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Database: UniProt
Entry: Q2G3J8
LinkDB: Q2G3J8
Original site: Q2G3J8 
ID   OTC_NOVAD               Reviewed;         311 AA.
AC   Q2G3J8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   14-MAY-2014, entry version 62.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argF; OrderedLocusNames=Saro_3140;
OS   Novosphingobium aromaticivorans (strain DSM 12444 / F199).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12444 / F199;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-2006) 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; CP000248; ABD27575.1; -; Genomic_DNA.
DR   RefSeq; YP_498409.1; NC_007794.1.
DR   ProteinModelPortal; Q2G3J8; -.
DR   SMR; Q2G3J8; 1-311.
DR   STRING; 279238.Saro_3140; -.
DR   EnsemblBacteria; ABD27575; ABD27575; Saro_3140.
DR   GeneID; 3918182; -.
DR   KEGG; nar:Saro_3140; -.
DR   PATRIC; 22789136; VBINovAro50627_3220.
DR   eggNOG; COG0078; -.
DR   HOGENOM; HOG000022686; -.
DR   OMA; KWAEQNA; -.
DR   OrthoDB; EOG690MGV; -.
DR   BioCyc; NARO279238:GHBU-3212-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    311       Ornithine carbamoyltransferase.
FT                                /FTId=PRO_1000213570.
FT   REGION       60     64       Carbamoyl phosphate binding (By
FT                                similarity).
FT   REGION      138    141       Carbamoyl phosphate binding (By
FT                                similarity).
FT   REGION      233    234       Ornithine binding (By similarity).
FT   REGION      267    270       Carbamoyl phosphate binding (By
FT                                similarity).
FT   BINDING       9      9       Carbamoyl phosphate (By similarity).
FT   BINDING      87     87       Carbamoyl phosphate (By similarity).
FT   BINDING     111    111       Carbamoyl phosphate (By similarity).
FT   BINDING     169    169       Ornithine (By similarity).
FT   BINDING     229    229       Ornithine (By similarity).
FT   BINDING     278    278       Carbamoyl phosphate (By similarity).
FT   BINDING     296    296       Carbamoyl phosphate (By similarity).
FT   SITE         30     30       Important for structural integrity (By
FT                                similarity).
FT   SITE        151    151       Important for structural integrity (By
FT                                similarity).
SQ   SEQUENCE   311 AA;  33086 MW;  E49EA03D88BF112A CRC64;
     MSQALKHFLN LTDAGGDAIA AMLNDALDRK SARAGQPKGK ADADAPLGGR VLAMVFEKNS
     TRTRVSFDIA MRQLGGSALI LDAGTTQLGR GETIADTARV LSRMADAIML RTDDHAKVEE
     LARHATVPVI NGLTDLSHPC QIMADLLTVI EHGKALPGLE VAWLGDGNNV LNSIVEAAGL
     MKFNVRIGVP EGYESDAGMI EAAVLAGAGI RVIRDPVEAV RGADVVVTDT WISMGQAHAE
     AKLAAMAPYQ VNDALMAHAK PDAVFLHCLP AHRGEEVTDA VIDGPRSVVW DEAENRIHAQ
     KSVLRWVFGQ I
//
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