PTC_STRMU
ID PTC_STRMU Reviewed; 339 AA.
AC Q8DW19; Q6IFZ2;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putrescine carbamoyltransferase;
DE Short=PTC;
DE Short=PTCase;
DE EC=2.1.3.6;
DE AltName: Full=Putrescine transcarbamoylase;
DE AltName: Full=Putrescine transcarbamylase;
GN Name=ptcA; Synonyms=aguB, arcB; OrderedLocusNames=SMU_262;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN AGMATINE CATABOLISM, AND
RP INDUCTION.
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=14996823; DOI=10.1128/jb.186.6.1902-1904.2004;
RA Griswold A.R., Chen Y.-Y.M., Burne R.A.;
RT "Analysis of an agmatine deiminase gene cluster in Streptococcus mutans
RT UA159.";
RL J. Bacteriol. 186:1902-1904(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3]
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 [4]
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 (Probable). Is involved in the
CC degradation pathway of the polyamine agmatine.
CC {ECO:0000269|PubMed:14996823, ECO:0000305}.
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 -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from N-carbamoylputrescine (transferase
CC route): step 1/1.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by agmatine. Expressed under the control of
CC carbohydrate catabolite repression. {ECO:0000269|PubMed:14996823}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. PTCase family. {ECO:0000305}.
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DR EMBL; BK004003; DAA04556.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58031.1; -; Genomic_DNA.
DR RefSeq; NP_720725.1; NC_004350.2.
DR RefSeq; WP_002282737.1; NC_004350.2.
DR AlphaFoldDB; Q8DW19; -.
DR SMR; Q8DW19; -.
DR STRING; 210007.SMU_262; -.
DR PRIDE; Q8DW19; -.
DR EnsemblBacteria; AAN58031; AAN58031; SMU_262.
DR GeneID; 66818250; -.
DR KEGG; smu:SMU_262; -.
DR PATRIC; fig|210007.7.peg.228; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_9; -.
DR OMA; RMAIFYP; -.
DR PhylomeDB; Q8DW19; -.
DR UniPathway; UPA00534; UER00941.
DR Proteomes; UP000002512; 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 1: Evidence at protein level;
KW Cytoplasm; Polyamine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..339
FT /note="Putrescine carbamoyltransferase"
FT /id="PRO_0000113034"
FT BINDING 54..58
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT SITE 29
FT /note="Important for structural integrity"
FT /evidence="ECO:0000250"
FT SITE 145
FT /note="Important for structural integrity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 38519 MW; A51CA727DC5BA8CC CRC64;
MMKKTDYITT EDFSKEELLK LVDLSLKIKA CIKNGYYPPL LEHKSLGMIF QQTSTRTRVS
FETAMSQLGG HAQYLAPGQI QLGGHETIED TSTVLSRLDD ILMARVERHQ SVVDLARCAS
IPVINGMSDY NHPTQELGDL CTMIEHLPAG KKLEDCKVVF VGDATQVCFS LALITTKMGM
EFVHFGPKGF QLNDMHKEKL DKICERSGGK YTVTDNEDAI EGADFLYTDV WYGLYEAELS
EEERMQIFFP KYQVDSQMMA KAGADCKFMH CLPATRGEEI TDEVMDGPHS ICFDEAENRL
TSIRGLLVYL LRDYREKNPY DLVKQEKAKE ELETFLKPE
