PTC_ENTFA
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 03-AUG-2022, entry version 122.
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; Firmicutes; 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}.
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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 OMA; RMAIFYP; -.
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; -; 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 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
