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Q9RXR4 (SPEA_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:DR_0243
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP-Rule MF_01417

Catalytic activity

L-arginine = agmatine + CO2. HAMAP-Rule MF_01417

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01417

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01417

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149959

Regions

Region308 – 31811Substrate-binding Potential

Amino acid modifications

Modified residue1261N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RXR4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 88DDA5636BD83E6A

FASTA66273,528
        10         20         30         40         50         60 
MCPARLRTPR TASLPTHRRS AMTTANPLNT SFTSADAAEL YQVPNWSGGW FRVSDKGLME 

        70         80         90        100        110        120 
ATPAPGLHAS LRAIVDEIVD RGESLPVILR FPQVLAGRVK HLNEAFQAAI NEYNYSGHYQ 

       130        140        150        160        170        180 
GVFPIKVNQR RAVVETVAAA GYDYAHGLEA GSKAELALCL AQKMHPDALL CCNGFKDDGF 

       190        200        210        220        230        240 
IKLALWGRTL GKNVVITIEK FTELDRILKQ AKALGVKPAV GVRFKLHARG SGQWEESGGD 

       250        260        270        280        290        300 
QAKFGLNAYE LLRVVERLKE ENMLDSLVML HTHIGSQITD IRRVKVAVRE AAQTYAGLIA 

       310        320        330        340        350        360 
AGADLKYLNV GGGLGVDYDG SKTTFYASMN YTVKEYAADI VYTVQEVCKA REVPEPVIVS 

       370        380        390        400        410        420 
ESGRALTAHH AVLILPVVDV TGPTRNLEDQ ELTVPGEDSH QIVRDMYETL ENISMRNYRE 

       430        440        450        460        470        480 
SYNDAVGDKQ TLHNLFDLGY VTLEDRARGE ALFNAILRKI AKLIQGEKYV PDELEDLQKV 

       490        500        510        520        530        540 
LADKFICNFS LFQSLPDNWA IGALFPIVPL DRLNEQPTRQ ATLVDITCDS DGKVEKFIDL 

       550        560        570        580        590        600 
RDVKATLPLH EPGDRPYYLG AFLMGAYQDV LGSAHNLFGK VSEAHVTVRP GGRFNIDLFV 

       610        620        630        640        650        660 
RGQKARRMIE SMGYEEPMLR DAIEDQADAA IGRGTLTQEQ EHELLEDYGE ELLGYTYLEY 


ES 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF09826.1.
PIRB75544.
RefSeqNP_293967.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RXR4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_0243.

Proteomic databases

PRIDEQ9RXR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF09826; AAF09826; DR_0243.
GeneID1799241.
KEGGdra:DR_0243.
PATRIC21627969. VBIDeiRad64572_0407.

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAIDHYVDG.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycDRAD243230:GH46-249-MONOMER.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPMF_01417. SpeA.
InterProIPR009006. 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]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR01273. speA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEA_DEIRA
AccessionPrimary (citable) accession number: Q9RXR4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families