ID OTC_ASPNG Reviewed; 370 AA.
AC P11066;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE EC=2.1.3.3;
DE AltName: Full=Ornithine transcarbamylase;
DE Short=OTCase;
DE Flags: Precursor;
GN Name=argB;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3443301; DOI=10.1016/0378-1119(87)90234-4;
RA Buxton F.P., Gwynne D.I., Garven S., Sibley S., Davies R.W.;
RT "Cloning and molecular analysis of the ornithine carbamoyl transferase gene
RT of Aspergillus niger.";
RL Gene 60:255-266(1987).
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: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; M19158; AAA32688.1; -; mRNA.
DR PIR; A27362; OWASG.
DR AlphaFoldDB; P11066; -.
DR SMR; P11066; -.
DR PaxDb; 5061-CADANGAP00011057; -.
DR VEuPathDB; FungiDB:An14g03400; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1170126; -.
DR VEuPathDB; FungiDB:ATCC64974_2980; -.
DR VEuPathDB; FungiDB:M747DRAFT_320140; -.
DR eggNOG; KOG1504; Eukaryota.
DR UniPathway; UPA00068; UER00112.
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-UniPathway.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00658; orni_carb_tr; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Mitochondrion; Transferase;
KW Transit peptide.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..370
FT /note="Ornithine carbamoyltransferase, mitochondrial"
FT /id="PRO_0000042692"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 97..100
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 148
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 175
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 178
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 216
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 282
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 286
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 287
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 324..325
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 351
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
SQ SEQUENCE 370 AA; 39925 MW; 77AA84B828FA665F CRC64;
MPSPLRTAPQ PPLRAFHNPP ALRRLYSSTS HSAATPATSP FAPRHLLSIA DLTPTEFATL
VRNASSHKRA IKSGSIPQSL HGALSGKTVA MMFSKRSTRT RISTEGAVVQ MGGHPMFLGK
DDIQLGVNES LYDTAVVVSS MVECIVARVG KHADVADLAK HSTKPVINAL CDSYHPLQAI
ADFQTISEHF AASGKGKLEG LGLNGLKIAW VGDANNVLFD MAISARKMGV DVAVATPKGY
EIPKEMLEII EKAGEGVKSP GKLVQTNVPE EAVKGADVLV TDTWVSMGQE EEAAKRLRDF
AGFQITSELA KRGGAKEGWR FMHCLPRHPE EVADEVFYGH RSLVFPEAEN RLWAAISALE
GFVVNKGKIE
//
