ID PTC_ENTFA Reviewed; 339 AA. AC Q837U7; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Putrescine carbamoyltransferase; DE Short=PTC; DE Short=PTCase; DE EC=2.1.3.6 {ECO:0000269|PubMed:17028272, ECO:0000269|PubMed:22363663, ECO:0000269|PubMed:4621632}; DE AltName: Full=Agmatine catabolism protein B; DE AltName: Full=Putrescine transcarbamoylase; DE AltName: Full=Putrescine transcarbamylase; GN Name=ptcA; Synonyms=agcB, argF-2; OrderedLocusNames=EF_0732; OS Enterococcus faecalis (strain ATCC 700802 / V583). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=226185; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700802 / V583; RX PubMed=12663927; DOI=10.1126/science.1080613; RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C., RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.; RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus RT faecalis."; RL Science 299:2071-2074(2003). RN [2] RP PROTEIN SEQUENCE OF 1-14, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION, RP CRYSTALLIZATION, AND KINETIC PARAMETERS. RC STRAIN=SD10; RX PubMed=17028272; DOI=10.1128/jb.01216-06; RA Llacer J.L., Polo L.M., Tavarez S., Alarcon B., Hilario R., Rubio V.; RT "The gene cluster for agmatine catabolism of Enterococcus faecalis: study RT of recombinant putrescine transcarbamylase and agmatine deiminase and a RT snapshot of agmatine deiminase catalyzing its reaction."; RL J. Bacteriol. 189:1254-1265(2007). RN [3] RP PROTEIN SEQUENCE OF 2-30. RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1; RX PubMed=2516870; DOI=10.1099/00221287-135-9-2453; RA Tricot C., De Coen J.-L., Momin P., Falmagne P., Stalon V.; RT "Evolutionary relationships among bacterial carbamoyltransferases."; RL J. Gen. Microbiol. 135:2453-2464(1989). RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1; RX PubMed=4621632; DOI=10.1128/jb.109.1.44-50.1972; RA Roon R.J., Barker H.A.; RT "Fermentation of agmatine in Streptococcus faecalis: occurrence of RT putrescine transcarbamoylase."; RL J. Bacteriol. 109:44-50(1972). RN [5] RP SUBSTRATE SPECIFICITY, SUBUNIT, PH DEPENDENCE, AND ACTIVITY REGULATION. RX PubMed=116850; DOI=10.1111/j.1432-1033.1979.tb04226.x; RA Wargnies B., Lauwers N., Stalon V.; RT "Structure and properties of the putrescine carbamoyltransferase of RT Streptococcus faecalis."; RL Eur. J. Biochem. 101:143-152(1979). RN [6] RP GENE NAME. RX PubMed=15583144; DOI=10.1099/mic.0.27640-0; RA Naumoff D.G., Xu Y., Stalon V., Glansdorff N., Labedan B.; RT "The difficulty of annotating genes: the case of putrescine RT carbamoyltransferase."; RL Microbiology 150:3908-3911(2004). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 1-317, CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-54 AND 230-TYR--TYR-233. RX PubMed=22363663; DOI=10.1371/journal.pone.0031528; RA Polo L.M., Gil-Ortiz F., Cantin A., Rubio V.; RT "New insight into the transcarbamylase family: the structure of putrescine RT transcarbamylase, a key catalyst for fermentative utilization of RT agmatine."; RL PLoS ONE 7:e31528-e31528(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. Also has weak activity with CC ornithine and cadaverine. {ECO:0000269|PubMed:22363663, CC ECO:0000269|PubMed:4621632}. 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:0000269|PubMed:17028272, ECO:0000269|PubMed:22363663, CC ECO:0000269|PubMed:4621632}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21938; CC Evidence={ECO:0000269|PubMed:17028272, ECO:0000269|PubMed:22363663, CC ECO:0000269|PubMed:4621632}; CC -!- ACTIVITY REGULATION: Inhibited by spermidine (PubMed:116850). Inhibited CC by N-(phosphonoacetyl)-putrescine (PubMed:17028272, PubMed:4621632, CC PubMed:22363663). Inhibited by N-(phosphonoacetyl)-L-ornithine CC (PubMed:22363663). {ECO:0000269|PubMed:116850, CC ECO:0000269|PubMed:17028272, ECO:0000269|PubMed:22363663, CC ECO:0000269|PubMed:4621632}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=58 uM for carbamoyl phosphate {ECO:0000269|PubMed:17028272}; CC KM=2.3 mM for putrescine {ECO:0000269|PubMed:17028272}; CC KM=1.41 mM for putrescine {ECO:0000269|PubMed:22363663}; CC KM=36.4 mM for ornithine {ECO:0000269|PubMed:22363663}; CC pH dependence: CC Optimum pH is 6.7 with 10 mM putrescine and 10 mM carbamoyl CC phosphate, 7.8 with 0.2 mM putrescine and 0.2 mM carbamoyl phosphate, CC and 9.0 with 0.5 mM putrescine and 10 mM carbamoyl phosphate. CC {ECO:0000269|PubMed:116850}; CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via CC agmatine pathway; putrescine from N-carbamoylputrescine (transferase CC route): step 1/1. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:116850, CC ECO:0000269|PubMed:17028272}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. PTCase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016830; AAO80551.1; -; Genomic_DNA. DR RefSeq; NP_814481.1; NC_004668.1. DR RefSeq; WP_002355587.1; NZ_KE136527.1. DR PDB; 3TXX; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-339. DR PDB; 4A8H; X-ray; 2.50 A; A/B=1-339. DR PDB; 4A8P; X-ray; 2.00 A; A/B/C/D/E/F=1-339. DR PDB; 4A8T; X-ray; 1.59 A; A=1-317. DR PDB; 4AM8; X-ray; 1.99 A; A/B/C/D/E/F=1-339. DR PDBsum; 3TXX; -. DR PDBsum; 4A8H; -. DR PDBsum; 4A8P; -. DR PDBsum; 4A8T; -. DR PDBsum; 4AM8; -. DR AlphaFoldDB; Q837U7; -. DR SMR; Q837U7; -. DR STRING; 226185.EF_0732; -. DR EnsemblBacteria; AAO80551; AAO80551; EF_0732. DR GeneID; 60893028; -. DR KEGG; efa:EF0732; -. DR PATRIC; fig|226185.45.peg.2673; -. DR eggNOG; COG0078; Bacteria. DR HOGENOM; CLU_043846_3_1_9; -. DR BRENDA; 2.1.3.3; 2095. DR BRENDA; 2.1.3.6; 2095. DR SABIO-RK; Q837U7; -. DR UniPathway; UPA00534; UER00941. DR Proteomes; UP000001415; Chromosome. 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; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00658; orni_carb_tr; 1. DR NCBIfam; TIGR04384; putr_carbamoyl; 1. DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Polyamine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1..339 FT /note="Putrescine carbamoyltransferase" FT /id="PRO_0000112923" FT BINDING 52..56 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250" FT BINDING 130 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250" FT BINDING 268..271 FT /ligand="putrescine" FT /ligand_id="ChEBI:CHEBI:326268" FT /evidence="ECO:0000250" FT SITE 27 FT /note="Important for structural integrity" FT /evidence="ECO:0000250" FT SITE 143 FT /note="Important for structural integrity" FT /evidence="ECO:0000250" FT MUTAGEN 54 FT /note="R->G: Loss of activity with putrescine and FT ornithine." FT /evidence="ECO:0000269|PubMed:22363663" FT MUTAGEN 230..233 FT /note="YGLY->VSMG: Loss of activity with putrescine; FT increased activity with ornithine." FT /evidence="ECO:0000269|PubMed:22363663" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 13..31 FT /evidence="ECO:0007829|PDB:4A8T" FT TURN 38..41 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 43..50 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 54..65 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:4A8T" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:4AM8" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 86..96 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 131..143 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 155..161 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 164..175 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:3TXX" FT HELIX 192..205 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 215..218 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:4AM8" FT HELIX 239..246 FT /evidence="ECO:0007829|PDB:4A8T" FT TURN 247..250 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 254..260 FT /evidence="ECO:0007829|PDB:4A8T" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:4A8T" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 290..315 FT /evidence="ECO:0007829|PDB:4A8T" FT HELIX 320..335 FT /evidence="ECO:0007829|PDB:4AM8" SQ SEQUENCE 339 AA; 38343 MW; 1459EE8AC906CF96 CRC64; MKRDYVTTET YTKEEMHYLV DLSLKIKEAI KNGYYPQLLK NKSLGMIFQQ SSTRTRVSFE TAMEQLGGHG EYLAPGQIQL GGHETIEDTS RVLSRLVDIL MARVERHHSI VDLANCATIP VINGMSDYNH PTQELGDLCT MVEHLPEGKK LEDCKVVFVG DATQVCFSLG LITTKMGMNF VHFGPEGFQL NEEHQAKLAK NCEVSGGSFL VTDDASSVEG ADFLYTDVWY GLYEAELSEE ERMKVFYPKY QVNQEMMDRA GANCKFMHCL PATRGEEVTD EVIDGKNSIC FDEAENRLTS IRGLLVYLMN DYEAKNPYDL IKQAEAKKEL EVFLDTQSI //