(data stored in SCRATCH3701 zone)

SWISSPROT: 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   11-DEC-2019, entry version 107.
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}.
DR   EMBL; AL591973; CAC98251.1; -; Genomic_DNA.
DR   PIR; AE1079; AE1079.
DR   RefSeq; NP_463569.1; NC_003210.1.
DR   RefSeq; WP_003721659.1; NC_003210.1.
DR   SMR; Q8YAS7; -.
DR   STRING; 169963.lmo0036; -.
DR   PaxDb; Q8YAS7; -.
DR   EnsemblBacteria; CAC98251; CAC98251; CAC98251.
DR   GeneID; 39648696; -.
DR   GeneID; 985152; -.
DR   KEGG; lmo:lmo0036; -.
DR   PATRIC; fig|169963.11.peg.37; -.
DR   eggNOG; ENOG4105DBV; Bacteria.
DR   eggNOG; COG0078; LUCA.
DR   HOGENOM; HOG000022686; -.
DR   KO; K13252; -.
DR   OMA; VVYTTRW; -.
DR   PhylomeDB; Q8YAS7; -.
DR   BioCyc; LMON169963:LMO0036-MONOMER; -.
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;
DR   PRODOM; Q8YAS7.
DR   SWISS-2DPAGE; Q8YAS7.
KW   Cytoplasm; Polyamine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..341
FT                   /note="Putrescine carbamoyltransferase"
FT                   /id="PRO_0000112946"
FT   REGION          54..58
FT                   /note="Carbamoyl phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   REGION          271..274
FT                   /note="Putrescine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   BINDING         105
FT                   /note="Carbamoyl phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT   BINDING         132
FT                   /note="Carbamoyl phosphate"
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
//

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