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Q9HUX1 (SPEA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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:PA4839
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length636 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 – 636636Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149971

Regions

Region290 – 30011Substrate-binding Potential

Amino acid modifications

Modified residue1101N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HUX1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E7274FD432E0D187

FASTA63670,668
        10         20         30         40         50         60 
MAARRTRKDD GSNWTVADSR GVYGIRHWGA GYFAINDGGN VEVRPQGADS TPIDLYELVG 

        70         80         90        100        110        120 
QLREAGLSLP LLVRFPDILQ DRVRKLTGAF DANIERLEYQ SRYTALYPIK VNQQEAVVEN 

       130        140        150        160        170        180 
IIATENVSIG LEAGSKPELM AVLALAPKGG TIVCNGYKDR EFIKLALMGQ KLGHNVFIVI 

       190        200        210        220        230        240 
EKESEVQLVI EEAANVGVQP QVGLRVRLSS LASSKWADTG GEKAKFGLSA AQLLSVVERF 

       250        260        270        280        290        300 
RQAGLDQGVR LLHFHMGSQI ANLADYQHGF KEAIRYYGEL RALGLPVDHI DVGGGLGVDY 

       310        320        330        340        350        360 
DGTHSRNASS INYDIDDYAG VVVGMLKEFC DAQGLPHPHI FSESGRALTA HHAVLITQVT 

       370        380        390        400        410        420 
DVERHNDDVP KIVDLDEQPE IVRWLAELLG PTDAEMVTET YWRATHYIGD AAAQYADGKI 

       430        440        450        460        470        480 
SLAQKALAEQ CYFAICRRLH NQLKARQRSH RQVLDELNDK LADKYICNFS VFQSLPDTWA 

       490        500        510        520        530        540 
IGQVLPILPL HRLGEEPDRR AVLQDLTCDS DGKITQYVDE QSIETSLPVH EVKEGEDYLI 

       550        560        570        580        590        600 
GVFLVGAYQE ILGDMHNLFG DTDSVNVYQR ADGGIYHAGI ETHDTIEDML RYVHLSPEEL 

       610        620        630 
MTLYRDKVAG AKLTARERNQ YLDALRLGLT RSAYLS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG08224.1.
PIRH83040.
RefSeqNP_253526.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9HUX1.
SMRQ9HUX1. Positions 20-635.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA4839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID879594.
KEGGpae:PA4839.
PATRIC19844477. VBIPseAer58763_5070.

Organism-specific databases

PseudoCAPPA4839.

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
OrthoDBEOG676Z0R.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
HAMAPMF_01417. SpeA.
InterProIPR009006. 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.
[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.
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_PSEAE
AccessionPrimary (citable) accession number: Q9HUX1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 75 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