OTC_PIG
ID OTC_PIG Reviewed; 328 AA.
AC O19072;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ornithine transcarbamylase, mitochondrial {ECO:0000305|PubMed:9420013};
DE Short=OTCase {ECO:0000303|PubMed:9420013};
DE EC=2.1.3.3 {ECO:0000250|UniProtKB:P00480};
DE AltName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE Flags: Precursor; Fragment;
GN Name=OTC {ECO:0000250|UniProtKB:P00480};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9420013; DOI=10.2527/1997.75123368x;
RA Koger J.B., Jones E.E.;
RT "Nucleotide sequence of porcine OTCase cDNA.";
RL J. Anim. Sci. 75:3368-3368(1997).
CC -!- FUNCTION: Catalyzes the second step of the urea cycle, the condensation
CC of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea
CC cycle ensures the detoxification of ammonia by converting it to urea
CC for excretion. {ECO:0000250|UniProtKB:P00480}.
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 Evidence={ECO:0000250|UniProtKB:P00480};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19515;
CC Evidence={ECO:0000250|UniProtKB:P00480};
CC -!- ACTIVITY REGULATION: Negatively regulated by lysine acetylation.
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine
CC and carbamoyl phosphate: step 1/1. {ECO:0000250|UniProtKB:P00480}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P00480}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- PTM: Acetylation at Lys-62 negatively regulates ornithine
CC carbamoyltransferase activity in response to nutrient signals.
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; Y13045; CAA73480.1; -; mRNA.
DR AlphaFoldDB; O19072; -.
DR SMR; O19072; -.
DR STRING; 9823.ENSSSCP00000013022; -.
DR PaxDb; O19072; -.
DR PeptideAtlas; O19072; -.
DR eggNOG; KOG1504; Eukaryota.
DR InParanoid; O19072; -.
DR SABIO-RK; O19072; -.
DR UniPathway; UPA00158; UER00271.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Arginine biosynthesis; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide;
KW Urea cycle.
FT TRANSIT <1..6
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT CHAIN 7..328
FT /note="Ornithine transcarbamylase, mitochondrial"
FT /id="PRO_0000020336"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 237..241
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 276..279
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 44
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 54
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 62
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 62
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 118
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 118
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 195
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 195
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 205
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 205
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 212
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 212
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 248
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 263
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 281
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 281
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT NON_TER 1
SQ SEQUENCE 328 AA; 36738 MW; 89302B9A471CD265 CRC64;
GGQPLQNKVQ LKGRDLLTLK NFTGEEIKYI LWLSADLKFR IKQKGEYLPL LQGKSLGMIF
EKRSTRTRLS TETGFALLGG HPCFLTTQDI HLGVNESLKD TARVLSSMTD AVLARVYKQS
DLDILAQEAS IPIINGLSDL YHPIQILADY LTLQEHYGAL KGLTLSWIGD GNNILHSIMM
SAAKFGMHLQ VATPKGYEPD PSITKLAEQY AKENGTNVSL TNDPLEAARG GNVLITDTWI
SMGQEEEKKK RLQAFQGYQV TMKTAEVAAS DWTFLHCLPR KPEEVDDEVF YSPQSLVFPE
AENRKWTIMA VMVSLLTDYS PQLQKPKF
