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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation
  • pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciDRAD243230:GH46-249-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
Short name:
ADCUniRule annotation
Gene namesi
Name:speAUniRule annotation
Ordered Locus Names:DR_0243
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 662662Biosynthetic arginine decarboxylasePRO_0000149959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiQ9RXR4.

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_0243.

Structurei

3D structure databases

ProteinModelPortaliQ9RXR4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni308 – 31811Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiQ9RXR4.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
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]
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.

Q9RXR4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCPARLRTPR TASLPTHRRS AMTTANPLNT SFTSADAAEL YQVPNWSGGW
60 70 80 90 100
FRVSDKGLME ATPAPGLHAS LRAIVDEIVD RGESLPVILR FPQVLAGRVK
110 120 130 140 150
HLNEAFQAAI NEYNYSGHYQ GVFPIKVNQR RAVVETVAAA GYDYAHGLEA
160 170 180 190 200
GSKAELALCL AQKMHPDALL CCNGFKDDGF IKLALWGRTL GKNVVITIEK
210 220 230 240 250
FTELDRILKQ AKALGVKPAV GVRFKLHARG SGQWEESGGD QAKFGLNAYE
260 270 280 290 300
LLRVVERLKE ENMLDSLVML HTHIGSQITD IRRVKVAVRE AAQTYAGLIA
310 320 330 340 350
AGADLKYLNV GGGLGVDYDG SKTTFYASMN YTVKEYAADI VYTVQEVCKA
360 370 380 390 400
REVPEPVIVS ESGRALTAHH AVLILPVVDV TGPTRNLEDQ ELTVPGEDSH
410 420 430 440 450
QIVRDMYETL ENISMRNYRE SYNDAVGDKQ TLHNLFDLGY VTLEDRARGE
460 470 480 490 500
ALFNAILRKI AKLIQGEKYV PDELEDLQKV LADKFICNFS LFQSLPDNWA
510 520 530 540 550
IGALFPIVPL DRLNEQPTRQ ATLVDITCDS DGKVEKFIDL RDVKATLPLH
560 570 580 590 600
EPGDRPYYLG AFLMGAYQDV LGSAHNLFGK VSEAHVTVRP GGRFNIDLFV
610 620 630 640 650
RGQKARRMIE SMGYEEPMLR DAIEDQADAA IGRGTLTQEQ EHELLEDYGE
660
ELLGYTYLEY ES
Length:662
Mass (Da):73,528
Last modified:May 1, 2000 - v1
Checksum:i88DDA5636BD83E6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09826.1.
PIRiB75544.
RefSeqiNP_293967.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF09826; AAF09826; DR_0243.
GeneIDi1799241.
KEGGidra:DR_0243.
PATRICi21627969. VBIDeiRad64572_0407.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09826.1.
PIRiB75544.
RefSeqiNP_293967.1. NC_001263.1.

3D structure databases

ProteinModelPortaliQ9RXR4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0243.

Proteomic databases

PRIDEiQ9RXR4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF09826; AAF09826; DR_0243.
GeneIDi1799241.
KEGGidra:DR_0243.
PATRICi21627969. VBIDeiRad64572_0407.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiQ9RXR4.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-249-MONOMER.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
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]
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiSPEA_DEIRA
AccessioniPrimary (citable) accession number: Q9RXR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.