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Protein

Arginine decarboxylase

Gene

SPE2

Organism
Theobroma cacao (Cacao) (Cocoa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: agmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.
Proteins known to be involved in this subpathway in this organism are:
  1. Arginine decarboxylase (TCM_020310), Arginine decarboxylase (SPE2), Arginine decarboxylase (TCM_006773)
This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Short name:
ARGDC
Gene namesi
Name:SPE2
OrganismiTheobroma cacao (Cacao) (Cocoa)
Taxonomic identifieri3641 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMalvalesMalvaceaeByttnerioideaeTheobroma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000149955‹1 – ›406Arginine decarboxylaseAdd BLAST›406

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8N6-(pyridoxal phosphate)lysineBy similarity1

Structurei

3D structure databases

ProteinModelPortaliO81160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 202Substrate-bindingBy similarityAdd BLAST11

Sequence similaritiesi

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O81160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
YQGVYPVKSN QDRFVVEDIV KFGSSFRFGL EAGSKPELLL AMSCLCKGNP
60 70 80 90 100
EALLVCNGFK DAEYISLALL ARKLALKHVI VLEQEEEVDM VIDISQKLSV
110 120 130 140 150
RPVIGVRAKL RTKHSGHFGS TSGEKGKFGL TTTQVLRVVK KLQDSGMLDC
160 170 180 190 200
LQLLHFHIGS QIPSTALLSD GVGEAAQIYS ELVRLGARMK VVDFGGGLGI
210 220 230 240 250
DYNGSKSGDS DLSVPYGLQE YAHVVNAIRF VCDRKSVKHP VICSESGRAI
260 270 280 290 300
VSHHSILIFE AICLTAPATH NEPINIPFIM EGLSEDACAD YWNLRDTAMR
310 320 330 340 350
TGDGAFWFYA DQWKQRCVEQ FKEGTLGIEQ LASVDGLCEW VLKAIGASDP
360 370 380 390 400
VHTYNINLSV FTSIPDLWGI DQLFPIVPIH KLDQRPGARG ILSDLTCDSD

GKINKF
Length:406
Mass (Da):44,604
Last modified:November 1, 1998 - v1
Checksum:iA736338EE8ADD4D6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei4061

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045666 Genomic DNA. Translation: AAC68511.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045666 Genomic DNA. Translation: AAC68511.1.

3D structure databases

ProteinModelPortaliO81160.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPE2_THECC
AccessioniPrimary (citable) accession number: O81160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 71 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

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 one 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.