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Protein

Arginine decarboxylase

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript 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-14984.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Short name:
ARGDC
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 728728Arginine decarboxylasePRO_0000149953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611N6-(pyridoxal phosphate)lysineBy similarity

Structurei

3D structure databases

ProteinModelPortaliQ43075.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni345 – 35511Substrate-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]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q43075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPALTCFVDG AAALLHPPGY ALAGDFTLPL PFTFSAAATI TDDADATAVE
60 70 80 90 100
DSNSIWSPSL SSKLFRIDGW GFPYFGVNAA GDISVRPHGS ATMSHQEIDL
110 120 130 140 150
LKVVKKASDP KCCGGLGLQL PLVVRFPDVL KDRLESIHAA FDGAIQLQGY
160 170 180 190 200
ESHYQGVYPV KCNQDRYIVE DIVEFGSSFR FGLEAGSKPE LLLAMSCLCK
210 220 230 240 250
GNREAFLVCN GFKDSEYISL ALIARKLALN TVIVLEQEEE LDMVVEISNK
260 270 280 290 300
LCIRPVIGVR AKLKTKHSGH FGATSGDKGK FGLTTIQILH VVKKLEQLDM
310 320 330 340 350
LDCLQLLHFH IGSQIPTTEL LADGVREASQ IYCELLRLGA QMKVLDIGGG
360 370 380 390 400
LGIDYDGSKS GDSDESVAYG LEEYAAAVVH AVKYVCDRKN VKHPVICSES
410 420 430 440 450
GRAIVSHHSI LIFEASGAST NTAPSLSSIE LQYLGEGLSE EALADYQNIS
460 470 480 490 500
AATLRGEYEA CLLYTEQFKK RCVEEFKQGT LGIEQLAAVD GLCDLITETI
510 520 530 540 550
GVKDPVKKYH VNLSVFTSVP DFWGINQLFP IVPIHRLDEK PTARGILSDL
560 570 580 590 600
TCDSDGKIDK FIGGESSLPL HEMEGHGGGY YLGMFLGGSY EEALGGLHNL
610 620 630 640 650
FGGPSVVRVL QSDGPHGFAV TRAVAGSSCA DVLRVMQHEP QLMFETLKHR
660 670 680 690 700
ALEFCGQHDD DSVVNAGVLA NSLAQSFDNM PYLVSSTTCC LNALTNNNGF
710 720
YYCSGDDFSA DTVSVATSVA GEDENWSY
Length:728
Mass (Da):78,710
Last modified:November 1, 1996 - v1
Checksum:i4193A30AEAD8EC4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37540 mRNA. Translation: CAA85773.1.
PIRiS59553.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37540 mRNA. Translation: CAA85773.1.
PIRiS59553.

3D structure databases

ProteinModelPortaliQ43075.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciMetaCyc:MONOMER-14984.

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.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Expression of arginine decarboxylase is induced during early fruit development and in young tissues of Pisum sativum (L.)."
    Perez-Amador M.A., Carbonell J., Granell A.
    Plant Mol. Biol. 28:997-1009(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiSPE1_PEA
AccessioniPrimary (citable) accession number: Q43075
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.