 degrees Celsius).
- KM=6.42 µM for N1-aminopropylagmatine (at pH 7.5 and 70 degrees Celsius)1 Publication
- KM=486 µM for agmatine (at pH 7.5 and 70 degrees Celsius)1 Publication
Temperature dependencei
Optimum temperature is 90 degrees Celsius.1 Publication
: spermidine biosynthesis Pathwayi
This protein is involved in the pathway spermidine biosynthesis, which is part of Amine and polyamine biosynthesis.View all proteins of this organism that are known to be involved in the pathway spermidine biosynthesis and in Amine and polyamine biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 114 | Manganese 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 133 | Manganese 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 133 | Manganese 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 135 | Manganese 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 137 | Manganese 1PROSITE-ProRule annotation | 1 | |
Sitei | 144 | Important for catalytic activityBy similarity | 1 | |
Metal bindingi | 213 | Manganese 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 213 | Manganese 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 215 | Manganese 2PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- agmatinase activity Source: UniProtKB
- aminopropylagmatine ureohydrolase activity Source: UniProtKB-EC
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- putrescine biosynthetic process from arginine, using agmatinase Source: GO_Central
- spermidine biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | Polyamine biosynthesis, Spermidine biosynthesis |
Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.5.3.24, 5246 |
UniPathwayi | UPA00248 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Ordered Locus Names:TK0882 |
Organismi | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
Taxonomic identifieri | 69014 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Cells lacking this gene show to a decreased growth rate at 85 degrees Celsius and a severe growth defect at 93 degrees Celsius. This mutant accumulates N1-aminopropylagmatine and agmatine at 85 degrees Celsius.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000429862 | 1 – 288 | N(1)-aminopropylagmatine ureohydrolaseAdd BLAST | 288 |
Family & Domainsi
Sequence similaritiesi
Belongs to the arginase family.PROSITE-ProRule annotation
Phylogenomic databases
eggNOGi | arCOG01700, Archaea |
HOGENOMi | CLU_039478_0_2_2 |
InParanoidi | Q5JI38 |
OMAi | YELTTIM |
OrthoDBi | 52310at2157 |
PhylomeDBi | Q5JI38 |
Family and domain databases
InterProi | View protein in InterPro IPR005925, Agmatinase-rel IPR006035, Ureohydrolase IPR023696, Ureohydrolase_dom_sf |
PANTHERi | PTHR11358, PTHR11358, 1 hit |
Pfami | View protein in Pfam PF00491, Arginase, 1 hit |
PIRSFi | PIRSF036979, Arginase, 1 hit |
SUPFAMi | SSF52768, SSF52768, 1 hit |
TIGRFAMsi | TIGR01230, agmatinase, 1 hit |
PROSITEi | View protein in PROSITE PS51409, ARGINASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
Q5JI38-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEFLYTYETL KLEFPLVEPE KARFILLGVP FDGTTSYKAG ARFGPTLIRQ
60 70 80 90 100
ATLNLESYIL DYDLDIAELP IADIGDIAVV AGDPRKTADR VRETLEELKK
110 120 130 140 150
ANPKAIPILL GGEHSQTLGA VEALKPASYV VFDAHLDLRN SYEDNPYNHA
160 170 180 190 200
CVARRISELG VKEAIFGIRS GTKEEVDFAR ERDIPWVHAR DYSFDAFVDL
210 220 230 240 250
VEALPEPVYL SIDIDVFDLS MVPSTGTPEA GGLRFWEVVE AIEWLVEKKE
260 270 280
IAGFDIMEVA GEKLGDPTAL TAAKLLFYSI GAMAKFGR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AP006878 Genomic DNA Translation: BAD85071.1 |
RefSeqi | WP_011249833.1, NC_006624.1 |
Genome annotation databases
EnsemblBacteriai | BAD85071; BAD85071; TK0882 |
GeneIDi | 3234601 |
KEGGi | tko:TK0882 |
PATRICi | fig|69014.16.peg.861 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AP006878 Genomic DNA Translation: BAD85071.1 |
RefSeqi | WP_011249833.1, NC_006624.1 |
3D structure databases
SMRi | Q5JI38 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 69014.TK0882 |
Genome annotation databases
EnsemblBacteriai | BAD85071; BAD85071; TK0882 |
GeneIDi | 3234601 |
KEGGi | tko:TK0882 |
PATRICi | fig|69014.16.peg.861 |
Phylogenomic databases
eggNOGi | arCOG01700, Archaea |
HOGENOMi | CLU_039478_0_2_2 |
InParanoidi | Q5JI38 |
OMAi | YELTTIM |
OrthoDBi | 52310at2157 |
PhylomeDBi | Q5JI38 |
Enzyme and pathway databases
UniPathwayi | UPA00248 |
BRENDAi | 3.5.3.24, 5246 |
Family and domain databases
InterProi | View protein in InterPro IPR005925, Agmatinase-rel IPR006035, Ureohydrolase IPR023696, Ureohydrolase_dom_sf |
PANTHERi | PTHR11358, PTHR11358, 1 hit |
Pfami | View protein in Pfam PF00491, Arginase, 1 hit |
PIRSFi | PIRSF036979, Arginase, 1 hit |
SUPFAMi | SSF52768, SSF52768, 1 hit |
TIGRFAMsi | TIGR01230, agmatinase, 1 hit |
PROSITEi | View protein in PROSITE PS51409, ARGINASE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SPEBH_THEKO | |
Accessioni | Q5JI38Primary (citable) accession number: Q5JI38 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 9, 2014 |
Last sequence update: | February 15, 2005 | |
Last modified: | February 23, 2022 | |
This is version 95 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
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families