AGUB_SOLLC
ID AGUB_SOLLC Reviewed; 300 AA.
AC Q9XGI9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=N-carbamoylputrescine amidase;
DE EC=3.5.1.53;
GN Name=CPA;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. West Virginia 106; TISSUE=Fruit;
RA Chevalier C., Joubes J., Petit J., Raymond P.;
RT "Isolation and characterization of a cDNA clone for a putative beta-alanine
RT synthase from tomato (Lycopersicon esculentum Mill.) developing fruits.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=12435743; DOI=10.1074/jbc.m205699200;
RA Piotrowski M., Janowitz T., Kneifel H.;
RT "Plant C-N hydrolases and the identification of a plant N-
RT carbamoylputrescine amidohydrolase involved in polyamine biosynthesis.";
RL J. Biol. Chem. 278:1708-1712(2003).
CC -!- FUNCTION: Involved in polyamine biosynthesis.
CC {ECO:0000269|PubMed:12435743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O + N-carbamoylputrescine = CO2 + NH4(+) +
CC putrescine; Xref=Rhea:RHEA:22284, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58318, ChEBI:CHEBI:326268; EC=3.5.1.53;
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from N-carbamoylputrescine (amidase
CC route): step 1/1.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; Y19104; CAB45873.1; -; mRNA.
DR RefSeq; NP_001234385.1; NM_001247456.1.
DR AlphaFoldDB; Q9XGI9; -.
DR SMR; Q9XGI9; -.
DR STRING; 4081.Solyc11g068540.1.1; -.
DR PaxDb; Q9XGI9; -.
DR PRIDE; Q9XGI9; -.
DR EnsemblPlants; Solyc11g068540.2.1; Solyc11g068540.2.1; Solyc11g068540.2.
DR GeneID; 544141; -.
DR Gramene; Solyc11g068540.2.1; Solyc11g068540.2.1; Solyc11g068540.2.
DR KEGG; sly:544141; -.
DR eggNOG; KOG0806; Eukaryota.
DR HOGENOM; CLU_030130_4_0_1; -.
DR InParanoid; Q9XGI9; -.
DR OMA; NAPYFCQ; -.
DR OrthoDB; 996578at2759; -.
DR PhylomeDB; Q9XGI9; -.
DR UniPathway; UPA00534; UER00286.
DR Proteomes; UP000004994; Chromosome 11.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0050126; F:N-carbamoylputrescine amidase activity; IBA:GO_Central.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR017755; N-carbamoylputrescine_amidase.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR03381; agmatine_aguB; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Polyamine biosynthesis; Reference proteome.
FT CHAIN 1..300
FT /note="N-carbamoylputrescine amidase"
FT /id="PRO_0000261603"
FT DOMAIN 8..266
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 300 AA; 33405 MW; 4CE8C6540973C6BA CRC64;
MAEKNRLVTV AALQFACTDD VSTNVATAER LVRAAHQKGA NIILIQELFE GYYFCQAQKE
EFFHRAKPYP GHPTIVRMQN LAKELGVVIP VSFFEEANNA HYNSVAIIDA DGTDLGLYRK
SHIPDGPGYQ EKYYFNPGDT GFKVFQTKYA KIGVAICWDQ WFPEAARAMA LQGAEVLFYP
TAIGSEPQDD GLDSRDHWRR VMQGHAGANV VPLVASNRIG KEIIETEHGN SEITFYGYSF
IAGPTGELVA AAGDKEEAVL VAQFDLDKIK SKRHGWGVYR DRRPDLYKVL LTLDGSNPVK