PTC_LISMF
ID PTC_LISMF Reviewed; 341 AA.
AC Q725C8;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=argF-1;
GN OrderedLocusNames=LMOf2365_0045;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT02833.1; -; Genomic_DNA.
DR RefSeq; WP_003724872.1; NC_002973.6.
DR AlphaFoldDB; Q725C8; -.
DR SMR; Q725C8; -.
DR KEGG; lmf:LMOf2365_0045; -.
DR HOGENOM; CLU_043846_3_1_9; -.
DR OMA; RMAIFYP; -.
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_0000112944"
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
