Reviewed, UniProtKB/Swiss-Prot Q9SI64 (SPE1_ARATH)

Names and origin

Protein names

Recommended name:
    Arginine decarboxylase 1
      Short name=ARGDC 1
      Short name=ADC 1
      Short name=ADC-O
    EC=4.1.1.19

Gene names

Name:	SPE1
Ordered Locus Names:	At2g16500
ORF Names:	F1P15.12

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	702 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Putrescine biosynthesis Spermidine biosynthesis
Ligand	Magnesium Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process Inferred from electronic annotation. Source: InterPro putrescine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to cold Inferred from mutant phenotype. Source: TAIR response to oxidative stress Inferred from expression pattern. Source: TAIR response to salt stress Inferred from mutant phenotype. Source: TAIR seed development Inferred from genetic interaction. Source: TAIR spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	arginine decarboxylase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 702	702	Arginine decarboxylase 1		PRO_0000149946
Regions
	Region	320 – 330	11	Substrate-binding By similarity
Amino acid modifications
	Modified residue	136	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	452	1	S → F in AAB09723. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SI64-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8B9D182B2684BCA0	FASTA	702	76,175
	10 20 30 40 50 60 MPALAFVDTP IDTFSSIFTP SSVSTAVVDG SCHWSPSLSS SLYRIDGWGA PYFAANSSGN 70 80 90 100 110 120 ISVRPHGSNT LPHQDIDLMK VVKKVTDPSG LGLQLPLIVR FPDVLKNRLE CLQSAFDYAI 130 140 150 160 170 180 QSQGYDSHYQ GVYPVKCNQD RFIIEDIVEF GSGFRFGLEA GSKPEILLAM SCLCKGNPEA 190 200 210 220 230 240 FLVCNGFKDS EYISLALFGR KLELNTVIVL EQEEELDLVI DLSQKMNVRP VIGLRAKLRT 250 260 270 280 290 300 KHSGHFGSTS GEKGKFGLTT VQILRVVRKL SQVGMLDCLQ LLHFHIGSQI PSTALLSDGV 310 320 330 340 350 360 AEAAQLYCEL VRLGAHMKVI DIGGGLGIDY DGSKSGESDL SVAYSLEEYA AAVVASVRFV 370 380 390 400 410 420 CDQKSVKHPV ICSESGRAIV SHHSVLIFEA VSAGQQHETP TDHQFMLEGY SEEVRGDYEN 430 440 450 460 470 480 LYGAAMRGDR ESCLLYVDQL KQRCVEGFKE GSLGIEQLAG VDGLCEWVIK AIGASDPVLT 490 500 510 520 530 540 YHVNLSVFTS IPDFWGIDQL FPIVPIHKLD QRPAARGILS DLTCDSDGKI NKFIGGESSL 550 560 570 580 590 600 PLHEMDNNGC SGGRYYLGMF LGGAYEEALG GVHNLFGGPS VVRVLQSDGP HGFAVTRAVM 610 620 630 640 650 660 GQSSADVLRA MQHEPELMFQ TLKHRAEEPR NNNNKACGDK GNDKLVVASC LAKSFNNMPY 670 680 690 700 LSMETSTNAL TAAVNNLGVY YCDEAAAGGG GKGKDENWSY FG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of Arabidopsis thaliana (L.) Heynh Arginine decarboxylase by potassium deficiency stress." Watson M.B., Malmberg R.L. Plant Physiol. 111:1077-1083(1996) [PubMed: 8756495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [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. , 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
EMBL GenBank DDBJ	U52851 mRNA. Translation: AAB09723.1. AC007195 Genomic DNA. Translation: AAD26494.1. BT008636 mRNA. Translation: AAP40453.1.
IPI	IPI00543375.
PIR	A84541. S71239.
RefSeq	NP_179243.1.
UniGene	At.10173
3D structure databases
SMR	Q9SI64. Positions 69-616.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SI64.
Genome annotation databases
GeneID	816149.
GenomeReviews	Gene locus AT2G16500 in contig CT485783_GR.
KEGG	ath:AT2G16500.
NMPDR	fig|3702.1.peg.8640.
Organism-specific databases
TAIR	At2g16500.
Phylogenomic databases
eggNOG	COG1166.
HOGENOM	HBG321436.
InParanoid	Q9SI64.
PhylomeDB	Q9SI64.
Enzyme and pathway databases
BRENDA	4.1.1.19. 302.
Gene expression databases
ArrayExpress	Q9SI64.
Genevestigator	Q9SI64.
GermOnline	AT2G16500. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002985. Arg_decrbxlase. IPR000183. De-COase2. [Graphical view]
PANTHER	PTHR11482:SF3. Arg_decrbxlase. 1 hit.
Pfam	PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view]
PIRSF	PIRSF001336. Arg_decrbxlase. 1 hit.
PRINTS	PR01180. ARGDCRBXLASE. PR01179. ODADCRBXLASE.
TIGRFAMs	TIGR01273. speA. 1 hit.
PROSITE	PS00878. ODR_DC_2_1. 1 hit. PS00879. ODR_DC_2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPE1_ARATH

Accession

Primary (citable) accession number: Q9SI64
Secondary accession number(s): Q38938

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)