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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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