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 01-MAY-2013, entry version 72.
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; KHLLSIK; -.
DR ProtClustDB; PRK00779; -.
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 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
//
