OTC_ARATH
ID OTC_ARATH Reviewed; 375 AA.
AC O50039; Q9FWS2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ornithine transcarbamylase, chloroplastic;
DE Short=OTCase;
DE EC=2.1.3.3;
DE AltName: Full=Ornithine carbamoyltransferase, chloroplastic;
DE Flags: Precursor;
GN Name=OTC; OrderedLocusNames=At1g75330; ORFNames=F1B16.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10561504; DOI=10.1016/s0014-5793(99)01426-x;
RA Quesada V., Ponce M.R., Micol J.L.;
RT "OTC and AUL1, two convergent and overlapping genes in the nuclear genome
RT of Arabidopsis thaliana.";
RL FEBS Lett. 461:101-106(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-54, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER GLN-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; AJ000476; CAA04115.1; -; mRNA.
DR EMBL; AJ002524; CAA05510.1; -; Genomic_DNA.
DR EMBL; AC023754; AAG13075.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35701.1; -; Genomic_DNA.
DR EMBL; AF370270; AAK44085.1; -; mRNA.
DR EMBL; AY063030; AAL34204.1; -; mRNA.
DR PIR; G96783; G96783.
DR PIR; T51617; T51617.
DR RefSeq; NP_177667.1; NM_106187.4.
DR AlphaFoldDB; O50039; -.
DR SMR; O50039; -.
DR BioGRID; 29088; 3.
DR STRING; 3702.AT1G75330.1; -.
DR iPTMnet; O50039; -.
DR PaxDb; O50039; -.
DR PRIDE; O50039; -.
DR ProteomicsDB; 226041; -.
DR EnsemblPlants; AT1G75330.1; AT1G75330.1; AT1G75330.
DR GeneID; 843869; -.
DR Gramene; AT1G75330.1; AT1G75330.1; AT1G75330.
DR KEGG; ath:AT1G75330; -.
DR Araport; AT1G75330; -.
DR TAIR; locus:2018467; AT1G75330.
DR eggNOG; KOG1504; Eukaryota.
DR HOGENOM; CLU_043846_3_2_1; -.
DR InParanoid; O50039; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 1404554at2759; -.
DR PhylomeDB; O50039; -.
DR BioCyc; MetaCyc:AT1G75330-MON; -.
DR PRO; PR:O50039; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O50039; baseline and differential.
DR Genevisible; O50039; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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 Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_01109; OTCase; 1.
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 InterPro; IPR024904; OTCase_ArgI.
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.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Arginine biosynthesis; Chloroplast;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 54..375
FT /note="Ornithine transcarbamylase, chloroplastic"
FT /id="PRO_0000020340"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 123..126
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 174
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 201
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 204
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 232
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 293
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 297
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 298
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 333..334
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 361
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 54
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 158
FT /note="R -> P (in Ref. 1; CAA04115/CAA05510)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="E -> K (in Ref. 1; CAA04115/CAA05510)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..222
FT /note="VEGT -> FERK (in Ref. 1; CAA04115/CAA05510)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="N -> Y (in Ref. 1; CAA04115/CAA05510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41002 MW; 9DA2A0B512FCA323 CRC64;
MAAAMASHVS TARSPALSFS SSSSSFFPGT TLRRFSAVSL PSPALPRLRV SCQASSVTSP
SSPSDVKGKS DLKDFLAIDD FDTATIKTIL DKASEVKALL KSGERNYLPF KGKSMSMIFA
KPSMRTRVSF ETGFFLLGGH ALYLGPNDIQ MGKREETRDV ARVLSRYNDI IMARVFAHQD
ILDLANYSSV PVVNGLTDHN HPCQIMADAL TMIEHIGQVE GTKVVYVGDG NNMVHSWLEL
ASVIPFHFVC ACPKGYEPDK ERVSKAKQAG LSKIEITNDP KEAVIGADVV YSDVWASMGQ
KDEAEARRKA FQGFQVDEAL MKLAGQKAYF MHCLPAERGV EVTNGVVEAP YSIVFPQAEN
RMHAQNAIML HLLGF
