GenomeNet

Database: UniProt
Entry: Q42601
LinkDB: Q42601
Original site: Q42601 
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   13-FEB-2019, entry version 149.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain, chloroplastic;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
DE   AltName: Full=Protein VENOSA 6;
DE   Flags: Precursor;
GN   Name=CARB; Synonyms=VEN3; OrderedLocusNames=At1g29900;
GN   ORFNames=F1N18.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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)
RT   from 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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   of ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF PRO-149; GLY-587; ALA-844 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
RT   of arginine biosynthesis in Arabidopsis leaf development.";
RL   Plant J. 65:335-345(2011).
CC   -!- FUNCTION: Involved in arginine biosynthesis. Required for
CC       mesophyll development. {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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (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
CC       the 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
CC       are rescued by exogenous application of citrulline, an arginine
CC       precursor. {ECO:0000305|PubMed:21265888}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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   UniGene; At.10370; -.
DR   ProteinModelPortal; Q42601; -.
DR   SMR; Q42601; -.
DR   BioGrid; 25103; 2.
DR   IntAct; Q42601; 1.
DR   STRING; 3702.AT1G29900.1; -.
DR   iPTMnet; Q42601; -.
DR   PaxDb; Q42601; -.
DR   PRIDE; Q42601; -.
DR   ProMEX; Q42601; -.
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   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   InParanoid; Q42601; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 273358at2759; -.
DR   PhylomeDB; Q42601; -.
DR   BioCyc; ARA:AT1G29900-MONOMER; -.
DR   Reactome; R-ATH-500753; Pyrimidine biosynthesis.
DR   Reactome; R-ATH-70635; Urea cycle.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   PRO; PR:Q42601; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q42601; AT.
DR   GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
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: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; 3.40.50.1380; -; 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; 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;
KW   Chloroplast; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Plastid; Pyrimidine biosynthesis;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT       1     62       Chloroplast. {ECO:0000255}.
FT   CHAIN        63   1187       Carbamoyl-phosphate synthase large chain,
FT                                chloroplastic.
FT                                /FTId=PRO_0000423076.
FT   DOMAIN      224    420       ATP-grasp 1.
FT   DOMAIN      782    975       ATP-grasp 2.
FT   DOMAIN     1042   1183       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     251    308       ATP. {ECO:0000250}.
FT   NP_BIND     808    865       ATP. {ECO:0000250}.
FT   METAL       377    377       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       391    391       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       391    391       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       393    393       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       933    933       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       946    946       Magnesium or manganese 3. {ECO:0000250}.
FT   METAL       946    946       Magnesium or manganese 4. {ECO:0000250}.
FT   METAL       948    948       Magnesium or manganese 4. {ECO:0000250}.
FT   MUTAGEN     149    149       P->L: In ven3-2; reduced plant size and
FT                                reticulate leaf phenotype.
FT                                {ECO:0000269|PubMed:21265888}.
FT   MUTAGEN     587    587       G->E: In ven3-3; reticulate leaf
FT                                phenotype. {ECO:0000269|PubMed:21265888}.
FT   MUTAGEN     844    844       A->T: In ven3-4; reduced plant size and
FT                                reticulate leaf phenotype.
FT                                {ECO:0000269|PubMed:21265888}.
FT   MUTAGEN    1014   1014       P->L: In ven3-1; reticulate leaf
FT                                phenotype. {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
//
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