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Database: UniProt
Entry: Q740I5
LinkDB: Q740I5
Original site: Q740I5 
ID   OTC_MYCPA               Reviewed;         309 AA.
AC   Q740I5;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   19-FEB-2014, entry version 76.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argF; OrderedLocusNames=MAP_1365;
OS   Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D.,
RA   Banerji N., Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03682.1; -; Genomic_DNA.
DR   RefSeq; NP_960299.1; NC_002944.2.
DR   ProteinModelPortal; Q740I5; -.
DR   SMR; Q740I5; 4-307.
DR   STRING; 262316.MAP1365; -.
DR   EnsemblBacteria; AAS03682; AAS03682; MAP_1365.
DR   GeneID; 2720213; -.
DR   KEGG; mpa:MAP1365; -.
DR   PATRIC; 17995219; VBIMycAvi108102_1439.
DR   eggNOG; COG0078; -.
DR   KO; K00611; -.
DR   OMA; GNNVCNS; -.
DR   OrthoDB; EOG690MGV; -.
DR   ProtClustDB; PRK00779; -.
DR   BioCyc; MAVI262316:GCQR-1386-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    309       Ornithine carbamoyltransferase.
FT                                /FTId=PRO_0000112952.
FT   REGION       51     55       Carbamoyl phosphate binding (By
FT                                similarity).
FT   REGION      129    132       Carbamoyl phosphate binding (By
FT                                similarity).
FT   REGION      229    230       Ornithine binding (By similarity).
FT   REGION      264    267       Carbamoyl phosphate binding (By
FT                                similarity).
FT   BINDING       7      7       Carbamoyl phosphate (By similarity).
FT   BINDING      78     78       Carbamoyl phosphate (By similarity).
FT   BINDING     102    102       Carbamoyl phosphate (By similarity).
FT   BINDING     161    161       Ornithine (By similarity).
FT   BINDING     225    225       Ornithine (By similarity).
FT   BINDING     275    275       Carbamoyl phosphate (By similarity).
FT   BINDING     293    293       Carbamoyl phosphate (By similarity).
FT   SITE         28     28       Important for structural integrity (By
FT                                similarity).
FT   SITE        142    142       Important for structural integrity (By
FT                                similarity).
SQ   SEQUENCE   309 AA;  33595 MW;  7500E6BE03398101 CRC64;
     MTPRHFLRDD DLSPAEQAEV LALAAELKKD PFSARPLEGP RGVAVLFDKN STRTRFSFEV
     GIAQLGGHAV VVDARSTQLG RDETLEDTAR VLSRYVEAIV WRTFEQQRLE AMAGAATVPV
     INALSDEFHP CQMLADLQAI AEHKGSLSGL RMCYLGDGAN NMAHSLMLGG VTAGIHVTIA
     APDGFTPAPE FVAAARRRAE STGATVTLTT DARAAARGVD VLVTDTWTSM GQEDDGLDRR
     TPFWPYQLNA DLVSLADPEA IVLHCLPAHR GEEITDEVMD GPSSVVWDEA ENRLHAQKAL
     LTWLLERQS
//
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