PYRB_ARATH
ID PYRB_ARATH Reviewed; 390 AA.
AC P49077; Q683J9; Q94A47; Q9LTR1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Aspartate carbamoyltransferase, chloroplastic;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
DE Flags: Precursor;
GN Name=PYRB; OrderedLocusNames=At3g20330; ORFNames=MQC12.7;
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 [MRNA].
RX PubMed=8041358; DOI=10.1007/bf00280183;
RA Nasr F., Bertauche N., Dufour M.E., Minet M., Lacroute F.;
RT "Heterospecific cloning of Arabidopsis thaliana cDNAs by direct
RT complementation of pyrimidine auxotrophic mutants of Saccharomyces
RT cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the
RT second, fifth and sixth steps of the de novo pyrimidine biosynthesis
RT pathway.";
RL Mol. Gen. Genet. 244:23-32(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC -!- ACTIVITY REGULATION: Allosterically regulated by UMP. {ECO:0000250}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000305}.
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DR EMBL; X71843; CAA50687.1; -; mRNA.
DR EMBL; AB024036; BAB02813.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76365.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64914.1; -; Genomic_DNA.
DR EMBL; AY050381; AAK91399.1; -; mRNA.
DR EMBL; AY090338; AAL90999.1; -; mRNA.
DR EMBL; AK175118; BAD42881.1; -; mRNA.
DR PIR; S46441; S46441.
DR RefSeq; NP_001326915.1; NM_001338476.1.
DR RefSeq; NP_188668.1; NM_112924.4.
DR PDB; 6YPO; X-ray; 1.67 A; A/B=82-390.
DR PDB; 6YS6; X-ray; 1.55 A; A/B/C=82-390.
DR PDB; 6YSP; X-ray; 1.38 A; A/B/C=82-390.
DR PDB; 6YVB; X-ray; 1.83 A; A/B/C/D/E/F=82-390.
DR PDB; 6YW9; X-ray; 1.68 A; A/B/C=82-390.
DR PDB; 6YWJ; X-ray; 2.40 A; A/B=82-390.
DR PDB; 6YY1; X-ray; 3.06 A; A/B/C/D/E/F=82-390.
DR PDBsum; 6YPO; -.
DR PDBsum; 6YS6; -.
DR PDBsum; 6YSP; -.
DR PDBsum; 6YVB; -.
DR PDBsum; 6YW9; -.
DR PDBsum; 6YWJ; -.
DR PDBsum; 6YY1; -.
DR AlphaFoldDB; P49077; -.
DR SMR; P49077; -.
DR BioGRID; 6909; 2.
DR IntAct; P49077; 1.
DR STRING; 3702.AT3G20330.1; -.
DR SwissPalm; P49077; -.
DR PaxDb; P49077; -.
DR PRIDE; P49077; -.
DR ProteomicsDB; 226017; -.
DR EnsemblPlants; AT3G20330.1; AT3G20330.1; AT3G20330.
DR EnsemblPlants; AT3G20330.2; AT3G20330.2; AT3G20330.
DR GeneID; 821577; -.
DR Gramene; AT3G20330.1; AT3G20330.1; AT3G20330.
DR Gramene; AT3G20330.2; AT3G20330.2; AT3G20330.
DR KEGG; ath:AT3G20330; -.
DR Araport; AT3G20330; -.
DR TAIR; locus:2092369; AT3G20330.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_043846_1_1_1; -.
DR InParanoid; P49077; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1404554at2759; -.
DR PhylomeDB; P49077; -.
DR BioCyc; ARA:AT3G20330-MON; -.
DR BioCyc; MetaCyc:AT3G20330-MON; -.
DR UniPathway; UPA00070; UER00116.
DR PRO; PR:P49077; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P49077; baseline and differential.
DR Genevisible; P49077; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Chloroplast; Plastid;
KW Pyrimidine biosynthesis; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..390
FT /note="Aspartate carbamoyltransferase, chloroplastic"
FT /id="PRO_0000020348"
FT CONFLICT 225
FT /note="T -> N (in Ref. 4; AAK91399/AAL90999)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="Y -> F (in Ref. 2; CAA50687)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="R -> S (in Ref. 4; AAK91399/AAL90999)"
FT /evidence="ECO:0000305"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6YWJ"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 95..113
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6YSP"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6YSP"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:6YSP"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:6YSP"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6YPO"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:6YSP"
FT HELIX 368..388
FT /evidence="ECO:0007829|PDB:6YSP"
SQ SEQUENCE 390 AA; 43167 MW; EE8C9216629E826E CRC64;
MSIASSLTSA TLCGASVFPK ALACSSEFPI NLPSPFESSK ICLTSFPASR DLKKNATLNL
TRNVGPVRCH AMQAGTRELK KFELSDVIEG KQFDREMLSA IFDVAREMEK IEKSSSQSEI
LKGYLMATLF YEPSTRTRLS FESAMKRLGG EVLTTENARE FSSAAKGETL EDTIRTVEGY
SDIIVMRHFE SGAARKAAAT ANIPVINAGD GPGEHPTQAL LDVYTIQSEI GKLDGISVAL
VGDLANGRTV RSLAYLLAKF KDVKIYFVSP EIVKMKDDIK DYLTSSGVEW EESSDLMEVA
SKCDVVYQTR IQRERFGERL DLYEAARGKY IVDKDLLGVM QKKAIIMHPL PRLDEITADV
DADPRAAYFR QAKNGLFIRM ALLKLLLVGW
