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P22220 (SPE1_AVESA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine decarboxylase

Short name=ADC
Short name=ARGDC
EC=4.1.1.19
Gene names
Name:SPE1
OrganismAvena sativa (Oat)
Taxonomic identifier4498 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaePoeaeAveninaeAvena

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 – 607607Arginine decarboxylase
PRO_0000149948

Regions

Region290 – 30011Substrate-binding By similarity

Amino acid modifications

Modified residue1041N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P22220 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 757114B2C02EF8A5

FASTA60766,706
        10         20         30         40         50         60 
MAKNYGDVYH VEGWGEPYFA VNKDGHLCVR IYGRETLPGQ EIDVLSVIEQ ATSADGTGKK 

        70         80         90        100        110        120 
LQFPMILRFP DVLRHRINSL HTAFANAIKY TQYGSVYQGV FPVKVNQHKD VVQDMVHFGY 

       130        140        150        160        170        180 
DHSYGLEAGS KPELLIAMSC LTKAKPGAYL VCNGYKDSAY VALALAARAM GLNVIIVLEM 

       190        200        210        220        230        240 
EEELDIVIEE SSKLGVEPVI GVRAKLLTKI PGHFGSTAGK HGKFGLPAEK IYEVAKKLKA 

       250        260        270        280        290        300 
LNKLHWLKLL HFHVGSMIPT TDIVFKAASE ASDIYCALVK EYGVETMTTL DCGGGLGVDY 

       310        320        330        340        350        360 
DGTRSGSSDM SVAYGLEEYA SSIVQAVRLK CDYHGVPHPV LCTESGRAMA SYHSMIILEA 

       370        380        390        400        410        420 
LSAIPEPKDD EDEATTEQLH GRIRDLSSKL QPTGLSMSSH AVHIKKHGIE MYKLGKKLSK 

       430        440        450        460        470        480 
SVTTDAHTIY NYHMNLSVFS LMPDYWGIQH LFPMMPVSRL DEKPTHKATL VDVTCDSDGK 

       490        500        510        520        530        540 
VDKFIRDTET MPLHPLDPKL GGYYVAVLLT GAYQEALSNK HNLFGGPSLV RVVGTGNGGA 

       550        560        570        580        590        600 
FNVEAALLGS TTEELIGTVS YDVKQDISSV IEERARENKV WEMVEKLVES GLHTMPYLAD 


YKPPPMA 

« Hide

References

[1]"Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing."
Bell E., Malmberg R.L.
Mol. Gen. Genet. 224:431-436(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 427-437.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56802 mRNA. Translation: CAA40137.1.
PIRS12265.

3D structure databases

ProteinModelPortalP22220.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP22220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP22220.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14981.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProIPR009006. Ala_racemase/Decarboxylase_C.
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]
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.
SUPFAMSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPE1_AVESA
AccessionPrimary (citable) accession number: P22220
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways