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Database: UniProt/TrEMBL
Entry: C6DJL9_PECCP
LinkDB: C6DJL9_PECCP
Original site: C6DJL9_PECCP 
ID   C6DJL9_PECCP            Unreviewed;       335 AA.
AC   C6DJL9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   19-FEB-2014, entry version 41.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
DE   AltName: Full=Ornithine carbamoyltransferase, catabolic;
GN   Name=arcB; OrderedLocusNames=PC1_0374;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum
RT   PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
CC       + L-citrulline.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
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DR   EMBL; CP001657; ACT11432.1; -; Genomic_DNA.
DR   RefSeq; YP_003015968.1; NC_012917.1.
DR   ProteinModelPortal; C6DJL9; -.
DR   STRING; 561230.PC1_0374; -.
DR   EnsemblBacteria; ACT11432; ACT11432; PC1_0374.
DR   GeneID; 8131288; -.
DR   KEGG; pct:PC1_0374; -.
DR   PATRIC; 20485324; VBIPecCar70489_0376.
DR   eggNOG; COG0078; -.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OMA; AFTVACT; -.
DR   OrthoDB; EOG690MGV; -.
DR   ProtClustDB; PRK03515; -.
DR   BioCyc; PCAR561230:GKCK-388-MONOMER; -.
DR   UniPathway; UPA00254; UER00365.
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:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019546; P:arginine deiminase pathway; 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   Arginine metabolism; Complete proteome; Cytoplasm; Transferase.
FT   REGION       56     60       Carbamoyl phosphate binding (By
FT                                similarity).
FT   REGION      273    276       Ornithine binding (By similarity).
FT   BINDING     107    107       Carbamoyl phosphate (By similarity).
FT   BINDING     134    134       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   335 AA;  36818 MW;  091B75977C7CFB8C CRC64;
     MQPFYKRHFL RLMDFTPAEI ANLLALSTKL KADKKNGTEV RRLQGKNIAL IFEKDSTRTR
     CSFEVAAYDQ GAQVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGYG QQIVETLAQY
     AGVPVWNGLT NEFHPTQLLA DLLTMQEHLP GKPLSEMALV YVGDARNNMG NTMLEAAALT
     GLDLRLVAPK ACWPDAGLVA ECQAAAEQTG GSITLTEDIA TGVAGADFIY TDVWVSMGEP
     KETWQERIAL LKPYQVNAAM IAATGNPQVK FLHCLPAFHD DQTTMGQQMA EQYGLHGGME
     VTDEVFESAH SIVFDQAENR MHTIKAVMVA TLAQD
//
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