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Database: UniProt/TrEMBL
Entry: Q5PJB6_SALPA
LinkDB: Q5PJB6_SALPA
Original site: Q5PJB6_SALPA 
ID   Q5PJB6_SALPA            Unreviewed;       334 AA.
AC   Q5PJB6;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   11-JUN-2014, entry version 69.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=argI; OrderedLocusNames=SPA4269;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P.,
RA   Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M.,
RA   Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G.,
RA   Kohlberg S., Strong C., Du F., Carter J., Kremizki C., Layman D.,
RA   Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P.,
RA   Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L.,
RA   Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV80003.1; -; Genomic_DNA.
DR   RefSeq; YP_153315.1; NC_006511.1.
DR   ProteinModelPortal; Q5PJB6; -.
DR   SMR; Q5PJB6; 2-334.
DR   STRING; 295319.SPA4269; -.
DR   PRIDE; Q5PJB6; -.
DR   EnsemblBacteria; AAV80003; AAV80003; SPA4269.
DR   PATRIC; 32358362; VBISalEnt134188_4527.
DR   HOGENOM; HOG000022686; -.
DR   OMA; YQRHFLR; -.
DR   OrthoDB; EOG690MGV; -.
DR   BioCyc; SENT295319:GJBZ-4263-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   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){EA4}.
FT   BINDING     134    134       Carbamoyl phosphate (By similarity){EA4}.
FT   SITE         31     31       Important for structural integrity (By
FT                                similarity).
FT   SITE        147    147       Important for structural integrity (By
FT                                similarity).
SQ   SEQUENCE   334 AA;  36741 MW;  EF37A456A08BE0B4 CRC64;
     MSTFYQKPFL KLLDFTASEL TALLQLAAKL KADKKNGKEE QKLVGKNIAL IFEKDSTRTR
     CSFEVAAYDQ GARVTYLGSS GSQIGHKESI KDTARVLGRM FDGIQYRGYG QEIVETLAEY
     SGVPVWNGLT DEYHPTQLLA DLLTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT
     GLDLRLVAPK ACWPQAALVA ECSAMAKKNG GAITLTEDIA SGVKGADFIY TDVWVSMGEP
     KEKWAERIAL LRDYQVNSQM MALTGNPQVK FLHCLPAFHD DETTLGKKMA EEYGLHGGME
     VTDEVFESAA SIVFDEAENR MHTIKAVMVA TLSK
//
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