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B5YQD6 (SPEA_ECO5E) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:ECH74115_4241
OrganismEscherichia coli O157:H7 (strain EC4115 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier444450 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

L-arginine = agmatine + CO2. HAMAP MF_01417

Cofactor

Magnesium By similarity. HAMAP MF_01417

Pyridoxal phosphate By similarity. HAMAP MF_01417

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP 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 – 632632Biosynthetic arginine decarboxylase HAMAP MF_01417
PRO_1000145592

Regions

Region281 – 29111Substrate-binding Potential

Amino acid modifications

Modified residue1011N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B5YQD6 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: EE36CC59AF9D2569

FASTA63271,181
        10         20         30         40         50         60 
MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAQLV KTREAQGQRL 

        70         80         90        100        110        120 
PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI KVNQHRRVIE SLIHSGEPLG 

       130        140        150        160        170        180 
LEAGSKAELM AVLAHAGMTR SVIVCNGYKD REYIRLALIG EKMGHKVYLV IEKMSEIAIV 

       190        200        210        220        230        240 
LDEAERLNVV PRLGVRARLA SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LREAGRLDSL 

       250        260        270        280        290        300 
QLLHFHLGSQ MANIRDIATG VRESARFYVE LHKLGVNIQC FDVGGGLGVD YEGTRSQSDC 

       310        320        330        340        350        360 
SVNYGLNEYA NNIIWAIGDA CEENGLPHPT VITESGRAVT AHHTVLVSNI IGVERNEYTV 

       370        380        390        400        410        420 
PTAPAEDAPR ALQSMWETWQ EMHEPGTRRS LREWLHDSQM DLHDIHIGYS SGTFSLQERA 

       430        440        450        460        470        480 
WAEQLYLSMC HEVQKQLDPQ NRAHRPIIDE LQERMADKMY VNFSLFQSMP DAWGIDQLFP 

       490        500        510        520        530        540 
VLPLEGLDQV PERRAVLLDI TCDSDGAIDH YIDGDGIATT MPMPEYDPEN PPMLGFFMVG 

       550        560        570        580        590        600 
AYQEILGNMH NLFGDTEAVD VFVFPDGSVE VELSDEGDTV ADMLQYVQLD PKTLLTQFRD 

       610        620        630 
QVKKTDLDAE LQQQFLEEFE AGLYGYTYLE DE

« Hide

References

[1]"Complete genome sequence of Escherichia coli O157:H7 str. EC4115."
Eppinger M., Sebastian Y., Ravel J.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EC4115 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001164 Genomic DNA. Translation: ACI37609.1.
RefSeqYP_002272418.1. NC_011353.1.

3D structure databases

ProteinModelPortalB5YQD6.
ModBaseSearch...

Protein-protein interaction databases

STRINGB5YQD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000032051; EBESCP00000030754; EBESCG00000031101.
GeneID6968274.
GenomeReviewsGene locus ECH74115_4241 in contig CP001164_GR.
KEGGecf:ECH74115_4241.
PATRIC18369065. VBIEscCol74651_4159.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009574.
HOGENOMHBG321436.
OMALICNGYK.
ProtClustDBPRK05354.

Family and domain databases

HAMAPMF_01417. SpeA.
[Tree]
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]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits.
KOK01585.
PANTHERPTHR11482:SF3. Arg_decrbxlase. 1 hit.
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. Racem_decarbox_C. 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_ECO5E
AccessionPrimary (citable) accession number: B5YQD6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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