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Protein

Oxalate--CoA ligase

Gene

AAE3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Oxalyl-CoA synthetase acting exclusively against oxalate. No activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, glyoxylate or glutarate. Required for oxalate degradation, normal seed development and defense against oxalate-producing fungal pathogens.1 Publication

Catalytic activityi

ATP + oxalate + CoA = AMP + diphosphate + oxalyl-CoA.1 Publication

Kineticsi

  1. KM=149 µM for oxalate1 Publication
  1. Vmax=11.4 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei394 – 3941ATPBy similarity
Binding sitei409 – 4091ATPBy similarity
Binding sitei500 – 5001ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi170 – 1789ATPBy similarity
Nucleotide bindingi311 – 3166ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • oxalate-CoA ligase activity Source: TAIR

GO - Biological processi

  • defense response to fungus Source: TAIR
  • oxalate catabolic process Source: TAIR
  • positive regulation of seed germination Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to cytokinin Source: TAIR
  • seed coat development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Plant defense

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G48990-MONOMER.
BRENDAi6.2.1.8. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxalate--CoA ligaseCurated (EC:6.2.1.81 Publication)
Alternative name(s):
4-coumarate--CoA ligase isoform 8
Short name:
At4CL8
4-coumarate--CoA ligase-like 10
Acyl-activating enzyme 31 Publication
Adenosine monophosphate binding protein 3
Short name:
AtMPBP3
Oxalyl-CoA synthetase
Gene namesi
Name:AAE31 Publication
Synonyms:4CLL10, AMPBP3
Ordered Locus Names:At3g48990Imported
ORF Names:T2J13.170Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G48990.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytoplasm Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Decreased and delayed seed germination, but no other growth and development phenotypes. Increased sensitivity to oxalate-producing fungal pathogens.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Oxalate--CoA ligasePRO_0000415617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9SMT7.
PRIDEiQ9SMT7.

PTM databases

iPTMnetiQ9SMT7.

Expressioni

Inductioni

Up-regulated upon infection with oxalate-producing fungal pathogens.1 Publication

Gene expression databases

GenevisibleiQ9SMT7. AT.

Interactioni

Protein-protein interaction databases

BioGridi9378. 2 interactions.
STRINGi3702.AT3G48990.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SMT7.
SMRiQ9SMT7. Positions 32-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni241 – 31070SBD1By similarityAdd
BLAST
Regioni311 – 37464SBD2By similarityAdd
BLAST

Domaini

Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1176. Eukaryota.
COG0318. LUCA.
HOGENOMiHOG000229994.
InParanoidiQ9SMT7.
OMAiRAPPEFQ.
PhylomeDBiQ9SMT7.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SMT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSDTLSGLL ENVAKKFPDR RALSVSGKFN LTHARLHDLI ERAASRLVSD
60 70 80 90 100
AGIKPGDVVA LTFPNTVEFV IMFLAVIRAR ATAAPLNAAY TAEEFEFYLS
110 120 130 140 150
DSDSKLLLTS KEGNAPAQEA ASKLKISHVT ATLLDAGSDL VLSVADSDSV
160 170 180 190 200
VDSATELVNH PDDGALFLHT SGTTSRPKGV PLTQLNLASS VKNIKAVYKL
210 220 230 240 250
TESDSTVIVL PLFHVHGLLA GLLSSLGAGA AVTLPAAGRF SATTFWPDMK
260 270 280 290 300
KYNATWYTAV PTIHQIILDR HASHPETEYP KLRFIRSCSA SLAPVILSRL
310 320 330 340 350
EEAFGAPVLE AYAMTEATHL MSSNPLPEEG PHKPGSVGKP VGQEMAILNE
360 370 380 390 400
KGEIQEPNNK GEVCIRGPNV TKGYKNNPEA NKAGFEFGWF HTGDIGYFDT
410 420 430 440 450
DGYLHLVGRI KELINRGGEK ISPIEVDAVL LTHPDVSQGV AFGVPDEKYG
460 470 480 490 500
EEINCAVIPR EGTTVTEEDI KAFCKKNLAA FKVPKRVFIT DNLPKTASGK
510
IQRRIVAQHF LEKP
Length:514
Mass (Da):55,544
Last modified:May 1, 2000 - v1
Checksum:iDAF41A51D8934371
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371G → V in AAM65672 (Ref. 5) Curated
Sequence conflicti209 – 2091V → F in AAM65672 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503762 mRNA. Translation: AAM28620.1.
AL132967 Genomic DNA. Translation: CAB62011.1.
CP002686 Genomic DNA. Translation: AEE78480.1.
AY050824 mRNA. Translation: AAK92759.1.
AY062759 mRNA. Translation: AAL32837.1.
AY117254 mRNA. Translation: AAM51329.1.
BT003376 mRNA. Translation: AAO30039.1.
AY088127 mRNA. Translation: AAM65672.1.
PIRiT46131.
RefSeqiNP_190468.1. NM_114758.4.
UniGeneiAt.19806.

Genome annotation databases

EnsemblPlantsiAT3G48990.1; AT3G48990.1; AT3G48990.
GeneIDi824060.
GrameneiAT3G48990.1; AT3G48990.1; AT3G48990.
KEGGiath:AT3G48990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503762 mRNA. Translation: AAM28620.1.
AL132967 Genomic DNA. Translation: CAB62011.1.
CP002686 Genomic DNA. Translation: AEE78480.1.
AY050824 mRNA. Translation: AAK92759.1.
AY062759 mRNA. Translation: AAL32837.1.
AY117254 mRNA. Translation: AAM51329.1.
BT003376 mRNA. Translation: AAO30039.1.
AY088127 mRNA. Translation: AAM65672.1.
PIRiT46131.
RefSeqiNP_190468.1. NM_114758.4.
UniGeneiAt.19806.

3D structure databases

ProteinModelPortaliQ9SMT7.
SMRiQ9SMT7. Positions 32-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9378. 2 interactions.
STRINGi3702.AT3G48990.1.

PTM databases

iPTMnetiQ9SMT7.

Proteomic databases

PaxDbiQ9SMT7.
PRIDEiQ9SMT7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G48990.1; AT3G48990.1; AT3G48990.
GeneIDi824060.
GrameneiAT3G48990.1; AT3G48990.1; AT3G48990.
KEGGiath:AT3G48990.

Organism-specific databases

TAIRiAT3G48990.

Phylogenomic databases

eggNOGiKOG1176. Eukaryota.
COG0318. LUCA.
HOGENOMiHOG000229994.
InParanoidiQ9SMT7.
OMAiRAPPEFQ.
PhylomeDBiQ9SMT7.

Enzyme and pathway databases

BioCyciARA:AT3G48990-MONOMER.
BRENDAi6.2.1.8. 399.

Miscellaneous databases

PROiQ9SMT7.

Gene expression databases

GenevisibleiQ9SMT7. AT.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that participate in fatty acid and glycerolipid metabolism."
    Shockey J.M., Fulda M.S., Browse J.A.
    Plant Physiol. 129:1710-1722(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The substrate specificity-determining amino acid code of 4-coumarate:CoA ligase."
    Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D., Kombrink E., Stuible H.-P.
    Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A previously unknown oxalyl-CoA synthetase is important for oxalate catabolism in Arabidopsis."
    Foster J., Kim H.U., Nakata P.A., Browse J.
    Plant Cell 24:1217-1229(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INDUCTION BY PATHOGEN.
    Strain: cv. Columbia.

Entry informationi

Entry namei4CLLA_ARATH
AccessioniPrimary (citable) accession number: Q9SMT7
Secondary accession number(s): Q8L9Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.