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O23141

- SPE2_ARATH

UniProt

O23141 - SPE2_ARATH

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Protein

Arginine decarboxylase 2

Gene

SPE2

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

Functioni

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

GO - Molecular functioni

  1. arginine decarboxylase activity Source: TAIR

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. polyamine biosynthetic process Source: TAIR
  3. putrescine biosynthetic process Source: TAIR
  4. response to abscisic acid Source: TAIR
  5. response to cold Source: TAIR
  6. response to jasmonic acid Source: TAIR
  7. response to karrikin Source: TAIR
  8. response to osmotic stress Source: TAIR
  9. response to oxidative stress Source: TAIR
  10. response to salt stress Source: TAIR
  11. response to wounding Source: TAIR
  12. seed development Source: TAIR
  13. spermidine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:AT4G34710-MONOMER.
ARA:GQT-1021-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase 2 (EC:4.1.1.19)
Short name:
ADC 2
Short name:
ARGDC 2
Alternative name(s):
ADC-N
Gene namesi
Name:SPE2
Ordered Locus Names:At4g34710
ORF Names:T4L20.290
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G34710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 711711Arginine decarboxylase 2PRO_0000149947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiO23141.
PRIDEiO23141.

Expressioni

Gene expression databases

ExpressionAtlasiO23141. baseline and differential.
GenevestigatoriO23141.

Interactioni

Protein-protein interaction databases

BioGridi14905. 1 interaction.
IntActiO23141. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO23141.
SMRiO23141. Positions 51-640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 34111Substrate-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiO23141.
KOiK01583.
OMAiDSEDMVE.
PhylomeDBiO23141.

Family and domain databases

Gene3Di3.20.20.10. 1 hit.
InterProiIPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O23141-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPALACVDTS FVPPAYAFSD TAGDVFIPAS SPTSAAVVVD RWSPSLSSSL
60 70 80 90 100
YRIDGWGAPY FIANSSGNIS VRPHGSETLP HQDIDLLKIV KKVTGPKSSG
110 120 130 140 150
GLGLQLPLIV RFPDVLKNRL ECLQSAFDYA IKSQGYDSHY QGVYPVKCNQ
160 170 180 190 200
DRFVVEDIVK FGSSFRFGLE AGSKPEILLA MSCLCKGSPD AFLVCNGFKD
210 220 230 240 250
AEYISLALLG RKLALNTVIV LEQEEELDLV IELSQKMNVR PVIGLRAKLR
260 270 280 290 300
TKHSGHFGST SGEKGKFGLT TTQIVRVVRK LRQSGMLDCL QLLHFHIGSQ
310 320 330 340 350
IPSTSLLSDG VAEAAQLYCE LVRLGAHMKV IDIGGGLGID YDGSKSGESD
360 370 380 390 400
LSVAYSLEEY AEAVVASVRV VCDRSSVKHP VICSESGRAI VSHHSVLIFE
410 420 430 440 450
AVSADKPMVH QATPGDIQFL LEGNEEARAN YEDLYAAVMR GDHESCLLYV
460 470 480 490 500
DQLKQRCVEG FKEGVLSIEQ LASVDGLCEW VLKAIGASDP VHTYNINLSV
510 520 530 540 550
FTSIPDLWGI DQLFPIVPIH KLDQRPGARG ILSDLTCDSD GKINKFIGGE
560 570 580 590 600
SSLPLHELDK NGSGGRYFLG MFLGGAYEEA LGGVHNLFGG PSVVRVSQSD
610 620 630 640 650
GPHSFAVTRA VPGQSSADVL RAMQHEPELM FQTLKHRAEE MMHTKGGSEG
660 670 680 690 700
ENEEEEEDDE FNNVAASLDR SFHNMPYLAT EQASPSNSLS AAISNLGFYY
710
CDEDVYDYIS A
Length:711
Mass (Da):77,219
Last modified:January 1, 1998 - v1
Checksum:i8E003877173DEEE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009647 mRNA. Translation: AAB72179.1.
AL023094 Genomic DNA. Translation: CAA18850.1.
AL161586 Genomic DNA. Translation: CAB80188.1.
CP002687 Genomic DNA. Translation: AEE86413.1.
CP002687 Genomic DNA. Translation: AEE86414.1.
AY039581 mRNA. Translation: AAK62636.1.
AY093982 mRNA. Translation: AAM16243.1.
PIRiT05291.
RefSeqiNP_195197.1. NM_119637.2.
NP_974684.1. NM_202955.1.
UniGeneiAt.2313.
At.43941.

Genome annotation databases

EnsemblPlantsiAT4G34710.1; AT4G34710.1; AT4G34710.
AT4G34710.2; AT4G34710.2; AT4G34710.
GeneIDi829623.
KEGGiath:AT4G34710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009647 mRNA. Translation: AAB72179.1 .
AL023094 Genomic DNA. Translation: CAA18850.1 .
AL161586 Genomic DNA. Translation: CAB80188.1 .
CP002687 Genomic DNA. Translation: AEE86413.1 .
CP002687 Genomic DNA. Translation: AEE86414.1 .
AY039581 mRNA. Translation: AAK62636.1 .
AY093982 mRNA. Translation: AAM16243.1 .
PIRi T05291.
RefSeqi NP_195197.1. NM_119637.2.
NP_974684.1. NM_202955.1.
UniGenei At.2313.
At.43941.

3D structure databases

ProteinModelPortali O23141.
SMRi O23141. Positions 51-640.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 14905. 1 interaction.
IntActi O23141. 1 interaction.

Proteomic databases

PaxDbi O23141.
PRIDEi O23141.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G34710.1 ; AT4G34710.1 ; AT4G34710 .
AT4G34710.2 ; AT4G34710.2 ; AT4G34710 .
GeneIDi 829623.
KEGGi ath:AT4G34710.

Organism-specific databases

TAIRi AT4G34710.

Phylogenomic databases

eggNOGi COG1166.
HOGENOMi HOG000029191.
InParanoidi O23141.
KOi K01583.
OMAi DSEDMVE.
PhylomeDBi O23141.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci ARA:AT4G34710-MONOMER.
ARA:GQT-1021-MONOMER.

Gene expression databases

ExpressionAtlasi O23141. baseline and differential.
Genevestigatori O23141.

Family and domain databases

Gene3Di 3.20.20.10. 1 hit.
InterProi IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view ]
Pfami PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view ]
PIRSFi PIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSi PR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMi SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR01273. speA. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a second arginine decarboxylase cDNA from Arabidopsis."
    Watson M.B., Yu W., Galloway G., Malmberg R.L.
    Plant Gene Register PGR97-114
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [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.

Entry informationi

Entry nameiSPE2_ARATH
AccessioniPrimary (citable) accession number: O23141
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 125 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3