PTC_LACLA
ID PTC_LACLA Reviewed; 340 AA.
AC Q9CEY4;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=otcA;
GN OrderedLocusNames=LL1700; ORFNames=L0113;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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: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; AE005176; AAK05798.1; -; Genomic_DNA.
DR PIR; D86837; D86837.
DR RefSeq; NP_267856.1; NC_002662.1.
DR RefSeq; WP_003130905.1; NC_002662.1.
DR AlphaFoldDB; Q9CEY4; -.
DR SMR; Q9CEY4; -.
DR STRING; 272623.L0113; -.
DR PaxDb; Q9CEY4; -.
DR EnsemblBacteria; AAK05798; AAK05798; L0113.
DR GeneID; 66442681; -.
DR KEGG; lla:L0113; -.
DR PATRIC; fig|272623.7.peg.1824; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_9; -.
DR OMA; RMAIFYP; -.
DR UniPathway; UPA00534; UER00941.
DR Proteomes; UP000002196; 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..340
FT /note="Putrescine carbamoyltransferase"
FT /id="PRO_0000112934"
FT BINDING 56..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT BINDING 107
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT BINDING 134
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 31
FT /note="Important for structural integrity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
FT SITE 147
FT /note="Important for structural integrity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02102"
SQ SEQUENCE 340 AA; 37844 MW; 94BC8CCBC4250A2D CRC64;
MVTTNKRDFI TTEDYTKEEI LDIVTLGLKI KAAIKNGYYP PLLKNKSLGM IFQQTSTRTR
VSFETAMTQL GGHAEYLAPG QIQLGGHETI EDTSTVLSRL LDIIMARVDR HESVNNLAKH
TTIPVLNGMS DYNHPTQEVG DLTTMIEHLP AGKKLEDCKV VFVGDATQVC FSLGLIATKM
GMHFVHFGPK GYQLNEEHQA KLAANCEVSG GTYEVTDDEE SIVGADFLYT DVWYGLYDAE
LSEEERLAIF FPKYQVTPEM MAKAGAHTKF MHCLPASRGE EVVDAVIDGP NSICFDEAEN
RLTSIRALLV WLMSDYAEKN PYDLKAQAKA KAELEAYLAK
