OTCC_ENTFA
ID OTCC_ENTFA Reviewed; 339 AA.
AC Q839Q5; Q93K66;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic;
DE Short=OTCase;
DE EC=2.1.3.3;
GN Name=arcB; OrderedLocusNames=EF_0105;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29212 / DSM 2570;
RX PubMed=9578487; DOI=10.1046/j.1432-1327.1998.2530280.x;
RA Marina A., Uriarte M., Barcelona B., Fresquet V., Cervera J., Rubio V.;
RT "Carbamate kinase from Enterococcus faecalis and Enterococcus faecium:
RT cloning of the genes, studies on the enzyme expressed in Escherichia coli,
RT and sequence similarity with N-acetyl-L-glutamate kinase.";
RL Eur. J. Biochem. 253:280-291(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3;
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; AJ312276; CAC41342.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO79980.1; -; Genomic_DNA.
DR RefSeq; NP_813908.1; NC_004668.1.
DR RefSeq; WP_002356130.1; NZ_KE136524.1.
DR AlphaFoldDB; Q839Q5; -.
DR SMR; Q839Q5; -.
DR STRING; 226185.EF_0105; -.
DR EnsemblBacteria; AAO79980; AAO79980; EF_0105.
DR KEGG; efa:EF0105; -.
DR PATRIC; fig|226185.45.peg.155; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_9; -.
DR OMA; DGNNVCN; -.
DR SABIO-RK; Q839Q5; -.
DR UniPathway; UPA00254; UER00365.
DR Proteomes; UP000001415; 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:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_01109; OTCase; 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; IPR024904; OTCase_ArgI.
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 PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..339
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000112924"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 167
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 231
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 235..236
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 274..275
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 319
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT CONFLICT 17
FT /note="S -> T (in Ref. 1; CAC41342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 38029 MW; 2238D2AA1D4A075C CRC64;
MNSVFQGRSL LAEKDFSRAE LEYLVDFSIH LKELKKKGIP HHYLEGKNIA LLFEKTSTRT
RSAFTTAAID LGAHPEYLGA NDIQLGKKES VEDTAIVLGS MFDGIEFRGF SQEVVEDLAK
YSGVPVWNGL TDQWHPTQMI ADFMTVKENF GRLEGITLVY VGDGRNNMAN SLLVTGAILG
VNVRICAPKE LFPSDEVVNY AKEFAKESGA ELMITDDVAK GVKGANVLYT DVWVSMGEED
KFEERVNLLK PYQINMAMLE KTENMDGDLI VLHCLPAFHD TKTQYGEMVA EKFGITEMEI
TDEVFRSKYG RQFEEAENRM HSIKAIMAAT LGNLFIPRV
