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Protein

N(1)-aminopropylagmatine ureohydrolase

Gene

TTHA1129

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 cannot use agmatine as substrate.1 Publication

Catalytic activityi

N(1)-aminopropylagmatine + H2O = spermidine + urea.1 Publication

Cofactori

Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Pathwayi: spermidine biosynthesis

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Manganese 1PROSITE-ProRule annotation
Metal bindingi128 – 1281Manganese 1PROSITE-ProRule annotation
Metal bindingi128 – 1281Manganese 2PROSITE-ProRule annotation
Metal bindingi130 – 1301Manganese 2PROSITE-ProRule annotation
Metal bindingi132 – 1321Manganese 1PROSITE-ProRule annotation
Metal bindingi210 – 2101Manganese 1PROSITE-ProRule annotation
Metal bindingi210 – 2101Manganese 2PROSITE-ProRule annotation
Metal bindingi212 – 2121Manganese 2PROSITE-ProRule annotation

GO - Molecular functioni

  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • spermidine biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16737.
TTHE300852:GH8R-1161-MONOMER.
BRENDAi3.5.3.24. 2305.
UniPathwayiUPA00248.

Names & Taxonomyi

Protein namesi
Recommended name:
N(1)-aminopropylagmatine ureohydrolase (EC:3.5.3.24)
Alternative name(s):
Protein SpeB homolog
Gene namesi
Ordered Locus Names:TTHA1129
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show a significant defect of growth at 78 degrees Celsius and accumulate N1-aminopropylagmatine. The double mutant of speB and speE shows defective growth at 70 degrees Celsius and significant defective growth at 78 degrees Celsius. It accumulates agmatine and N1-aminopropylagmatine.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293N(1)-aminopropylagmatine ureohydrolasePRO_0000429863Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1129.

Structurei

3D structure databases

ProteinModelPortaliQ5SJ85.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CYW. Bacteria.
COG0010. LUCA.
HOGENOMiHOG000204320.
KOiK01480.
OMAiSHASIMF.
PhylomeDBiQ5SJ85.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SJ85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLVFGEKDT PYEEARVVVL PVPYDLSLSF LPGARRGPEA ILLASRELEP
60 70 80 90 100
FLLELGAAPE EVGIHAAEPV PWVAGMAEES HRLIREEALR HLRAGKWVVA
110 120 130 140 150
LGGDHSVTHP LVQAHREALG DFSLLHVDAH ADLYPEWQGS VYSHASPFYR
160 170 180 190 200
LLTEGFPLVQ VGIRAMDRDS LRLARKKGVA LFPAHRIHRE GLPLDEILRA
210 220 230 240 250
LGKRVYISLD FDALDPSLMP SVGTPLPGGL SYRQVVDLLE AVFREKEVVG
260 270 280 290
MDFVELSPNG QFHAEMTAAQ LVYHAIGLKG LQAGWLSREV DHI
Length:293
Mass (Da):32,483
Last modified:December 21, 2004 - v1
Checksum:i4777ADEEFBCC2EC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70952.1.
RefSeqiWP_011228458.1. NC_006461.1.
YP_144395.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70952; BAD70952; BAD70952.
GeneIDi3168815.
KEGGittj:TTHA1129.
PATRICi23957217. VBITheThe93045_1108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70952.1.
RefSeqiWP_011228458.1. NC_006461.1.
YP_144395.1. NC_006461.1.

3D structure databases

ProteinModelPortaliQ5SJ85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70952; BAD70952; BAD70952.
GeneIDi3168815.
KEGGittj:TTHA1129.
PATRICi23957217. VBITheThe93045_1108.

Phylogenomic databases

eggNOGiENOG4105CYW. Bacteria.
COG0010. LUCA.
HOGENOMiHOG000204320.
KOiK01480.
OMAiSHASIMF.
PhylomeDBiQ5SJ85.

Enzyme and pathway databases

UniPathwayiUPA00248.
BioCyciMetaCyc:MONOMER-16737.
TTHE300852:GH8R-1161-MONOMER.
BRENDAi3.5.3.24. 2305.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSEPBH_THET8
AccessioniPrimary (citable) accession number: Q5SJ85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In T.thermophilus, the biosynthetic pathways of spermidine operates via N1-aminopropylagmatine without the production of putrescine.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.