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Database: UniProt
Entry: Q46XK9
LinkDB: Q46XK9
Original site: Q46XK9 
ID   OTC_CUPPJ               Reviewed;         307 AA.
AC   Q46XK9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-SEP-2014, entry version 65.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argF; OrderedLocusNames=Reut_A2763;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia
OS   eutropha (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group
CC       from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine
CC       (ORN) to produce L-citrulline (By similarity).
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
CC       + L-citrulline.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
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DR   EMBL; CP000090; AAZ62124.1; -; Genomic_DNA.
DR   RefSeq; WP_011298909.1; NC_007347.1.
DR   RefSeq; YP_296968.1; NC_007347.1.
DR   ProteinModelPortal; Q46XK9; -.
DR   STRING; 264198.Reut_A2763; -.
DR   EnsemblBacteria; AAZ62124; AAZ62124; Reut_A2763.
DR   GeneID; 3612333; -.
DR   KEGG; reu:Reut_A2763; -.
DR   PATRIC; 20231204; VBIRalEut24049_3435.
DR   eggNOG; COG0078; -.
DR   HOGENOM; HOG000022686; -.
DR   OMA; KWAEQNA; -.
DR   OrthoDB; EOG690MGV; -.
DR   BioCyc; CPIN264198:GIW3-2810-MONOMER; -.
DR   UniPathway; UPA00068; UER00112.
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-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
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; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024904; Orn_carbamltrans.
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   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Transferase.
FT   CHAIN         1    307       Ornithine carbamoyltransferase.
FT                                /FTId=PRO_1000065113.
FT   REGION       56     60       Carbamoyl phosphate binding (By
FT                                similarity).
FT   REGION      134    137       Carbamoyl phosphate binding (By
FT                                similarity).
FT   REGION      227    228       Ornithine binding (By similarity).
FT   REGION      262    265       Carbamoyl phosphate binding (By
FT                                similarity).
FT   BINDING      10     10       Carbamoyl phosphate (By similarity).
FT   BINDING      83     83       Carbamoyl phosphate (By similarity).
FT   BINDING     107    107       Carbamoyl phosphate (By similarity).
FT   BINDING     165    165       Ornithine (By similarity).
FT   BINDING     223    223       Ornithine (By similarity).
FT   BINDING     291    291       Carbamoyl phosphate (By similarity).
FT   SITE         31     31       Important for structural integrity (By
FT                                similarity).
FT   SITE        147    147       Important for structural integrity (By
FT                                similarity).
SQ   SEQUENCE   307 AA;  34728 MW;  2ACD07F864BCB828 CRC64;
     MSSTPIKHYL QFSDLTPDEY EYLLDRARIL KAKFKNYETW HPLHDRTLAM IFEKNSTRTR
     LSFEAGIHQL GGHAVFLNTR DSQLGRGEPI EDAAQVISRM VDIIMIRTFG QDIIERFAAH
     SRVPVINGLT NEYHPCQVLA DVFTYIEQRG SIRGKTVAWI GDANNMAYTW IQAAERLGFT
     FHFSAPPGYQ LDPALVPASA AGQLKVFEDP LAACKGASLV TTDVWTSMGF EAENEARKRA
     FQNWMVTTAM MDRAEPDALF MHCLPAHRGE EVEAAVIDGP KSVVWDEAEN RLHVQKALME
     YLLCGRY
//
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