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P22220

- SPE1_AVESA

UniProt

P22220 - SPE1_AVESA

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Protein
Arginine decarboxylase
Gene
SPE1
Organism
Avena sativa (Oat)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Pyridoxal phosphate.
Magnesium.

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.
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 decarboxylase
PRO_0000149948Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiP22220.

Structurei

3D structure databases

ProteinModelPortaliP22220.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 30011Substrate-binding By similarity
Add
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]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
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

MAKNYGDVYH VEGWGEPYFA VNKDGHLCVR IYGRETLPGQ EIDVLSVIEQ    50
ATSADGTGKK LQFPMILRFP DVLRHRINSL HTAFANAIKY TQYGSVYQGV 100
FPVKVNQHKD VVQDMVHFGY DHSYGLEAGS KPELLIAMSC LTKAKPGAYL 150
VCNGYKDSAY VALALAARAM GLNVIIVLEM EEELDIVIEE SSKLGVEPVI 200
GVRAKLLTKI PGHFGSTAGK HGKFGLPAEK IYEVAKKLKA LNKLHWLKLL 250
HFHVGSMIPT TDIVFKAASE ASDIYCALVK EYGVETMTTL DCGGGLGVDY 300
DGTRSGSSDM SVAYGLEEYA SSIVQAVRLK CDYHGVPHPV LCTESGRAMA 350
SYHSMIILEA LSAIPEPKDD EDEATTEQLH GRIRDLSSKL QPTGLSMSSH 400
AVHIKKHGIE MYKLGKKLSK SVTTDAHTIY NYHMNLSVFS LMPDYWGIQH 450
LFPMMPVSRL DEKPTHKATL VDVTCDSDGK VDKFIRDTET MPLHPLDPKL 500
GGYYVAVLLT GAYQEALSNK HNLFGGPSLV RVVGTGNGGA FNVEAALLGS 550
TTEELIGTVS YDVKQDISSV IEERARENKV WEMVEKLVES GLHTMPYLAD 600
YKPPPMA 607
Length:607
Mass (Da):66,706
Last modified:August 1, 1991 - v1
Checksum:i757114B2C02EF8A5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56802 mRNA. Translation: CAA40137.1.
PIRiS12265.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56802 mRNA. Translation: CAA40137.1 .
PIRi S12265.

3D structure databases

ProteinModelPortali P22220.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P22220.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P22220.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci MetaCyc:MONOMER-14981.

Family and domain databases

Gene3Di 2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProi IPR009006. 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 ]
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 SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1990) [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: June 11, 2014
This is version 77 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

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