PTC_LISMO
ID PTC_LISMO Reviewed; 341 AA.
AC Q8YAS7;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=lmo0036;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP REANNOTATION AS A PTCASE.
RX PubMed=15287962; DOI=10.1186/1471-2164-5-52;
RA Naumoff D.G., Xu Y., Glansdorff N., Labedan B.;
RT "Retrieving sequences of enzymes experimentally characterized but
RT erroneously annotated: the case of the putrescine carbamoyltransferase.";
RL BMC Genomics 5:52-52(2004).
RN [3]
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).
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:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. PTCase family. {ECO:0000255|HAMAP-Rule:MF_02102}.
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DR EMBL; AL591973; CAC98251.1; -; Genomic_DNA.
DR PIR; AE1079; AE1079.
DR RefSeq; NP_463569.1; NC_003210.1.
DR RefSeq; WP_003721659.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8YAS7; -.
DR SMR; Q8YAS7; -.
DR STRING; 169963.lmo0036; -.
DR PaxDb; Q8YAS7; -.
DR EnsemblBacteria; CAC98251; CAC98251; CAC98251.
DR GeneID; 985152; -.
DR KEGG; lmo:lmo0036; -.
DR PATRIC; fig|169963.11.peg.37; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_9; -.
DR OMA; RMAIFYP; -.
DR PhylomeDB; Q8YAS7; -.
DR BioCyc; LMON169963:LMO0036-MON; -.
DR UniPathway; UPA00534; UER00941.
DR Proteomes; UP000000817; 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; IBA:GO_Central.
DR GO; GO:0050231; F:putrescine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..341
FT /note="Putrescine carbamoyltransferase"
FT /id="PRO_0000112946"
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; 38428 MW; 266C2B25ABD24E6B CRC64;
MNKKRDFIDT KDFSKEEILF MIEIGRKMKE SIKNGHYPQL LKHKTLGMIF EQSSTRTRVS
FETAMTQLGG HAQYLAPGQI QLGGHESVGD TAKVLSRLVD ILMARVERHQ TVVELANTAA
IPVINGMSDY NHPTQELGDA ITMFEHLPKG KKIEDCKIVF VGDATQVCAS TMFMATKLGM
DFVQFGPKGF QLREEHLKVA EENCEVSGGS YLITEDVDIA LKDADFIYTD VWYGLYEAEL
SEEERMKTFY PKYQVNKELI SKAAPHVKFM HCLPATRGEE VTDEVLDAPY SVVIDEAENR
LTAMRALLVY FMNPYVKEAG FAVAEKYDAE LELLLRNGAG L
