(data stored in ACNUC7421 zone)

SWISSPROT: E6S865_INTC7

ID   E6S865_INTC7            Unreviewed;       335 AA.
AC   E6S865;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   RecName: Full=Ornithine carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS00393033};
DE            Short=OTCase {ECO:0000256|HAMAP-Rule:MF_01109};
DE            EC=2.1.3.3 {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS00393033};
GN   OrderedLocusNames=Intca_0421 {ECO:0000313|EMBL:ADU46969.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46969.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46969.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(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:
CC       Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC         phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00341539}.
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; CP002343; ADU46969.1; -; Genomic_DNA.
DR   RefSeq; WP_013491290.1; NC_014830.1.
DR   STRING; 710696.Intca_0421; -.
DR   EnsemblBacteria; ADU46969; ADU46969; Intca_0421.
DR   KEGG; ica:Intca_0421; -.
DR   eggNOG; ENOG4105DBV; Bacteria.
DR   eggNOG; COG0078; LUCA.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OrthoDB; 988597at2; -.
DR   BioCyc; ICAL710696:GH9U-431-MONOMER; -.
DR   Proteomes; UP000008914; 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-UniRule.
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; IPR036901; Asp/Orn_carbamoylTrfase_sf.
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; E6S865.
DR   SWISS-2DPAGE; E6S865.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|SAAS:SAAS00420337};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|RuleBase:RU003634, ECO:0000256|SAAS:SAAS00470455,
KW   ECO:0000313|EMBL:ADU46969.1}.
FT   DOMAIN        9    149       OTCace_N. {ECO:0000259|Pfam:PF02729}.
FT   DOMAIN      157    330       OTCace. {ECO:0000259|Pfam:PF00185}.
FT   REGION       58     61       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      136    139       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      237    238       Ornithine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   REGION      275    276       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   COILED       25     45       {ECO:0000256|SAM:Coils}.
FT   BINDING      85     85       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     109    109       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     169    169       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     233    233       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     320    320       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
SQ   SEQUENCE   335 AA;  36928 MW;  62F53CF1DDBCA64B CRC64;
     MTVASLFGRN VLKESDLTPD EFRALLDLAA DLKAAKRERR EQRRLAGLNI ALLFEKTSTR
     TRCAFEVAAA DQGASTTYLD PAGSQMGHKE SIKDTARVLG RYYDGIEYRG AGHDVVETLG
     AWAGVPVWNG LTDDWHPTQS LCDALTMREH AAKPDSEIAF AYVGDARFNM GNSLLVMGAM
     LGMDVRIAAP RSLWPSEAVV AQAKSYAAES GSRVTLTEDV AEGIAGVDFV HTDVWVSMGE
     AKDVWAERIR LLTPYQVNAE LLQLTGNRDV RFMHCLPAFH DLETKVGRDV HAEFGRKELE
     VTDDVFESEA SIVFDQAENR MHTIKALLVA TLARP
//

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