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O82475

- SPE1_BRAJU

UniProt

O82475 - SPE1_BRAJU

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Protein

Arginine decarboxylase

Gene
ADC1
Organism
Brassica juncea (Indian mustard) (Sinapis juncea)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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

UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Short name:
ARGDC
Gene namesi
Name:ADC1
OrganismiBrassica juncea (Indian mustard) (Sinapis juncea)
Taxonomic identifieri3707 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 702702Arginine decarboxylasePRO_0000149949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei141 – 1411N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

PRIDEiO82475.

Structurei

3D structure databases

ProteinModelPortaliO82475.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni325 – 33511Substrate-binding By 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.

O82475-1 [UniParc]FASTAAdd to Basket

« Hide

MPALALVDTP VDAFSGDCSG VFIPPSPNSS SASLDWSPSL SSSLYRIDGW    50
GAPYFAANSS GNISVRPHGS NTMPHQEIDL TKVVKKATDP KSSGGLALQF 100
PLIVRFPDVL KNRLESLQSA FEFAIQTQGY ESRYQGVYPV KCNQDRFIIE 150
DIVEFGSSFR FGLEAGSKPE ILLAMSCLCK GSPEAFLVCN GFKDAEYVSL 200
ALLGRKLQLN TVIVLEQEEE LDLVIALSKK VNVRPVIGLR AKLRTKHSGH 250
FGSTSGEKGK FGLTTVQIIR VVRKLRDVGM LDCLQLLHFH IGSQIPSTAL 300
LSDGVSEAAQ LYCELVRLGA RMEVIDIGGG LGIDYDGSKS GESDLSVAYS 350
LEEYAAAVVA SVRFVCDQKS VKHPVICSES GRAIVSHHSV LIFEAVSAGK 400
RHETTPSDLQ FLLEGYSEEA RGDYENLYDA VMRGDRESCL LYVDQLKQRC 450
VEEFKEGSLS IEQLAGVDGL CEWVTKEIGG SDPVLTYNVN LSVFHSIPDF 500
WGIDQLFPIV PIHRLDQRPV ARGILSDLTC DSDGKINKFI GGESSLPLHE 550
LDNNGYYLGM FLGGAYEEAL GGVHNLFGGP SVVRVLQKDG PHGFAVTRAM 600
MGQSSADVLR AMQHEPELMF QTLKHRAEEL SLVHKPGGDK GNDKLVASCL 650
ARSFNNMPYL SVGTSTNALT AAINNLVYYS DEAAVGNGGG CGKNGKWSYS 700
VD 702
Length:702
Mass (Da):76,188
Last modified:November 1, 1998 - v1
Checksum:i4FF22C7A8D1B1B92
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077547 mRNA. Translation: AAC62017.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077547 mRNA. Translation: AAC62017.1 .

3D structure databases

ProteinModelPortali O82475.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi O82475.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .

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.
TIGRFAMsi TIGR01273. speA. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of an arginine decarboxylase cDNA from mustard (Brassica juncea [L.] Czern & Coss)."
    Mo H., Pua E.-C.
    Plant Gene Register PGR98-160
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiSPE1_BRAJU
AccessioniPrimary (citable) accession number: O82475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 72 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

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