SEPBH_THET8
ID SEPBH_THET8 Reviewed; 293 AA.
AC Q5SJ85;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-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=TTHA1129;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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).
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. It cannot use agmatine as substrate.
CC {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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a significant defect
CC of growth at 78 degrees Celsius and accumulate N1-aminopropylagmatine.
CC The double mutant of speB and speE shows defective growth at 70 degrees
CC Celsius and significant defective growth at 78 degrees Celsius. It
CC accumulates agmatine and N1-aminopropylagmatine.
CC {ECO:0000269|PubMed:15983049}.
CC -!- MISCELLANEOUS: In T.thermophilus, the biosynthetic pathways of
CC spermidine operates via N1-aminopropylagmatine without the production
CC of putrescine. {ECO:0000305|PubMed:15983049}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; AP008226; BAD70952.1; -; Genomic_DNA.
DR RefSeq; WP_011228458.1; NC_006461.1.
DR RefSeq; YP_144395.1; NC_006461.1.
DR AlphaFoldDB; Q5SJ85; -.
DR SMR; Q5SJ85; -.
DR STRING; 300852.55772511; -.
DR EnsemblBacteria; BAD70952; BAD70952; BAD70952.
DR GeneID; 3168815; -.
DR KEGG; ttj:TTHA1129; -.
DR PATRIC; fig|300852.9.peg.1108; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_0_2_0; -.
DR OMA; YELTTIM; -.
DR PhylomeDB; Q5SJ85; -.
DR BioCyc; MetaCyc:MON-16737; -.
DR BRENDA; 3.5.3.24; 2305.
DR UniPathway; UPA00248; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043920; F:aminopropylagmatine ureohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:UniProtKB.
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 Cytoplasm; Hydrolase; Manganese; Metal-binding; Polyamine biosynthesis;
KW Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..293
FT /note="N(1)-aminopropylagmatine ureohydrolase"
FT /id="PRO_0000429863"
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"
SQ SEQUENCE 293 AA; 32483 MW; 4777ADEEFBCC2EC5 CRC64;
MRLVFGEKDT PYEEARVVVL PVPYDLSLSF LPGARRGPEA ILLASRELEP FLLELGAAPE
EVGIHAAEPV PWVAGMAEES HRLIREEALR HLRAGKWVVA LGGDHSVTHP LVQAHREALG
DFSLLHVDAH ADLYPEWQGS VYSHASPFYR LLTEGFPLVQ VGIRAMDRDS LRLARKKGVA
LFPAHRIHRE GLPLDEILRA LGKRVYISLD FDALDPSLMP SVGTPLPGGL SYRQVVDLLE
AVFREKEVVG MDFVELSPNG QFHAEMTAAQ LVYHAIGLKG LQAGWLSREV DHI
