ID B7LMS5_ESCF3 Unreviewed; 340 AA.
AC B7LMS5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Ornithine carbamoyltransferase;
DE Short=OTCase;
DE EC=2.1.3.3;
GN Name=argI; OrderedLocusNames=EFER_4334;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ91753.1; -; Genomic_DNA.
DR RefSeq; YP_002385342.1; NC_011740.1.
DR ProteinModelPortal; B7LMS5; -.
DR STRING; 585054.EFER_4334; -.
DR EnsemblBacteria; CAQ91753; CAQ91753; EFER_4334.
DR GeneID; 7122021; -.
DR KEGG; efe:EFER_4334; -.
DR PATRIC; 32132982; VBIEscFer122920_4172.
DR eggNOG; COG0078; -.
DR HOGENOM; HOG000022686; -.
DR KO; K00611; -.
DR BioCyc; EFER585054:GJJM-4326-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 62 66 Carbamoyl phosphate binding (By
FT similarity).
FT REGION 279 282 Ornithine binding (By similarity).
FT BINDING 113 113 Carbamoyl phosphate (By similarity).
FT BINDING 140 140 Carbamoyl phosphate (By similarity).
FT SITE 37 37 Important for structural integrity (By
FT similarity).
FT SITE 153 153 Important for structural integrity (By
FT similarity).
SQ SEQUENCE 340 AA; 37391 MW; 15A3DAB5217B5114 CRC64;
MPWEGSMSSF YQKHFLKLLD FTSSELTTLL QLAATLKSAK KNGTEEAKLT GKNIALIFEK
DSTRTRCSFE VAAYDQGARV TYLGSSGSQI GHKESIKDTA RVLGRMYDGI QYRGYGQEIV
ETLAEYAGVP VWNGLTDEFH PTQLLADLLT MQEHLPGKAF NEMTLVYAGD ARNNMGNSML
EAAALTGLDL RLVAPKACWP EASLVAECSA LAQKHGGKIT LTEDIASGVK GADFIYTDVW
VSMGEPKEKW AERIALLRDY QVNSKMMALT GNSQVKFLHC LPAFHDDQTT LGKKMAAEFG
LYGGMEVTDE VFESPASIVF DQAENRMHTI KAIMVATLAK
//
