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B4THH1 (SPEA_SALHS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:SeHA_C3325
OrganismSalmonella heidelberg (strain SL476) [Complete proteome] [HAMAP]
Taxonomic identifier454169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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-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

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. 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 – 632632Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000145600

Regions

Region281 – 29111Substrate-binding Potential

Amino acid modifications

Modified residue1011N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B4THH1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 98BB424D2BC97370

FASTA63271,163
        10         20         30         40         50         60 
MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAKLV KAREAQGQRL 

        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 
LEEAERLNVV PRLGVRARLA SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LRDAGRLDSL 

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

       310        320        330        340        350        360 
SVNYGLNEYA NNIIWAIGDA CEEHGLPHPT VITESGRAVT AHHTVLVSNI IGVERNEYTD 

       370        380        390        400        410        420 
PTAPAEDAPR ALQNLWETWQ EMHKPGTRRS LREWLHDSQM DLHDIHIGYS SGAFSLQERA 

       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 PKTLLTHFRD 

       610        620        630 
QVKQTDLDDA LQQQFLEEFE AGLYGYTYLE DE 

« Hide

References

[1]"Complete genome of Salmonella heidelberg strain SL476."
Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SL476.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001120 Genomic DNA. Translation: ACF69056.1.

3D structure databases

ProteinModelPortalB4THH1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING454169.SeHA_C3325.

Proteomic databases

PRIDEB4THH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF69056; ACF69056; SeHA_C3325.
PATRIC18514188. VBISalEnt43179_3173.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
OMAMIHFHIG.
OrthoDBEOG676Z0R.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycSENT454169:GHYG-3303-MONOMER.
UniPathwayUPA00186; UER00284.

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_SALHS
AccessionPrimary (citable) accession number: B4THH1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 41 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

PATHWAY comments

Index of metabolic and biosynthesis pathways