(data stored in SCRATCH zone)

SWISSPROT: C6AZH1_RHILS

ID   C6AZH1_RHILS            Unreviewed;       304 AA.
AC   C6AZH1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 71.
DE   RecName: Full=Ornithine carbamoyltransferase, catabolic {ECO:0000256|HAMAP-Rule:MF_01109};
DE            Short=OTCase {ECO:0000256|HAMAP-Rule:MF_01109};
DE            EC=2.1.3.3 {ECO:0000256|HAMAP-Rule:MF_01109};
GN   Name=arcB {ECO:0000256|HAMAP-Rule:MF_01109};
GN   OrderedLocusNames=Rleg_0186 {ECO:0000313|EMBL:ACS54497.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54497.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54497.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54497.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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:0000256|SAAS:SAAS00009102}.
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
CC       + L-citrulline. {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00106053}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01109}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00106153}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|RuleBase:RU003634,
CC       ECO:0000256|SAAS:SAAS00578869}.
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DR   EMBL; CP001622; ACS54497.1; -; Genomic_DNA.
DR   RefSeq; WP_012755913.1; NC_012850.1.
DR   ProteinModelPortal; C6AZH1; -.
DR   EnsemblBacteria; ACS54497; ACS54497; Rleg_0186.
DR   KEGG; rlg:Rleg_0186; -.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OMA; HPMFLGK; -.
DR   OrthoDB; POG091H0543; -.
DR   UniPathway; UPA00254; UER00365.
DR   Proteomes; UP000002256; 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-HAMAP.
DR   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019546; P:arginine deiminase pathway; 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; 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; C6AZH1.
DR   SWISS-2DPAGE; C6AZH1.
KW   Arginine metabolism {ECO:0000256|HAMAP-Rule:MF_01109};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|SAAS:SAAS00009103};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|RuleBase:RU003634, ECO:0000256|SAAS:SAAS00106165,
KW   ECO:0000313|EMBL:ACS54497.1}.
FT   DOMAIN        4    144       OTCace_N. {ECO:0000259|Pfam:PF02729}.
FT   DOMAIN      150    299       OTCace. {ECO:0000259|Pfam:PF00185}.
FT   REGION       53     56       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      131    134       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      226    227       Ornithine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   REGION      261    262       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   BINDING      80     80       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     104    104       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     162    162       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     222    222       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     289    289       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
SQ   SEQUENCE   304 AA;  33423 MW;  E4566B4554F5656C CRC64;
     MSPKHFLDLS AVTSADLRTI MNDALARKQA FKAGQGDKPL AGKMLAMIFE KPSTRTRVSF
     DVGMRQLGGE TLFLSGTEMQ LGRAETIGDT AKVLSRYVDA IMIRTTEHSR LVELAQHATV
     PVINALTDDT HPCQIMADIM TFEEHRGPIK GKTIAWTGDG NNVLHSLVEG AARFGYRMNM
     AVPLGSEPKD HYLNWARNEG AEIMLCHDAD RAVAGVDCVV TDTWVSMNQE HRARGHNVFQ
     PYQVNAALMA KAGNDALFMH CLPAHRGEEV TDEVIDGPQS VVFDEAENRL HAQKSILAWC
     LGAI
//

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