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Protein

Arginine decarboxylase

Gene

SPE1

Organism
Avena sativa (Oat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. putrescine biosynthetic process Source: UniProtKB-KW
  3. 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

BioCyciMetaCyc:MONOMER-14981.
BRENDAi4.1.1.19. 588.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Short name:
ARGDC
Gene namesi
Name:SPE1
OrganismiAvena sativa (Oat)
Taxonomic identifieri4498 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaePoeaeAveninaeAvena

Organism-specific databases

GrameneiP22220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Arginine decarboxylasePRO_0000149948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP22220.

Structurei

3D structure databases

ProteinModelPortaliP22220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 30011Substrate-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProiIPR009006. 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]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22220-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKNYGDVYH VEGWGEPYFA VNKDGHLCVR IYGRETLPGQ EIDVLSVIEQ
60 70 80 90 100
ATSADGTGKK LQFPMILRFP DVLRHRINSL HTAFANAIKY TQYGSVYQGV
110 120 130 140 150
FPVKVNQHKD VVQDMVHFGY DHSYGLEAGS KPELLIAMSC LTKAKPGAYL
160 170 180 190 200
VCNGYKDSAY VALALAARAM GLNVIIVLEM EEELDIVIEE SSKLGVEPVI
210 220 230 240 250
GVRAKLLTKI PGHFGSTAGK HGKFGLPAEK IYEVAKKLKA LNKLHWLKLL
260 270 280 290 300
HFHVGSMIPT TDIVFKAASE ASDIYCALVK EYGVETMTTL DCGGGLGVDY
310 320 330 340 350
DGTRSGSSDM SVAYGLEEYA SSIVQAVRLK CDYHGVPHPV LCTESGRAMA
360 370 380 390 400
SYHSMIILEA LSAIPEPKDD EDEATTEQLH GRIRDLSSKL QPTGLSMSSH
410 420 430 440 450
AVHIKKHGIE MYKLGKKLSK SVTTDAHTIY NYHMNLSVFS LMPDYWGIQH
460 470 480 490 500
LFPMMPVSRL DEKPTHKATL VDVTCDSDGK VDKFIRDTET MPLHPLDPKL
510 520 530 540 550
GGYYVAVLLT GAYQEALSNK HNLFGGPSLV RVVGTGNGGA FNVEAALLGS
560 570 580 590 600
TTEELIGTVS YDVKQDISSV IEERARENKV WEMVEKLVES GLHTMPYLAD

YKPPPMA
Length:607
Mass (Da):66,706
Last modified:August 1, 1991 - v1
Checksum:i757114B2C02EF8A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56802 mRNA. Translation: CAA40137.1.
PIRiS12265.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56802 mRNA. Translation: CAA40137.1.
PIRiS12265.

3D structure databases

ProteinModelPortaliP22220.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP22220.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP22220.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciMetaCyc:MONOMER-14981.
BRENDAi4.1.1.19. 588.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProiIPR009006. 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]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 427-437.
    Tissue: Leaf.

Entry informationi

Entry nameiSPE1_AVESA
AccessioniPrimary (citable) accession number: P22220
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 1, 2015
This is version 80 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.