ID   AGUB_SOLTU              Reviewed;         300 AA.
AC   Q3HVN1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=N-carbamoylputrescine amidase;
DE            EC=3.5.1.53;
GN   Name=CPA;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kuras; TISSUE=Tuber;
RA   Nielsen K.L., Welinder K.G., Nielsen H.V., Emmersen J.M.G.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in polyamine biosynthesis. {ECO:0000250}.
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; DQ191642; ABA40443.1; -; mRNA.
DR   RefSeq; NP_001275125.1; NM_001288196.1.
DR   AlphaFoldDB; Q3HVN1; -.
DR   SMR; Q3HVN1; -.
DR   STRING; 4113.PGSC0003DMT400067716; -.
DR   GeneID; 102600318; -.
DR   KEGG; sot:102600318; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   InParanoid; Q3HVN1; -.
DR   OrthoDB; 996578at2759; -.
DR   UniPathway; UPA00534; UER00286.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q3HVN1; baseline.
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_0000261604"
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;  82F4121E79E4D2F0 CRC64;
     MAEKNRLVTV AALQFACTDD VSTNVATAER LVRAAHQKGA NIILIQELFE GYYFCQAQKE
     EFFHRAKPYL GHPTIVRMQN LAKELGVVIP VSFFEEANNA HYNSVAIIDA DGTDLGLYRK
     SHIPDGPGYQ EKFYFNPGDT GFKVFQTKYA KIGVAICWDQ WFPEAARAMA LQGAEVLFYP
     TAIGSEPQDD GLDSRDHWRR VMQGHAGANV VPLVASNRIG KEIIETEHGN SEITFYGYSF
     IAGPTGELVA AAGDKEEAVL VAQFDLDKIK SKRHGWGVYR DRRPDLYKVL LTLDGSNPVK