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PTC_LISMC
ID   PTC_LISMC               Reviewed;         341 AA.
AC   C1KV77;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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}; OrderedLocusNames=Lm4b_00045;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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}.
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DR   EMBL; FM242711; CAS03835.1; -; Genomic_DNA.
DR   RefSeq; WP_003724872.1; NC_012488.1.
DR   AlphaFoldDB; C1KV77; -.
DR   SMR; C1KV77; -.
DR   PRIDE; C1KV77; -.
DR   KEGG; lmc:Lm4b_00045; -.
DR   HOGENOM; CLU_043846_3_1_9; -.
DR   OMA; RMAIFYP; -.
DR   BioCyc; LMON568819:LM4B_RS00230-MON; -.
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..341
FT                   /note="Putrescine carbamoyltransferase"
FT                   /id="PRO_1000216419"
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         271..274
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   341 AA;  38469 MW;  8027DF93BDBE9D12 CRC64;
     MNKKRDFIDT KDFSKEEILF MIEIGRKMKE SIKNGHYPQL LKHKTLGMIF EQSSTRTRVS
     FETAMTQLGG HAQYLAPGQI QLGGHESVGD TAKVLSRLVD ILMARVERHQ TVVELANTAA
     IPVINGMSDY NHPTQELGDA ITMFEHLPKG KKIEDCKIVF VGDATQVCAS TMFMATKLGM
     DFVQFGPKGF QLREEHLKIA EENCKVSGGS YLITEDVDIA LKDADFIYTD VWYGLYEAEL
     SEEERMKTFY PKYQVNKELI SKAAPHVKFM HCLPATRGEE VTDEVLDAPY SVVIDEAENR
     LTAMRALLVY FMNPYVREAG FAVAEKYDAE LELLLRNGAG L
 
 
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