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Protein

N(1)-aminopropylagmatine ureohydrolase

Gene

TTHA1129

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Catalytic activityi

N1-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)DescriptionActionsGraphical viewLength
Metal bindingi105Manganese 1PROSITE-ProRule annotation1
Metal bindingi128Manganese 1PROSITE-ProRule annotation1
Metal bindingi128Manganese 2PROSITE-ProRule annotation1
Metal bindingi130Manganese 2PROSITE-ProRule annotation1
Metal bindingi132Manganese 1PROSITE-ProRule annotation1
Metal bindingi210Manganese 1PROSITE-ProRule annotation1
Metal bindingi210Manganese 2PROSITE-ProRule annotation1
Metal bindingi212Manganese 2PROSITE-ProRule annotation1

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

Keywordsi

Molecular functionHydrolase
Biological processPolyamine biosynthesis, Spermidine biosynthesis
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16737
TTHE300852:G1GKC-1134-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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004298631 – 293N(1)-aminopropylagmatine ureohydrolaseAdd BLAST293

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1129

Structurei

3D structure databases

ProteinModelPortaliQ5SJ85
SMRiQ5SJ85
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CYW Bacteria
COG0010 LUCA
HOGENOMiHOG000204320
KOiK01480
OMAiDTYFGAE
PhylomeDBiQ5SJ85

Family and domain databases

InterProiView protein in InterPro
IPR005925 Agmatinase-rel
IPR006035 Ureohydrolase
IPR023696 Ureohydrolase_dom_sf
PfamiView protein in Pfam
PF00491 Arginase, 1 hit
PIRSFiPIRSF036979 Arginase, 1 hit
SUPFAMiSSF52768 SSF52768, 1 hit
TIGRFAMsiTIGR01230 agmatinase, 1 hit
PROSITEiView protein in PROSITE
PS51409 ARGINASE_2, 1 hit

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
PATRICifig|300852.9.peg.1108

Similar proteinsi

Entry informationi

Entry nameiSEPBH_THET8
AccessioniPrimary (citable) accession number: Q5SJ85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: December 21, 2004
Last modified: March 28, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome