PTC_MYCMS
ID PTC_MYCMS Reviewed; 365 AA.
AC Q6MSR6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=arcB;
GN OrderedLocusNames=MSC_0703;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
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; BX293980; CAE77322.1; -; Genomic_DNA.
DR RefSeq; NP_975680.1; NC_005364.2.
DR AlphaFoldDB; Q6MSR6; -.
DR SMR; Q6MSR6; -.
DR STRING; 272632.MSC_0703; -.
DR EnsemblBacteria; CAE77322; CAE77322; MSC_0703.
DR KEGG; mmy:MSC_0703; -.
DR PATRIC; fig|272632.4.peg.757; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_14; -.
DR OMA; DGNNVCN; -.
DR UniPathway; UPA00534; UER00941.
DR Proteomes; UP000001016; 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.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Polyamine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..365
FT /note="Putrescine carbamoyltransferase"
FT /id="PRO_0000380722"
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 277..280
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 365 AA; 42280 MW; DCCECD36DED69238 CRC64;
MNKVRHFIDT QDLSKKEIFE IFRLMKMLKE ARYCGAVPEL LKNKTLAMIF EEPSTRTRVS
FEAAMTLLGG HAQYLKPGEL HLGVRESLYD TTKVLSHMCD GIMCRALKNE TVLNLAKYAD
VPVLNGLTDY NHPTQAICDV FTMLEYMPAT KNLEYEDIKF EDIKVVFIGD RTNVCSSTMH
ITTKLGMNFV HISPKRYQSP QEWIDIANEN IKQANSGSVL VTDDLEQVRG ADIVYTDLWW
WVDQEDEAEE RVKAFKPTYQ VTPELMEKAG KQALFMHCLP ASRNVEVYDE VIDSDQSIAF
EQAENRLTAQ MGLLVYYLYP QIDKSSNAVK DYYRGKVEAF MEHQDRSWKQ RYTYNNDYAE
TKNKK
