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Reviewed, UniProtKB/Swiss-Prot O23141 (SPE2_ARATH)

Last modified November 3, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginine decarboxylase 2
      Short name=ARGDC 2
      Short name=ADC 2
    EC=4.1.1.19
Alternative name(s):
    ADC-N
Gene names
Name: SPE2
Ordered Locus Names: At4g34710
ORF Names: T4L20.290
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

L-arginine = agmatine + CO2.

Cofactor

Pyridoxal phosphate.

Magnesium.

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 711711Arginine decarboxylase 2
PRO_0000149947

Regions

Region331 – 34111Substrate-binding By similarity

Amino acid modifications

Modified residue1471N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O23141-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8E003877173DEEE5

FASTA71177,219
        10         20         30         40         50         60 
MPALACVDTS FVPPAYAFSD TAGDVFIPAS SPTSAAVVVD RWSPSLSSSL YRIDGWGAPY 

        70         80         90        100        110        120 
FIANSSGNIS VRPHGSETLP HQDIDLLKIV KKVTGPKSSG GLGLQLPLIV RFPDVLKNRL 

       130        140        150        160        170        180 
ECLQSAFDYA IKSQGYDSHY QGVYPVKCNQ DRFVVEDIVK FGSSFRFGLE AGSKPEILLA 

       190        200        210        220        230        240 
MSCLCKGSPD AFLVCNGFKD AEYISLALLG RKLALNTVIV LEQEEELDLV IELSQKMNVR 

       250        260        270        280        290        300 
PVIGLRAKLR TKHSGHFGST SGEKGKFGLT TTQIVRVVRK LRQSGMLDCL QLLHFHIGSQ 

       310        320        330        340        350        360 
IPSTSLLSDG VAEAAQLYCE LVRLGAHMKV IDIGGGLGID YDGSKSGESD LSVAYSLEEY 

       370        380        390        400        410        420 
AEAVVASVRV VCDRSSVKHP VICSESGRAI VSHHSVLIFE AVSADKPMVH QATPGDIQFL 

       430        440        450        460        470        480 
LEGNEEARAN YEDLYAAVMR GDHESCLLYV DQLKQRCVEG FKEGVLSIEQ LASVDGLCEW 

       490        500        510        520        530        540 
VLKAIGASDP VHTYNINLSV FTSIPDLWGI DQLFPIVPIH KLDQRPGARG ILSDLTCDSD 

       550        560        570        580        590        600 
GKINKFIGGE SSLPLHELDK NGSGGRYFLG MFLGGAYEEA LGGVHNLFGG PSVVRVSQSD 

       610        620        630        640        650        660 
GPHSFAVTRA VPGQSSADVL RAMQHEPELM FQTLKHRAEE MMHTKGGSEG ENEEEEEDDE 

       670        680        690        700        710 
FNNVAASLDR SFHNMPYLAT EQASPSNSLS AAISNLGFYY CDEDVYDYIS A 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF009647 mRNA. Translation: AAB72179.1.
AL023094 Genomic DNA. Translation: CAA18850.1.
AL161586 Genomic DNA. Translation: CAB80188.1.
AY039581 mRNA. Translation: AAK62636.1.
AY093982 mRNA. Translation: AAM16243.1.
IPIIPI00547586.
PIRT05291.
RefSeqNP_195197.1.
NP_974684.1.
UniGeneAt.2313
At.43941

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO23141.

Proteomic databases

PRIDEO23141.

Genome annotation databases

GeneID829623.
GenomeReviewsGene locus AT4G34710 in contig CT486007_GR.
KEGGath:AT4G34710.
NMPDRfig|3702.1.peg.21544.

Organism-specific databases

TAIRAt4g34710.

Phylogenomic databases

OMAARANREY.

Enzyme and pathway databases

BRENDA4.1.1.19. 302.

Gene expression databases

GenevestigatorO23141.
GermOnlineAT4G34710. Arabidopsis thaliana.

Family and domain databases

InterProIPR002985. Arg_decrbxlase.
IPR000183. De-COase2.
[Graphical view]
PANTHERPTHR11482:SF3. Arg_decrbxlase. 1 hit.
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
TIGRFAMsTIGR01273. speA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPE2_ARATH
AccessionPrimary (citable) accession number: O23141
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents