OTC_SCHPO
ID OTC_SCHPO Reviewed; 327 AA.
AC P31317;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE EC=2.1.3.3 {ECO:0000269|PubMed:1313366, ECO:0000269|PubMed:18849471};
DE AltName: Full=Ornithine transcarbamylase;
DE Short=OTCase;
DE Flags: Precursor;
GN Name=arg3; ORFNames=SPAC4G9.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 38365 / 975;
RX PubMed=1313366; DOI=10.1111/j.1432-1033.1992.tb16749.x;
RA van Huffel C., Dubois E., Messenguy F.;
RT "Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces
RT pombe on a 10-kb DNA fragment. Heterologous expression and mitochondrial
RT targeting of their translation products.";
RL Eur. J. Biochem. 205:33-43(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TRX2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18849471; DOI=10.1128/ec.00106-08;
RA Song J.Y., Kim K.D., Roe J.H.;
RT "Thiol-independent action of mitochondrial thioredoxin to support the urea
RT cycle of arginine biosynthesis in Schizosaccharomyces pombe.";
RL Eukaryot. Cell 7:2160-2167(2008).
CC -!- FUNCTION: Ornithine carbamoyltransferase involved in the synthesis of
CC arginine from glutamate via ornithine and the urea cycle.
CC {ECO:0000269|PubMed:1313366, ECO:0000269|PubMed:18849471}.
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:1313366,
CC ECO:0000269|PubMed:18849471};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19514;
CC Evidence={ECO:0000305|PubMed:1313366, ECO:0000305|PubMed:18849471};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC {ECO:0000305|PubMed:1313366, ECO:0000305|PubMed:18849471}.
CC -!- SUBUNIT: Interacts with trx2. {ECO:0000269|PubMed:18849471}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:1313366,
CC ECO:0000305|PubMed:18849471}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; X63577; CAA45133.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93560.1; -; Genomic_DNA.
DR PIR; S22390; OWZP.
DR RefSeq; NP_593692.1; NM_001019124.2.
DR AlphaFoldDB; P31317; -.
DR SMR; P31317; -.
DR BioGRID; 280008; 45.
DR STRING; 4896.SPAC4G9.10.1; -.
DR MaxQB; P31317; -.
DR PaxDb; P31317; -.
DR EnsemblFungi; SPAC4G9.10.1; SPAC4G9.10.1:pep; SPAC4G9.10.
DR GeneID; 2543593; -.
DR KEGG; spo:SPAC4G9.10; -.
DR PomBase; SPAC4G9.10; arg3.
DR VEuPathDB; FungiDB:SPAC4G9.10; -.
DR eggNOG; KOG1504; Eukaryota.
DR HOGENOM; CLU_043846_3_0_1; -.
DR InParanoid; P31317; -.
DR OMA; DGNNVCN; -.
DR PhylomeDB; P31317; -.
DR Reactome; R-SPO-1268020; Mitochondrial protein import.
DR Reactome; R-SPO-70635; Urea cycle.
DR UniPathway; UPA00068; UER00112.
DR PRO; PR:P31317; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IMP:PomBase.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IMP:PomBase.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IC:PomBase.
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.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..327
FT /note="Ornithine carbamoyltransferase, mitochondrial"
FT /id="PRO_0000020346"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 63..66
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 114
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 141
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 144
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 172
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 236
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 240
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 241
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 276..277
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 303
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
SQ SEQUENCE 327 AA; 36119 MW; BF0E83E3C0051884 CRC64;
MSFKKFPRHL LSIRDLSRGE IVKLIDRSSE IKQAYKQNFQ NRRSVQMSGL SSQNVAMIFS
KRSTRTRVSV ESAVSCLGGN AMFLGKDDIQ LGVNESLYDT SKVISSMVSG IVARVNKYSD
VATLAKHASC PVINGLCDTF HPLQALADLL TIKETFKSFD GLKVAWVGDA NNVLHDLMIA
NAKVGIHTSV AKPKDVNVRD DILSIVNEAA NENGSTFEIV NDPKVAVKNA DIVVTDTWIS
MGQEAEKEQR LKQFTGFQVT GEIMKLAKPS CKFMHCLPRH PEEVSDEVFY GENSLVFQEA
ENRKWTTVAV LEALLVNRGE ILPPASA
