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Protein

Oxalate--CoA ligase

Gene

AAE3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei394ATPBy similarity1
Binding sitei409ATPBy similarity1
Binding sitei500ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi170 – 178ATPBy similarity9
Nucleotide bindingi311 – 316ATPBy similarity6

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

Keywordsi

Molecular functionLigase
Biological processPlant defense
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G48990-MONOMER
MetaCyc:AT3G48990-MONOMER
BRENDAi6.2.1.8 399
ReactomeiR-ATH-77289 Mitochondrial Fatty Acid Beta-Oxidation

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

AraportiAT3G48990
TAIRilocus:2101368 AT3G48990

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004156171 – 514Oxalate--CoA ligaseAdd BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

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

ExpressionAtlasiQ9SMT7 differential
GenevisibleiQ9SMT7 AT

Interactioni

Protein-protein interaction databases

BioGridi9378, 2 interactors
STRINGi3702.AT3G48990.1

Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 16Combined sources11
Beta strandi20 – 25Combined sources6
Turni26 – 28Combined sources3
Beta strandi29 – 32Combined sources4
Helixi33 – 50Combined sources18
Beta strandi58 – 61Combined sources4
Helixi67 – 78Combined sources12
Beta strandi82 – 85Combined sources4
Helixi92 – 101Combined sources10
Beta strandi104 – 112Combined sources9
Helixi115 – 123Combined sources9
Beta strandi127 – 132Combined sources6
Beta strandi141 – 144Combined sources4
Turni153 – 156Combined sources4
Beta strandi163 – 169Combined sources7
Beta strandi173 – 176Combined sources4
Beta strandi179 – 183Combined sources5
Helixi184 – 198Combined sources15
Beta strandi205 – 207Combined sources3
Helixi215 – 219Combined sources5
Turni220 – 222Combined sources3
Helixi223 – 227Combined sources5
Beta strandi231 – 234Combined sources4
Helixi242 – 251Combined sources10
Beta strandi256 – 259Combined sources4
Helixi261 – 273Combined sources13
Beta strandi283 – 287Combined sources5
Helixi294 – 304Combined sources11
Beta strandi308 – 314Combined sources7
Helixi315 – 317Combined sources3
Beta strandi319 – 323Combined sources5
Turni327 – 329Combined sources3
Beta strandi338 – 340Combined sources3
Beta strandi342 – 348Combined sources7
Beta strandi361 – 367Combined sources7
Helixi378 – 384Combined sources7
Beta strandi389 – 398Combined sources10
Beta strandi404 – 409Combined sources6
Helixi410 – 412Combined sources3
Beta strandi414 – 416Combined sources3
Beta strandi419 – 421Combined sources3
Helixi423 – 430Combined sources8
Beta strandi436 – 446Combined sources11
Turni447 – 449Combined sources3
Beta strandi450 – 459Combined sources10
Helixi467 – 477Combined sources11
Helixi480 – 482Combined sources3
Beta strandi487 – 489Combined sources3
Helixi503 – 510Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IE0X-ray2.00A/B1-514[»]
5IE2X-ray1.85A/B1-514[»]
5IE3X-ray1.90A/B1-514[»]
ProteinModelPortaliQ9SMT7
SMRiQ9SMT7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni241 – 310SBD1By similarityAdd BLAST70
Regioni311 – 374SBD2By similarityAdd BLAST64

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
KOiK22133
OMAiDEFEFYI
OrthoDBiEOG09360906
PhylomeDBiQ9SMT7

Family and domain databases

InterProiView protein in InterPro
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti137G → V in AAM65672 (Ref. 5) Curated1
Sequence conflicti209V → F in AAM65672 (Ref. 5) Curated1

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_114758.5
UniGeneiAt.19806

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry namei4CLLA_ARATH
AccessioniPrimary (citable) accession number: Q9SMT7
Secondary accession number(s): Q8L9Z5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 1, 2000
Last modified: June 20, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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