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PTC_PEDPA
ID   PTC_PEDPA               Reviewed;         344 AA.
AC   Q03HM9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=PEPE_0189;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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).
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; CP000422; ABJ67293.1; -; Genomic_DNA.
DR   RefSeq; WP_011672910.1; NC_008525.1.
DR   AlphaFoldDB; Q03HM9; -.
DR   SMR; Q03HM9; -.
DR   STRING; 278197.PEPE_0189; -.
DR   EnsemblBacteria; ABJ67293; ABJ67293; PEPE_0189.
DR   GeneID; 33062946; -.
DR   KEGG; ppe:PEPE_0189; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_1_9; -.
DR   OMA; RMAIFYP; -.
DR   OrthoDB; 988597at2; -.
DR   UniPathway; UPA00534; UER00941.
DR   Proteomes; UP000000773; 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   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..344
FT                   /note="Putrescine carbamoyltransferase"
FT                   /id="PRO_0000380723"
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   344 AA;  38811 MW;  50B56D9C6A09A0AA CRC64;
     MNTKRDFIDT NTYTQEEITY MINLGLKIKE SIKNGYYPPL LKNKTLGMIF EQSSTRTRTS
     AEAAMTELGG HAQYLAPGQI QLGGHETIED TSQVLGRILD IIGARVDRHK TVAEVGKYAK
     VPVVNFMSDY NHPTQELGDI TTMVEHLPAG KKLSDCKIVF VGDATQVCVS TMFMTTKMGM
     DFVQFGPKGF QMKDDVVEIG KENAKKYGGS VTITEDADEA MKDADFVYTD VWYGLYDDEM
     PKEERMNIFY PKYQVNAELM AKASDHVKFM HCLPATRGEE VTDEVLDSDY SIVWDEAENR
     KTAMRAIFVY LLNPSLNYAS KAVAEKYDAE FELMLKNAVD SRNN
 
 
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