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Q32C07 (Q32C07_SHIDS) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
Short name=ADC HAMAP-Rule MF_01417
EC=4.1.1.19 HAMAP-Rule MF_01417
Gene names
Name:speA HAMAP-Rule MF_01417 EMBL ABB63148.1
Ordered Locus Names:SDY_3134 EMBL ABB63148.1
OrganismShigella dysenteriae serotype 1 (strain Sd197) [Reference proteome] [HAMAP] EMBL ABB63148.1
Taxonomic identifier300267 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella ›

Protein attributes

Sequence length658 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 SAAS SAAS022644 RuleBase RU003740

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01417 SAAS SAAS022644 RuleBase RU003740

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01417 SAAS SAAS022644

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. HAMAP-Rule MF_01417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region307 – 31711Substrate-binding By similarity HAMAP-Rule MF_01417

Amino acid modifications

Modified residue1271N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01417

Sequences

Sequence LengthMass (Da)Tools
Q32C07 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 87106BF8727B6EE2

FASTA65873,886
        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 IHIGYSSGTF 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

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References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sd197 EMBL ABB63148.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000034 Genomic DNA. Translation: ABB63148.1.
RefSeqYP_404639.1. NC_007606.1.

3D structure databases

ProteinModelPortalQ32C07.
ModBaseSearch...

Protein-protein interaction databases

STRING300267.SDY_3134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB63148; ABB63148; SDY_3134.
GeneID3799012.
KEGGsdy:SDY_3134.
PATRIC18696682. VBIShiDys99784_3743.

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycSDYS300267:GJEW-3130-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]
PANTHERPTHR11482:SF3. PTHR11482:SF3. 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 nameQ32C07_SHIDS
AccessionPrimary (citable) accession number: Q32C07
Entry history
Integrated into UniProtKB/TrEMBL: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info