KDTA_ARATH
ID KDTA_ARATH Reviewed; 447 AA.
AC Q8VZA5; Q9FFN3; Q9LZR2;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial;
DE Short=AtKdtA;
DE Short=Kdo transferase A;
DE EC=2.4.99.12;
DE EC=2.4.99.13;
DE AltName: Full=Bifunctional Kdo transferase;
DE AltName: Full=Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
DE AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
DE Flags: Precursor;
GN Name=KDTA; OrderedLocusNames=At5g03770; ORFNames=F17C15.190, MED24.5;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20124190; DOI=10.1093/glycob/cwq011;
RA Seveno M., Seveno-Carpentier E., Voxeur A., Menu-Bouaouiche L., Rihouey C.,
RA Delmas F., Chevalier C., Driouich A., Lerouge P.;
RT "Characterization of a putative 3-deoxy-D-manno-2-octulosonic acid (Kdo)
RT transferase gene from Arabidopsis thaliana.";
RL Glycobiology 20:617-628(2010).
RN [6]
RP PATHWAY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=21709257; DOI=10.1073/pnas.1108840108;
RA Li C., Guan Z., Liu D., Raetz C.R.;
RT "Pathway for lipid A biosynthesis in Arabidopsis thaliana resembling that
RT of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11387-11392(2011).
CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC glycolipid that in bacteria anchors the lipopolysaccharide to the outer
CC membrane of the cell. Catalyzes the transfer of two 3-deoxy-D-manno-
CC octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the
CC tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Lipid A-
CC like molecules in plants may serve as structural components of the
CC outer membranes of mitochondria and/or chloroplasts, or may be involved
CC in signal transduction or plant defense responses. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) =
CC alpha-Kdo-(2->6)-lipid IVA + CMP + H(+); Xref=Rhea:RHEA:28066,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->6)-lipid IVA + CMP-3-deoxy-beta-D-manno-
CC octulosonate = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP +
CC H(+); Xref=Rhea:RHEA:28062, ChEBI:CHEBI:15378, ChEBI:CHEBI:60364,
CC ChEBI:CHEBI:60365, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987;
CC EC=2.4.99.13;
CC -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-
CC lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step
CC 1/4. {ECO:0000269|PubMed:21709257}.
CC -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-
CC lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step
CC 2/4. {ECO:0000269|PubMed:21709257}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20124190}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:20124190}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants lacking KDTA accumulate high levels of
CC tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
CC {ECO:0000269|PubMed:20124190, ECO:0000269|PubMed:21709257}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 30 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08602.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB82942.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB005235; BAB08602.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL162506; CAB82942.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90652.1; -; Genomic_DNA.
DR EMBL; AY065115; AAL38291.1; -; mRNA.
DR EMBL; AY128758; AAM91158.1; -; mRNA.
DR PIR; T48404; T48404.
DR RefSeq; NP_195997.2; NM_120458.3.
DR AlphaFoldDB; Q8VZA5; -.
DR SMR; Q8VZA5; -.
DR STRING; 3702.AT5G03770.1; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR PaxDb; Q8VZA5; -.
DR PRIDE; Q8VZA5; -.
DR ProteomicsDB; 250745; -.
DR EnsemblPlants; AT5G03770.1; AT5G03770.1; AT5G03770.
DR GeneID; 831727; -.
DR Gramene; AT5G03770.1; AT5G03770.1; AT5G03770.
DR KEGG; ath:AT5G03770; -.
DR Araport; AT5G03770; -.
DR TAIR; locus:2144643; AT5G03770.
DR eggNOG; ENOG502QSA5; Eukaryota.
DR HOGENOM; CLU_036146_1_0_1; -.
DR InParanoid; Q8VZA5; -.
DR OMA; FIKYEFW; -.
DR OrthoDB; 1258887at2759; -.
DR PhylomeDB; Q8VZA5; -.
DR BioCyc; ARA:AT5G03770-MON; -.
DR BRENDA; 2.4.99.12; 399.
DR BRENDA; 2.4.99.13; 399.
DR UniPathway; UPA00360; UER00483.
DR UniPathway; UPA00360; UER00484.
DR PRO; PR:Q8VZA5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZA5; baseline and differential.
DR Genevisible; Q8VZA5; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.11720; -; 1.
DR InterPro; IPR007507; Glycos_transf_N.
DR InterPro; IPR038107; Glycos_transf_N_sf.
DR InterPro; IPR039901; Kdotransferase.
DR PANTHER; PTHR42755; PTHR42755; 1.
DR Pfam; PF04413; Glycos_transf_N; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..447
FT /note="Probable 3-deoxy-D-manno-octulosonic acid
FT transferase, mitochondrial"
FT /id="PRO_0000421462"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 278..279
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 320..322
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 347..350
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT SITE 136
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 49888 MW; C36614207A499510 CRC64;
MKLGVFVYRL YRALTYGVSP LIHLHIRWRR LRGLEHFSRW PERFGHPSAV RPPGSLIWFH
AVSLGEGMAA IPVIRHCNEV KSDLTILMTT TTVSAFEVIK NQLPVGVLHQ FAPLDTPLAI
DRFLGHWKPN AIIIMENELW PNLIMAASGL LIPLGLLNAR MSTKSFKRWS SPLLLPLVSL
LLSKFSLIAP LSTLQGIRFQ LLHAPPFVIN YSGDLKYVVN KFHVSSGTSE SIRDLKVELA
EMKVWIASSL HRGEEEVILG VHNMLLESHP DSVVIIVPRH PHHGQQIAHK LRKDGQSVAL
RSQNEKLTPR KTNIYVVDTL GELRELYSVA PIAVIGGSFI PGLTGHNLSE AAAAGCAVIT
GCHVGHFSHM VKAMQQANPL SVTQVSTKLE LKEAVDLLLS NPEILETHQR ASKDVYESLS
SCIITNIWKL LNLHIFRGKS RNHIECK
