ID   PTC_STRRT               Reviewed;         339 AA.
AC   B7S4N1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Putrescine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_02102};
DE            Short=PTC {ECO:0000255|HAMAP-Rule:MF_02102};
DE            Short=PTCase {ECO:0000255|HAMAP-Rule:MF_02102};
DE            EC=2.1.3.6 {ECO:0000255|HAMAP-Rule:MF_02102};
DE   AltName: Full=Putrescine transcarbamoylase {ECO:0000255|HAMAP-Rule:MF_02102};
DE   AltName: Full=Putrescine transcarbamylase {ECO:0000255|HAMAP-Rule:MF_02102};
GN   Name=ptcA {ECO:0000255|HAMAP-Rule:MF_02102}; Synonyms=aguB;
OS   Streptococcus ratti.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FA-1;
RX   PubMed=19121075; DOI=10.1111/j.1399-302x.2008.00459.x;
RA   Griswold A.R., Nascimento M.M., Burne R.A.;
RT   "Distribution, regulation and role of the agmatine deiminase system in
RT   mutans streptococci.";
RL   Oral Microbiol. Immunol. 24:79-82(2009).
CC   -!- FUNCTION: Catalyzes the phosphorolysis of N-carbamoylputrescine to form
CC       carbamoyl phosphate and putrescine. Is involved in the degradation
CC       pathway of the polyamine agmatine. {ECO:0000255|HAMAP-Rule:MF_02102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + putrescine = H(+) + N-
CC         carbamoylputrescine + phosphate; Xref=Rhea:RHEA:21936,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:58318, ChEBI:CHEBI:326268; EC=2.1.3.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02102};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       agmatine pathway; putrescine from N-carbamoylputrescine (transferase
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_02102}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_02102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02102}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. PTCase family. {ECO:0000255|HAMAP-Rule:MF_02102}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN81019.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; EF104920; ABN81019.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B7S4N1; -.
DR   SMR; B7S4N1; -.
DR   PRIDE; B7S4N1; -.
DR   UniPathway; UPA00534; UER00941.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProt.
DR   GO; GO:0050231; F:putrescine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033390; P:putrescine biosynthetic process from arginine via N-carbamoylputrescine; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_02102; PTCase; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024903; PtcA.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR   TIGRFAMs; TIGR04384; putr_carbamoyl; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Transferase.
FT   CHAIN           1..339
FT                   /note="Putrescine carbamoyltransferase"
FT                   /id="PRO_0000380724"
FT   BINDING         54..58
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   BINDING         105
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   BINDING         132
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   BINDING         270..273
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   SITE            29
FT                   /note="Important for structural integrity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   SITE            145
FT                   /note="Important for structural integrity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
SQ   SEQUENCE   339 AA;  38476 MW;  6316AD392B311804 CRC64;
     MMKKTDYITT EDFSKEELLK LVDLSLKIKA CIKNGYYPPL LEHKSLGMIF QQTSTRTRVS
     FETAMSQLGG HAQYLAPGQI QLGGHETIED TSTVLSRLDD ILMARVERHQ SVVDLARCAS
     IPVINGMSDY NHPTQELGDL CTMIEHLPAG KKLEDCKVVF VGDATQVCFS LALITTKMGM
     EFVHFGPKGF QLNDMHKEEL DKICELSGGK YTVTDNEDAI EGANFLYTDV WYGLYEAELS
     EEERMQIFFP KYQVDSQMMA KAGADCKFMH CLPATRGEEI TDEVMDGPHS ICFDEAENRL
     TSIRGLLVYL LRDYREKNPY DLVKQEKAKE ELETFLKPE