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 27-MAR-2024, entry version 95.
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; Bacillota; 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 GeneID; 33062946; -.
DR KEGG; ppe:PEPE_0189; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_9; -.
DR OrthoDB; 9802587at2; -.
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; 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 3: Inferred from homology;
KW Cytoplasm; Polyamine biosynthesis; 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
//
