ID Q5PJB6_SALPA Unreviewed; 334 AA.
AC Q5PJB6;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 01-MAY-2013, entry version 63.
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 GeneID; 3178178; -.
DR KEGG; spt:SPA4269; -.
DR PATRIC; 32358362; VBISalEnt134188_4527.
DR HOGENOM; HOG000022686; -.
DR KO; K00611; -.
DR OMA; RLMDFTP; -.
DR ProtClustDB; PRK03515; -.
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:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
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; Asp/Orn_carbamoyltranf; 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).
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 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
//
