OTC_THET2
ID OTC_THET2 Reviewed; 301 AA.
AC P96134;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000303|PubMed:9346304};
DE Short=OTC {ECO:0000303|PubMed:9346304};
DE Short=OTCase {ECO:0000303|PubMed:9346304};
DE EC=2.1.3.3 {ECO:0000305|PubMed:9346304};
GN Name=argF {ECO:0000303|PubMed:9346304}; OrderedLocusNames=TT_C0838;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN OTCASE, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=9346304; DOI=10.1111/j.1432-1033.1997.00466.x;
RA Sanchez R., Baetens M., van de Casteele M., Roovers M., Legrain C.,
RA Glansdorff N.;
RT "Ornithine carbamoyltransferase from the extreme thermophile Thermus
RT thermophilus -- analysis of the gene and characterisation of the protein.";
RL Eur. J. Biochem. 248:466-474(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sanchez R., Roovers M., Glansdorff N.;
RT "Organisation of arginine biosynthetic genes in Thermus thermophilus.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline, which is a substrate for argininosuccinate
CC synthetase, the enzyme involved in the final step in arginine
CC biosynthesis. {ECO:0000269|PubMed:9346304}.
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:0000305|PubMed:9346304};
CC -!- ACTIVITY REGULATION: Inhibited by delta-N-phosphonoacetyl-L-ornithine.
CC {ECO:0000269|PubMed:9346304}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.10 mM for carbamoyl phosphate (at pH 7)
CC {ECO:0000269|PubMed:9346304};
CC KM=0.10 mM for L-ornithine (at pH 7) {ECO:0000269|PubMed:9346304};
CC pH dependence:
CC Optimum pH is dependent on ornithine concentration with an optimum at
CC pH 8 for ornithine concentrations around KM values. Higher
CC concentrations shift the optimum towards lower pH. At pH 7.0, the
CC maximum velocity remains constant even when the ornithine
CC concentration is very high (> 10 mM). At more alkaline pH, however,
CC substrate inhibition is observed above 0.25 mM ornithine.
CC {ECO:0000269|PubMed:9346304};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Highly thermostable.
CC {ECO:0000269|PubMed:9346304};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:9346304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved threonine residue in position 57, which is
CC part of the carbamoylphosphate binding site; it is replaced by a
CC leucine residue (PMIS:9346304). {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y10266; CAA71315.1; -; Genomic_DNA.
DR EMBL; Y18353; CAA77140.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81184.1; -; Genomic_DNA.
DR RefSeq; WP_011173269.1; NC_005835.1.
DR AlphaFoldDB; P96134; -.
DR SMR; P96134; -.
DR STRING; 262724.TT_C0838; -.
DR EnsemblBacteria; AAS81184; AAS81184; TT_C0838.
DR KEGG; tth:TT_C0838; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_2_0; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 988597at2; -.
DR SABIO-RK; P96134; -.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000000592; 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 GO; GO:0006526; P:arginine biosynthetic process; 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.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Transferase.
FT CHAIN 1..301
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000113050"
FT BINDING 107
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 134..137
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 165
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 220
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 224..225
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 260..261
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 288
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ SEQUENCE 301 AA; 33205 MW; 0433F585C7E9DD23 CRC64;
MGGEALTLPK DLLDFSGYGP KELQALLDLA ERLKRERYRG EDLKGKVLAL LFEKPSLRTR
TTLEVAMVHL GGHAVYLDQK QVGIGEREPV RDVAKNLERF VEGIAARVFR HETVEALARH
AKVPVVNALS DRAHPLQALA DLLTLKEVFG GLAGLEVAWV GDGNNVLNSL LEVAPLAGLK
VRVATPKGYE PDPGLLKRAN AFFTHDPKEA ALGAHALYTD VWTSMGQEAE RAKRLRDFQG
FQVNGELLKL LRPEGVFLHC LPAHYGEETT EEAVHGPRSR VFDQAENRLH TAKAVLLTLL
K
