PTC_LEVBR
ID PTC_LEVBR Reviewed; 349 AA.
AC Q7B9Y6; B8PV38;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 73.
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}; Synonyms=otc;
OS Levilactobacillus brevis (Lactobacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IOEB 9809;
RX PubMed=14659544; DOI=10.1016/s0378-1097(03)00787-0;
RA Lucas P., Landete J., Coton M., Coton E., Lonvaud-Funel A.;
RT "The tyrosine decarboxylase operon of Lactobacillus brevis IOEB 9809:
RT characterization and conservation in tyramine-producing bacteria.";
RL FEMS Microbiol. Lett. 229:65-71(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NS77;
RA Coton E., Coton M.;
RT "tyrdc locus polymorphism in Lactobacillus brevis indicates that the
RT tyramine-producing pathway corresponds to a strain-dependent genomic
RT island.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF446085; AAQ83560.4; -; Genomic_DNA.
DR EMBL; EU195891; ABY71224.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7B9Y6; -.
DR SMR; Q7B9Y6; -.
DR UniPathway; UPA00534; UER00941.
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; Transferase.
FT CHAIN 1..349
FT /note="Putrescine carbamoyltransferase"
FT /id="PRO_0000380719"
FT BINDING 55..59
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT BINDING 106
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT BINDING 133
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT BINDING 272..275
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT SITE 30
FT /note="Important for structural integrity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT SITE 146
FT /note="Important for structural integrity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT CONFLICT 222
FT /note="F -> L (in Ref. 2; ABY71224)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="R -> H (in Ref. 2; ABY71224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39295 MW; D92FF9D99D4BABB9 CRC64;
MNMTKRDFID TNTYTKEEIQ YMIDLGIKIK ESIKNGYYPP LLKNKTLGMI FEQSSTRTRT
SAEAAMTELG GHAQYLAPGQ IQLGGHETIE DTSQVLGRIL DIIGARVERH HTVAEVGKFA
KVPVVNFMSD YNHPTQELGD IITMTEHLPK GKKLSDCKIV FVGDATQVCV STMFMATKMG
MDFVQFGPKG FQIKPETLKI GQQNAKVSGG SVTITEDADE AFKDADFIYT DVWYGLYEAE
LSEEDRMKIF YPKYQVNAEL VAKASDHVKF MHCLPATRGE EVTDEVIDSD YSIVWDEAEN
RKTAMRAIFV YLLNPELRKA QASQAVADKY DAEFSLMLRN AVDDQRNAD
