OTC_LITCT
ID OTC_LITCT Reviewed; 350 AA.
AC P31326;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE EC=2.1.3.3;
DE AltName: Full=Ornithine transcarbamylase;
DE Short=OTCase;
DE Flags: Precursor;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1291156; DOI=10.1002/dvg.1020130406;
RA Helbing C., Gergely G., Atkinson B.G.;
RT "Sequential up-regulation of thyroid hormone beta receptor, ornithine
RT transcarbamylase, and carbamyl phosphate synthetase mRNAs in the liver of
RT Rana catesbeiana tadpoles during spontaneous and thyroid hormone-induced
RT metamorphosis.";
RL Dev. Genet. 13:289-301(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Iwase K., Yamauchi K., Ishikawa K.;
RT "Molecular cloning of bullfrog (Rana catesbeiana) ornithine
RT transcarbamylase and induction of its mRNA during spontaneous
RT metamorphosis.";
RL Rep. Fac. Sci. Shizouka Univ. 29:45-54(1995).
CC -!- FUNCTION: OTC is necessary for the tadpoles transition from an
CC ammonotelic, aquatic larva to a ureotelic, terrestrial adult.
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;
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine
CC and carbamoyl phosphate: step 1/1.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development.
CC -!- INDUCTION: By thyroid hormone.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; M95193; AAA49528.1; -; mRNA.
DR EMBL; D38304; BAA22775.1; -; mRNA.
DR PIR; A48421; A48421.
DR AlphaFoldDB; P31326; -.
DR SMR; P31326; -.
DR UniPathway; UPA00158; UER00271.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Mitochondrion; Transferase;
KW Transit peptide; Urea cycle.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 31..350
FT /note="Ornithine carbamoyltransferase, mitochondrial"
FT /id="PRO_0000020338"
FT ACT_SITE 299
FT /evidence="ECO:0000250"
FT BINDING 86..90
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 259..263
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 298..301
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 39637 MW; E1E598355F03C13E CRC64;
MLHHMRTIIN ASWRYGNKCI VRQFGFSQTY SQLKGRDLLT LKNYSAEEIK YLLWVAADLK
YRIKEKGEYL PLLQGKSLAM IFEKRSTRTR LSTETGFALL GGHPSFLTTQ DIHLGVNESL
KDTARVLSGM TDAVLARVYH QSDLEVLAEE ASIPIVNGLS DDYHPIQILA DYLTIQEHYG
HLKGLTISWI GDGNNVLHSI MMSAAKFGMH LHIATPKGYE PNSSLTEAAK QFSKECGTKL
LMTNDPLEAA NGANVLVTDT WVSMGQEEEK KKRLLDFKGY QITMKTAKLA APNWIFLHCL
PRKPEEVDDE VFYCPKSLVF QEAENRKWTI MGVMVSLLTD YSPQLLRPTF
