CARA_ARATH
ID CARA_ARATH Reviewed; 430 AA.
AC Q9LVW7; O24447;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Carbamoyl-phosphate synthase small chain, chloroplastic;
DE EC=6.3.5.5 {ECO:0000305|PubMed:21265888};
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000303|PubMed:21265888};
DE AltName: Full=Protein VENOSA 6 {ECO:0000303|PubMed:21265888};
DE Flags: Precursor;
GN Name=CARA; Synonyms=VEN6 {ECO:0000303|PubMed:21265888};
GN OrderedLocusNames=At3g27740; ORFNames=MGF10.15;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-430.
RC STRAIN=cv. Columbia;
RA Brandenburg S.A., Williamson C.L., Slocum R.D.;
RT "Characterization of a cDNA encoding the small subunit of Arabidopsis
RT carbamoyl phosphate synthetase.";
RL (er) Plant Gene Register PGR98-087(1998).
RN [5]
RP INDUCTION.
RX PubMed=15820655; DOI=10.1016/j.plaphy.2005.01.003;
RA Hewitt M.M., Carr J.M., Williamson C.L., Slocum R.D.;
RT "Effects of phosphate limitation on expression of genes involved in
RT pyrimidine synthesis and salvaging in Arabidopsis.";
RL Plant Physiol. Biochem. 43:91-99(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-410, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=21265888; DOI=10.1111/j.1365-313x.2010.04425.x;
RA Molla-Morales A., Sarmiento-Manus R., Robles P., Quesada V.,
RA Perez-Perez J.M., Gonzalez-Bayon R., Hannah M.A., Willmitzer L.,
RA Ponce M.R., Micol J.L.;
RT "Analysis of ven3 and ven6 reticulate mutants reveals the importance of
RT arginine biosynthesis in Arabidopsis leaf development.";
RL Plant J. 65:335-345(2011).
CC -!- FUNCTION: Subunit of the carbamoyl-phosphate synthetase (CPS) composed
CC of a small chain CARA/VEN6 and a large chain CARB/VEN3. Involved in
CC arginine biosynthesis. Required for mesophyll development.
CC {ECO:0000269|PubMed:21265888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000305|PubMed:21265888};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18635;
CC Evidence={ECO:0000305|PubMed:21265888};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LVW7-1; Sequence=Displayed;
CC -!- INDUCTION: By phosphate starvation in shoot.
CC {ECO:0000269|PubMed:15820655}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size. Reticulate leaves with
CC reduced number of palissade mesophyll cells.
CC {ECO:0000269|PubMed:21265888}.
CC -!- MISCELLANEOUS: The ven6-1 phenotype is rescued by exogenous application
CC of citrulline, an arginine precursor. {ECO:0000305|PubMed:21265888}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25961.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018114; BAB02698.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77358.1; -; Genomic_DNA.
DR EMBL; AY046004; AAK76678.1; -; mRNA.
DR EMBL; AY079315; AAL85046.1; -; mRNA.
DR EMBL; U73175; AAC25961.1; ALT_INIT; mRNA.
DR RefSeq; NP_566824.1; NM_113690.3. [Q9LVW7-1]
DR AlphaFoldDB; Q9LVW7; -.
DR SMR; Q9LVW7; -.
DR BioGRID; 7726; 8.
DR IntAct; Q9LVW7; 1.
DR STRING; 3702.AT3G27740.1; -.
DR MEROPS; C26.A04; -.
DR PaxDb; Q9LVW7; -.
DR PRIDE; Q9LVW7; -.
DR ProteomicsDB; 222784; -. [Q9LVW7-1]
DR EnsemblPlants; AT3G27740.1; AT3G27740.1; AT3G27740. [Q9LVW7-1]
DR GeneID; 822396; -.
DR Gramene; AT3G27740.1; AT3G27740.1; AT3G27740. [Q9LVW7-1]
DR KEGG; ath:AT3G27740; -.
DR Araport; AT3G27740; -.
DR TAIR; locus:2089149; AT3G27740.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_035901_2_1_1; -.
DR InParanoid; Q9LVW7; -.
DR OMA; CFNTGMT; -.
DR PhylomeDB; Q9LVW7; -.
DR BioCyc; ARA:AT3G27740-MON; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR PRO; PR:Q9LVW7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVW7; baseline and differential.
DR Genevisible; Q9LVW7; AT.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:TAIR.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:TAIR.
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:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid biosynthesis; Arginine biosynthesis;
KW ATP-binding; Chloroplast; Glutamine amidotransferase; Ligase;
KW Nucleotide-binding; Plastid; Pyrimidine biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..430
FT /note="Carbamoyl-phosphate synthase small chain,
FT chloroplastic"
FT /id="PRO_0000423074"
FT DOMAIN 243..429
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 402
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /evidence="ECO:0000250"
FT MUTAGEN 410
FT /note="H->Y: In ven6-1; reticulate leaf phenotype."
FT /evidence="ECO:0000269|PubMed:21265888"
SQ SEQUENCE 430 AA; 47059 MW; 25E615DB33D26ECC CRC64;
MAMATRTLGF VLPTSLSSQP SFDRRGGGFR VSVIRCSTSP LTFPTSGVVE KPWTSYNARL
VLEDGSIWPA KSFGAPGTRI AELVFNTSLT GYQEILTDPS YAGQFVLMTN PQIGNTGVNP
DDEESGQCFL TGLVIRNLSI STSNWRCTKT LADYLTERDI MGVYDLDTRA ITRRLREDGS
LIGVLSTEQS KTDDELLQMS RSWDIVGIDL ISDVSCKSPY EWVDKTNAEW DFNTNSRDGK
SYKVIAYDFG IKQNILRRLS SYGCQITVVP STFPAAEALK MNPDGILFSN GPGDPSAVPY
AVETVKELLG KVPVYGICMG HQLLGQALGG KTFKMKFGHH GGNHPVRNNR TGQVEISAQN
HNYAVDPASL PGGVEVTHVN LNDGSCAGLS FPEMNVMSLQ YHPEASPGPH DSDNAFREFI
ELMKRSKQSS
