OTC_CHICK
ID OTC_CHICK Reviewed; 354 AA.
AC Q9YHY9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ornithine transcarbamylase, mitochondrial {ECO:0000305|PubMed:7332529};
DE Short=OTCase {ECO:0000303|PubMed:9792920};
DE EC=2.1.3.3 {ECO:0000269|PubMed:7332529};
DE AltName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE Flags: Precursor;
GN Name=OTC {ECO:0000250|UniProtKB:P00480};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=White leghorn {ECO:0000269|PubMed:9792920};
RC TISSUE=Kidney {ECO:0000269|PubMed:9792920};
RX PubMed=9792920; DOI=10.1093/oxfordjournals.jbchem.a022214;
RA Shimogiri T., Kono M., Mannen H., Mizutani M., Tsuji S.;
RT "Chicken ornithine transcarbamylase gene, structure, regulation, and
RT chromosomal assignment: repetitive sequence motif in intron 3 regulates
RT this enzyme activity.";
RL J. Biochem. 124:962-971(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=7332529; DOI=10.1007/bf00504253;
RA Tsuji S., Fukushima T.;
RT "Comparison of renal ornithine transcarbamylase activities within different
RT chicken breeds.";
RL Biochem. Genet. 19:881-893(1981).
RN [3] {ECO:0000305}
RP ENZYME KINETICS.
RX PubMed=6419722; DOI=10.1007/bf00483945;
RA Tsuji S., Nakagawa K., Fukushima T.;
RT "Genetically controlled quantitative variation of ornithine
RT transcarbamylase in the chick kidney.";
RL Biochem. Genet. 21:857-869(1983).
RN [4] {ECO:0000305}
RP GENETIC REGULATION.
RX PubMed=6661175; DOI=10.1007/bf00483944;
RA Tsuji S., Nakagawa K., Fukushima T.;
RT "Genetic control of ornithine transcarbamylase induction in chick kidney.";
RL Biochem. Genet. 21:843-855(1983).
RN [5] {ECO:0000305}
RP ENZYME KINETICS, AND SUBUNIT.
RX PubMed=6418730; DOI=10.1093/oxfordjournals.jbchem.a134476;
RA Tsuji S.;
RT "Chicken ornithine transcarbamylase: purification and some properties.";
RL J. Biochem. 94:1307-1315(1983).
RN [6] {ECO:0000305}
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=6682551; DOI=10.3382/ps.0620519;
RA Tsuji S., Nakagawa K., Nomura Y., Mukai F., Fukushima T.;
RT "Induction of ornithine transcarbamylase activity with egg yolk in chick
RT kidney.";
RL Poult. Sci. 62:519-524(1983).
RN [7] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=3606562; DOI=10.1007/bf00499319;
RA Tsuji S., Kanazawa S.;
RT "Chicken ornithine transcarbamylase: its unexpected expression.";
RL Biochem. Genet. 25:259-266(1987).
CC -!- FUNCTION: Catalyzes the second step of the urea cycle, the condensation
CC of carbamoyl phosphate with L-ornithine to form L-citrulline
CC (PubMed:7332529). The urea cycle ensures the detoxification of ammonia
CC by converting it to urea for excretion (Probable).
CC {ECO:0000269|PubMed:7332529, ECO:0000305}.
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:0000269|PubMed:7332529};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19515;
CC Evidence={ECO:0000305|PubMed:7332529};
CC -!- ACTIVITY REGULATION: Inhibition by ornithine increases at higher pH.
CC {ECO:0000269|PubMed:6418730}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for carbamoyl phosphate (at pH 7.5);
CC KM=1.21 mM for ornithine (at pH 7.5);
CC Note=With an increase in pH, a decrease in KM values for ornithine
CC and an increase in the extent of inhibition by ornithine are
CC observed.;
CC pH dependence:
CC Optimum pH is 7.5 in the presence of 5 mM ornithine. The curve shifts
CC toward a more alkaline region with a decrease in ornithine
CC concentration.;
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine
CC and carbamoyl phosphate: step 1/1. {ECO:0000305|PubMed:7332529}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:6418730}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, brain, heart, liver, pancreas,
CC gizzard, small intestine and breast muscle. More abundant in
CC mitochondrion-rich organs (heart, liver and brain) than in other
CC organs. Activity is only detected in the kidney.
CC {ECO:0000269|PubMed:3606562}.
CC -!- DEVELOPMENTAL STAGE: Activity detectable in embryos by day 14.
CC Increases until 7 days post-hatching, then decreases again.
CC {ECO:0000269|PubMed:6682551}.
CC -!- INDUCTION: By diet of egg yolk in animals which have a high level of
CC OTC activity due to presence of OCB gene. {ECO:0000269|PubMed:6682551}.
CC -!- PTM: Cleavage of the precursor form to the active form occurs only in
CC the kidney. {ECO:0000269|PubMed:3606562}.
CC -!- MISCELLANEOUS: Ornithine transcarbamylase activity varies within and
CC between different breeds of chicken.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; AF065629; AAD12234.1; -; mRNA.
DR EMBL; AF065638; AAD33083.1; -; Genomic_DNA.
DR EMBL; AF065630; AAD33083.1; JOINED; Genomic_DNA.
DR EMBL; AF065631; AAD33083.1; JOINED; Genomic_DNA.
DR EMBL; AF065632; AAD33083.1; JOINED; Genomic_DNA.
DR EMBL; AF065634; AAD33083.1; JOINED; Genomic_DNA.
DR EMBL; AF065635; AAD33083.1; JOINED; Genomic_DNA.
DR EMBL; AF065636; AAD33083.1; JOINED; Genomic_DNA.
DR EMBL; AF065637; AAD33083.1; JOINED; Genomic_DNA.
DR PIR; JE0309; JE0309.
DR RefSeq; NP_990241.1; NM_204910.1.
DR AlphaFoldDB; Q9YHY9; -.
DR SMR; Q9YHY9; -.
DR STRING; 9031.ENSGALP00000026160; -.
DR PaxDb; Q9YHY9; -.
DR PRIDE; Q9YHY9; -.
DR GeneID; 395735; -.
DR KEGG; gga:395735; -.
DR CTD; 5009; -.
DR VEuPathDB; HostDB:geneid_395735; -.
DR eggNOG; KOG1504; Eukaryota.
DR InParanoid; Q9YHY9; -.
DR OrthoDB; 1404554at2759; -.
DR PhylomeDB; Q9YHY9; -.
DR Reactome; R-GGA-187630; Arginine metabolism.
DR SABIO-RK; Q9YHY9; -.
DR UniPathway; UPA00158; UER00271.
DR PRO; PR:Q9YHY9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1370; -; 2.
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 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide; Urea cycle.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT CHAIN 33..354
FT /note="Ornithine transcarbamylase, mitochondrial"
FT /id="PRO_0000020337"
FT ACT_SITE 303
FT /evidence="ECO:0000250"
FT BINDING 90..94
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 263..267
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 302..305
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 40245 MW; 20447180BAD9D4ED CRC64;
MLFNLKNLYR ITKLTQNSKH LPRHFCRGPP NQMNVCLKGR DLLTLQNYTA DELKYLLWVA
SDLKQRIKDK GEYLPLMQGK SLAMIFEKRS TRTRLSAETG FALLGGHSSF LTKQDIHLGT
NESLTDTARV LSSMTNAILA RVYKHNDLDL MTKEATIPVI NGLSDLYHPL QILADYLTLQ
EHYGGLNGLT IAWIGDGNNV LHSIMTSAAK LGMHLRIATP KGFEPDLRIT KVTEQYSKEY
GTRLLLTTDP LEAANGANVL VTDTWISMGQ EEEKRRRLKA FQGYQITMQT VQSAASNWTF
LHCLPRKPEE VDDEVFYSPR SLVFQEAENR KWTIMAVMVS LLTDYSPQLQ MPTF
