CDS5_ARATH
ID CDS5_ARATH Reviewed; 399 AA.
AC Q9M001;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phosphatidate cytidylyltransferase 5, chloroplastic {ECO:0000303|PubMed:20442275};
DE EC=2.7.7.41 {ECO:0000269|PubMed:20442275};
DE AltName: Full=CDP-DAG synthase 5;
DE AltName: Full=CDP-DG synthase 5;
DE AltName: Full=CDP-diacylglycerol synthase 5;
DE Short=CDS 5;
DE AltName: Full=CDP-diglyceride pyrophosphorylase 5;
DE AltName: Full=CDP-diglyceride synthase 5;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase 5;
DE Flags: Precursor;
GN Name=CDS5 {ECO:0000303|PubMed:20442275};
GN OrderedLocusNames=At3g60620 {ECO:0000312|Araport:AT3G60620};
GN ORFNames=T4C21_30 {ECO:0000312|EMBL:CAB82666.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20442275; DOI=10.1104/pp.110.156422;
RA Haselier A., Akbari H., Weth A., Baumgartner W., Frentzen M.;
RT "Two closely related genes of Arabidopsis encode plastidial
RT cytidinediphosphate diacylglycerol synthases essential for photoautotrophic
RT growth.";
RL Plant Physiol. 153:1372-1384(2010).
CC -!- FUNCTION: May be involved in the synthesis of minor phospholipids and
CC in modulation of IP3-mediated signal transduction. Promotes the
CC biosynthesis of plastidial phosphatidylglycerol (PG) which is required
CC for structure and function of thylakoid membranes and, hence, for
CC photoautotrophic growth. {ECO:0000269|PubMed:20442275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000269|PubMed:20442275};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20442275};
CC Note=Requires a divalent cation for activity. Displays highest
CC activities with MgCl(2). {ECO:0000269|PubMed:20442275};
CC -!- ACTIVITY REGULATION: Highest activities is obtained at about 30 mM CTP
CC and 2 mM phosphatidic acid (PA). {ECO:0000269|PubMed:20442275}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20442275};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000269|PubMed:20442275}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:20442275}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: When associated with the disruption of CDS5,
CC requires sucrose (Suc) treatment to grow. Pale yellow-green leaves with
CC reduced chlorophyll levels but an increased chlorophyll a/b ratio.
CC Reduced plastidial phosphatidylglycerol (PG) biosynthesis leading to
CC abnormal thylakoid membrane development. {ECO:0000269|PubMed:20442275}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; AL162295; CAB82666.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80089.1; -; Genomic_DNA.
DR EMBL; AY035018; AAK59523.1; -; mRNA.
DR EMBL; AY059084; AAL15190.1; -; mRNA.
DR PIR; T47873; T47873.
DR RefSeq; NP_191621.1; NM_115926.4.
DR AlphaFoldDB; Q9M001; -.
DR SMR; Q9M001; -.
DR IntAct; Q9M001; 4.
DR STRING; 3702.AT3G60620.1; -.
DR PaxDb; Q9M001; -.
DR ProteomicsDB; 222810; -.
DR EnsemblPlants; AT3G60620.1; AT3G60620.1; AT3G60620.
DR GeneID; 825233; -.
DR Gramene; AT3G60620.1; AT3G60620.1; AT3G60620.
DR KEGG; ath:AT3G60620; -.
DR Araport; AT3G60620; -.
DR TAIR; locus:2101786; AT3G60620.
DR eggNOG; KOG1440; Eukaryota.
DR HOGENOM; CLU_037294_4_1_1; -.
DR InParanoid; Q9M001; -.
DR OMA; CPCRSTP; -.
DR OrthoDB; 1072976at2759; -.
DR PhylomeDB; Q9M001; -.
DR BRENDA; 2.7.7.41; 399.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:Q9M001; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M001; baseline and differential.
DR Genevisible; Q9M001; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IMP:TAIR.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR000374; PC_trans.
DR PROSITE; PS01315; CDS; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Plastid; Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 27..399
FT /note="Phosphatidate cytidylyltransferase 5, chloroplastic"
FT /id="PRO_0000431834"
FT TRANSMEM 123..143
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
SQ SEQUENCE 399 AA; 43251 MW; BB667730E84CAA1A CRC64;
MAPFVEVCRY KPLPLSLSSL CTCPCRSSPR KYLILPQFSE KYPKPLLSHS RFTPISVNRR
VITAVARAES NQIGDDANSK EEHNIDQELQ NVEEDSSLDD QKQKSRSQFK KRVTFGLGIG
LSVGGIVLAG GWVFTVAVAA AVLLSAREYF ELVRSKGIAQ GMTPPPRYLS RVCSIICALM
PILTLYFGHI DISITSAAFV VAMALLLQRG NPRFSQLSST MFGLFYCGYL PCFWVKLRCG
LTAPVLNTGI GRSWPTILGG QAHWTVGLVA ILISFCGIIA SDTFAFLGGK AFGRTPLISI
SPKKTWEGAF AGLVGCISIT ILLSKSLSWP QSLVSTIAFG VLNFFGSVFG DLTESMIKRD
AGVKDSGSLI PGHGGILDRV DSYIFTGALA YSFVRLHGV
