CARB_ARATH
ID CARB_ARATH Reviewed; 1187 AA.
AC Q42601;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Carbamoyl-phosphate synthase large chain, chloroplastic;
DE EC=6.3.5.5 {ECO:0000305|PubMed:21265888};
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000303|PubMed:21265888};
DE AltName: Full=Protein VENOSA 3 {ECO:0000303|PubMed:21265888};
DE Flags: Precursor;
GN Name=CARB; Synonyms=VEN3 {ECO:0000303|PubMed:21265888};
GN OrderedLocusNames=At1g29900; ORFNames=F1N18.6;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Williamson C.L., Lake M.R., Slocum R.D.;
RT "A cDNA encoding carbamoyl phosphate synthetase large subunit (carB) from
RT Arabidopsis.";
RL (er) Plant Gene Register PGR96-055(1996).
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 TISSUE SPECIFICITY, AND 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PRO-149; GLY-587; ALA-844
RP AND PRO-1014.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00409};
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 -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:15820655}.
CC -!- INDUCTION: By phosphate starvation in shoot.
CC {ECO:0000269|PubMed:15820655}.
CC -!- MISCELLANEOUS: The ven3-1, ven3-2, ven3-3 and ven3-4 phenotypes are
CC rescued by exogenous application of citrulline, an arginine precursor.
CC {ECO:0000305|PubMed:21265888}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; U40341; AAB67843.1; -; mRNA.
DR EMBL; AC008030; AAG10606.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31148.1; -; Genomic_DNA.
DR EMBL; AF367268; AAK56257.1; -; mRNA.
DR EMBL; AY133548; AAM91378.1; -; mRNA.
DR PIR; F86422; F86422.
DR RefSeq; NP_564338.1; NM_102730.2.
DR AlphaFoldDB; Q42601; -.
DR SMR; Q42601; -.
DR BioGRID; 25103; 16.
DR IntAct; Q42601; 1.
DR STRING; 3702.AT1G29900.1; -.
DR iPTMnet; Q42601; -.
DR MetOSite; Q42601; -.
DR PaxDb; Q42601; -.
DR PRIDE; Q42601; -.
DR ProMEX; Q42601; -.
DR ProteomicsDB; 222801; -.
DR EnsemblPlants; AT1G29900.1; AT1G29900.1; AT1G29900.
DR GeneID; 839868; -.
DR Gramene; AT1G29900.1; AT1G29900.1; AT1G29900.
DR KEGG; ath:AT1G29900; -.
DR Araport; AT1G29900; -.
DR TAIR; locus:2019302; AT1G29900.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_0_1; -.
DR InParanoid; Q42601; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 273358at2759; -.
DR PhylomeDB; Q42601; -.
DR BioCyc; ARA:AT1G29900-MON; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR PRO; PR:Q42601; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42601; baseline and differential.
DR Genevisible; Q42601; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; NAS:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR033937; MGS_CPS_CarB.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Chloroplast;
KW Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Plastid;
KW Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase;
KW Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..1187
FT /note="Carbamoyl-phosphate synthase large chain,
FT chloroplastic"
FT /id="PRO_0000423076"
FT DOMAIN 224..420
FT /note="ATP-grasp 1"
FT DOMAIN 782..975
FT /note="ATP-grasp 2"
FT DOMAIN 1042..1183
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT BINDING 251..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 393
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 808..865
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 933
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 946
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 946
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 948
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MUTAGEN 149
FT /note="P->L: In ven3-2; reduced plant size and reticulate
FT leaf phenotype."
FT /evidence="ECO:0000269|PubMed:21265888"
FT MUTAGEN 587
FT /note="G->E: In ven3-3; reticulate leaf phenotype."
FT /evidence="ECO:0000269|PubMed:21265888"
FT MUTAGEN 844
FT /note="A->T: In ven3-4; reduced plant size and reticulate
FT leaf phenotype."
FT /evidence="ECO:0000269|PubMed:21265888"
FT MUTAGEN 1014
FT /note="P->L: In ven3-1; reticulate leaf phenotype."
FT /evidence="ECO:0000269|PubMed:21265888"
SQ SEQUENCE 1187 AA; 129957 MW; 328072F4A5B671DC CRC64;
MRNHCLELSS NCSSIFASSK SNPRFSPSKL SYSTFFSRSA IYYRSKPKQA SSSSSFSTFP
PCLNRKSSLT HVLKPVSELA DTTTKPFSPE IVGKRTDLKK IMILGAGPIV IGQACEFDYS
GTQACKALRE EGYEVILINS NPATIMTDPE TANRTYIAPM TPELVEQVIE KERPDALLPT
MGGQTALNLA VALAESGALE KYGVELIGAK LGAIKKAEDR ELFKDAMKNI GLKTPPSGIG
TTLDECFDIA EKIGEFPLII RPAFTLGGTG GGIAYNKEEF ESICKSGLAA SATSQVLVEK
SLLGWKEYEL EVMRDLADNV VIICSIENID PMGVHTGDSI TVAPAQTLTD REYQRLRDYS
IAIIREIGVE CGGSNVQFAV NPVDGEVMII EMNPRVSRSS ALASKATGFP IAKMAAKLSV
GYTLDQIPND ITRKTPASFE PSIDYVVTKI PRFAFEKFPG SQPLLTTQMK SVGESMALGR
TFQESFQKAL RSLECGFSGW GCAKIKELDW DWDQLKYSLR VPNPDRIHAI YAAMKKGMKI
DEIYELSMVD KWFLTQLKEL VDVEQYLMSG TLSEITKEDL YEVKKRGFSD KQIAFATKTT
EEEVRTKRIS LGVVPSYKRV DTCAAEFEAH TPYMYSSYDV ECESAPNNKK KVLILGGGPN
RIGQGIEFDY CCCHTSFALQ DAGYETIMLN SNPETVSTDY DTSDRLYFEP LTIEDVLNVI
DLEKPDGIIV QFGGQTPLKL ALPIKHYLDK HMPMSLSGAG PVRIWGTSPD SIDAAEDRER
FNAILDELKI EQPKGGIAKS EADALAIAKE VGYPVVVRPS YVLGGRAMEI VYDDSRLITY
LENAVQVDPE RPVLVDKYLS DAIEIDVDTL TDSYGNVVIG GIMEHIEQAG VHSGDSACML
PTQTIPASCL QTIRTWTTKL AKKLNVCGLM NCQYAITTSG DVFLLEANPR ASRTVPFVSK
AIGHPLAKYA ALVMSGKSLK DLNFEKEVIP KHVSVKEAVF PFEKFQGCDV ILGPEMRSTG
EVMSISSEFS SAFAMAQIAA GQKLPLSGTV FLSLNDMTKP HLEKIAVSFL ELGFKIVATS
GTAHFLELKG IPVERVLKLH EGRPHAADMV ANGQIHLMLI TSSGDALDQK DGRQLRQMAL
AYKVPVITTV AGALATAEGI KSLKSSAIKM TALQDFFEVK NVSSLLV
