(data stored in ACNUC7421 zone)

SWISSPROT: OTC_RHOOB

ID   OTC_RHOOB               Reviewed;         315 AA.
AC   C1ASZ8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Ornithine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01109};
DE            Short=OTCase {ECO:0000255|HAMAP-Rule:MF_01109};
DE            EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN   Name=arcB {ECO:0000255|HAMAP-Rule:MF_01109};
GN   OrderedLocusNames=ROP_06830;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
CC       + L-citrulline. {ECO:0000255|HAMAP-Rule:MF_01109}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01109}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01109}.
DR   EMBL; AP011115; BAH48930.1; -; Genomic_DNA.
DR   RefSeq; WP_012687932.1; NC_012522.1.
DR   ProteinModelPortal; C1ASZ8; -.
DR   SMR; C1ASZ8; -.
DR   STRING; 632772.ROP_06830; -.
DR   EnsemblBacteria; BAH48930; BAH48930; ROP_06830.
DR   KEGG; rop:ROP_06830; -.
DR   PATRIC; fig|632772.20.peg.744; -.
DR   eggNOG; ENOG4105DBV; Bacteria.
DR   eggNOG; COG0078; LUCA.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OMA; HPMFLGK; -.
DR   OrthoDB; POG091H0543; -.
DR   UniPathway; UPA00254; UER00365.
DR   Proteomes; UP000002212; Chromosome.
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-EC.
DR   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
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; OTCase_ArgI.
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;
DR   PRODOM; C1ASZ8.
DR   SWISS-2DPAGE; C1ASZ8.
KW   Arginine metabolism; Complete proteome; Cytoplasm; Transferase.
FT   CHAIN         1    315       Ornithine carbamoyltransferase.
FT                                /FTId=PRO_1000163976.
FT   REGION       53     56       Carbamoyl phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01109}.
FT   REGION      131    134       Carbamoyl phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01109}.
FT   REGION      231    232       Ornithine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01109}.
FT   REGION      267    268       Carbamoyl phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01109}.
FT   BINDING      80     80       Carbamoyl phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     104    104       Carbamoyl phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     163    163       Ornithine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     227    227       Ornithine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     295    295       Carbamoyl phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01109}.
SQ   SEQUENCE   315 AA;  33990 MW;  46957D7BA8387180 CRC64;
     MTTVVKHFLR DDDLTPEQQA EVLELAARLK KAPFAERPLE GPRGVGVIFE KNSTRTRFSF
     EMGIAQLGGH AIVVDGRSTQ LGREETLQDT GRVLSRYVDA VVWRTFGQKR LEAMASGADV
     PIVNALSDEF HPCQVLADLQ TLAERKGSLK GLKLTYLGDG ANNMAHSLML GGVTAGVDVT
     IASPEGFAPL PWVVEAARAR AADTGATITL TEDPQAAVVG ADALVTDTWT SMGQENDGLD
     RVGPFRPFQI NEALLAKAAA DAVVLHCLPA HRGEEITDEV LDGPQSVVWD EAENRLHAQK
     ALLVWLLAQR TGNRP
//

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