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P21170 (SPEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:b2938, JW2905
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Pyridoxal phosphate.

Magnesium.

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule MF_01417

Subunit structure

Homotetramer.

Subcellular location

Periplasm Ref.1.

Induction

By growth in an acidic enriched medium containing arginine (biodegradative form), by growth in minimal media at neutral pH (biosynthetic). Putrescine and spermidine repress the speA gene and feedback inhibit ADC. HAMAP-Rule MF_01417

Post-translational modification

Processed post-translationally to a 70 kDa mature form. HAMAP-Rule MF_01417

The N-terminus is blocked. HAMAP-Rule MF_01417

Miscellaneous

ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins.

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 8.4. HAMAP-Rule MF_01417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 658658Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149960

Regions

Region307 – 31711Substrate-binding Potential

Amino acid modifications

Modified residue1271N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict2261A → R in AAA24646. Ref.1

Secondary structure

..................................................................................................... 658
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21170 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: 22613CEA5F957CC3

FASTA65873,898
        10         20         30         40         50         60 
MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD VNELGHISVC 

        70         80         90        100        110        120 
PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL RSINAAFKRA RESYGYNGDY 

       130        140        150        160        170        180 
FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG SKAELMAVLA HAGMTRSVIV CNGYKDREYI 

       190        200        210        220        230        240 
RLALIGEKMG HKVYLVIEKM SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK 

       250        260        270        280        290        300 
SKFGLAATQV LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL 

       310        320        330        340        350        360 
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN GLPHPTVITE 

       370        380        390        400        410        420 
SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS MWETWQEMHE PGTRRSLREW 

       430        440        450        460        470        480 
LHDSQMDLHD IHIGYSSGIF SLQERAWAEQ LYLSMCHEVQ KQLDPQNRAH RPIIDELQER 

       490        500        510        520        530        540 
MADKMYVNFS LFQSMPDAWG IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG 

       550        560        570        580        590        600 
DGIATTMPMP EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS 

       610        620        630        640        650 
DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY GYTYLEDE 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli."
Moore R.C., Boyle S.M.
J. Bacteriol. 172:4631-4640(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli."
Szumanski M.B.W., Boyle S.M.
J. Bacteriol. 174:758-764(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-658.
Strain: K12.
[5]"Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties."
Wu W.H., Morris D.R.
J. Biol. Chem. 248:1687-1695(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: UW 44 / ATCC 27549.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31770 Genomic DNA. Translation: AAA24646.1.
U28377 Genomic DNA. Translation: AAA69105.1.
U00096 Genomic DNA. Translation: AAC75975.1.
AP009048 Genomic DNA. Translation: BAE77001.1.
M32363 Genomic DNA. No translation available.
PIRA65079.
RefSeqNP_417413.1. NC_000913.3.
YP_491137.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NZQX-ray3.10A/B1-658[»]
ProteinModelPortalP21170.
SMRP21170. Positions 34-658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10905N.
IntActP21170. 16 interactions.
STRING511145.b2938.

Proteomic databases

PaxDbP21170.
PRIDEP21170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75975; AAC75975; b2938.
BAE77001; BAE77001; BAE77001.
GeneID12933352.
947432.
KEGGecj:Y75_p2868.
eco:b2938.
PATRIC32121288. VBIEscCol129921_3032.

Organism-specific databases

EchoBASEEB0952.
EcoGeneEG10959. speA.

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
OrthoDBEOG676Z0R.
PhylomeDBP21170.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycEcoCyc:ARGDECARBOXBIO-MONOMER.
ECOL316407:JW2905-MONOMER.
MetaCyc:ARGDECARBOXBIO-MONOMER.
SABIO-RKP21170.
UniPathwayUPA00186; UER00284.

Gene expression databases

GenevestigatorP21170.

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...

Other

EvolutionaryTraceP21170.
PROP21170.

Entry information

Entry nameSPEA_ECOLI
AccessionPrimary (citable) accession number: P21170
Secondary accession number(s): Q2M9Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 29, 2003
Last modified: April 16, 2014
This is version 131 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene