SPEBH_THET2
ID SPEBH_THET2 Reviewed; 293 AA.
AC Q72JK8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=N(1)-aminopropylagmatine ureohydrolase;
DE EC=3.5.3.24;
DE AltName: Full=Protein SpeB homolog;
GN OrderedLocusNames=TT_C0764;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15983049; DOI=10.1074/jbc.m413332200;
RA Ohnuma M., Terui Y., Tamakoshi M., Mitome H., Niitsu M., Samejima K.,
RA Kawashima E., Oshima T.;
RT "N1-aminopropylagmatine, a new polyamine produced as a key intermediate in
RT polyamine biosynthesis of an extreme thermophile, Thermus thermophilus.";
RL J. Biol. Chem. 280:30073-30082(2005).
RN [3]
RP PATHWAY.
RX PubMed=20675472; DOI=10.1128/jb.00279-10;
RA Morimoto N., Fukuda W., Nakajima N., Masuda T., Terui Y., Kanai T.,
RA Oshima T., Imanaka T., Fujiwara S.;
RT "Dual biosynthesis pathway for longer-chain polyamines in the
RT hyperthermophilic archaeon Thermococcus kodakarensis.";
RL J. Bacteriol. 192:4991-5001(2010).
CC -!- FUNCTION: Involved in the biosynthesis of polyamines which are thought
CC to support the growth of thermophilic microorganisms under high-
CC temperature conditions. It seems that long-chain and branched-chain of
CC polyamines effectively stabilize DNA and RNA, respectively. Catalyzes
CC the decarboxylation of N1-(3-aminopropyl)agmatine to yield spermidine
CC and urea. Does not act on agmatine. {ECO:0000269|PubMed:15983049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-aminopropylagmatine = spermidine + urea;
CC Xref=Rhea:RHEA:35827, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:64335; EC=3.5.3.24;
CC Evidence={ECO:0000269|PubMed:15983049};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis.
CC {ECO:0000269|PubMed:20675472}.
CC -!- MISCELLANEOUS: The biosynthetic pathway, by which spermidine is
CC synthesized from agmatine via N1-aminopropylagmatine has been
CC characterized in the hyperthermophilic archaeon Pyrococcus kodakarensis
CC and the thermophilic Gram-negative bacterium Thermus thermophilus.
CC {ECO:0000305|PubMed:20675472}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017221; AAS81110.1; -; Genomic_DNA.
DR RefSeq; WP_011173199.1; NC_005835.1.
DR AlphaFoldDB; Q72JK8; -.
DR SMR; Q72JK8; -.
DR STRING; 262724.TT_C0764; -.
DR EnsemblBacteria; AAS81110; AAS81110; TT_C0764.
DR KEGG; tth:TT_C0764; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_0_2_0; -.
DR OMA; YELTTIM; -.
DR OrthoDB; 1598732at2; -.
DR UniPathway; UPA00248; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0043920; F:aminopropylagmatine ureohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01230; agmatinase; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Manganese; Metal-binding; Polyamine biosynthesis;
KW Spermidine biosynthesis.
FT CHAIN 1..293
FT /note="N(1)-aminopropylagmatine ureohydrolase"
FT /id="PRO_0000424213"
FT BINDING 105
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 210
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 210
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT SITE 144
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 32454 MW; 5C7CB462E7C57B5F CRC64;
MRLVFGEKDA PYEEARVVVL PVPYDLSLSF LPGARRGPEA ILLASRELEP FLLELGAAPE
EVGIHAAEPV PWVAGMAEES HRLIREEALK HLRAGKWLVA LGGDHSVTHP LVQAHREALG
EFSLLHVDAH ADLYPEWQGS VYSHASPFYR LLTEGFPLVQ VGIRAMDRDS LRLARKRGVA
LFPAHRIHRE GLPLDEILEA LGKRVYISLD FDALDPSLMP SVGTPLPGGL SYRQVVDLLE
AVFREKEVVG MDFVELSPNG QFHAEMTAAQ LVYHAIGLKG LQAGWLSREV DHI
