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A1AS90 (SPEA_PELPD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 51. 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:Ppro_2606
OrganismPelobacter propionicus (strain DSM 2379) [Complete proteome] [HAMAP]
Taxonomic identifier338966 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length635 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 – 635635Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000068492

Regions

Region282 – 29211Substrate-binding Potential

Amino acid modifications

Modified residue1001N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AS90 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: A1A77BF7734E5614

FASTA63571,801
        10         20         30         40         50         60 
MERWSINDSA KIYNLNNWGG DLFSINKKGN ICVHPSPNSK YSIELASLVD DLIKRKIKPP 

        70         80         90        100        110        120 
ILLRFMNILE GRIASINRVF RNAIQTNNYP AQYQTFYPIK VNQQRQVVEA IANFGKKYNI 

       130        140        150        160        170        180 
GLEVGSKPEL VAAISISTNN SLPIICNGYK DTEFIETVLY ATKIGYNITI VIEKLFELEK 

       190        200        210        220        230        240 
VIELSRKTGI TPKLGIRVKL SSKGTGKWAT SGGEDAKFGL RISEIITAID LLKQYNLIDS 

       250        260        270        280        290        300 
VKLLHSHIGS QVTKIDKIKN ALIEGARIYV EMKKLGVNLE YIDIGGGLGV DYDGSKSSYF 

       310        320        330        340        350        360 
SSVNYSVEEY ANDVIYQIKN ICDEAGVDCP NIISESGRAT VAHYSVMVTN ILNTNTQNQM 

       370        380        390        400        410        420 
PDFESILTQA EPLSPTVRKL VDIYKSIDRH SLREDYHDTL QLIQEAVSLF NLGYLNLNDR 

       430        440        450        460        470        480 
AMAEWLYTRI IKKINNLVEK MKPVPEELQN FKLSMRQTYF ANFSLFQSIP DSWAIDQLFP 

       490        500        510        520        530        540 
IMPIQRLGEK PDVIASIADI TCDSDGEITS FVGENGRTKY LPLHKIRKNE EYYIGFFLIG 

       550        560        570        580        590        600 
AYQEILGDLH NLFGDTNAVH ITFNKKTNYR IDTVISGDAI QQSLKYVQYD GNEILKKVRD 

       610        620        630 
SLENGVASKK ISIEESSHFL ELLDKTIQAY TYLGE 

« Hide

References

[1]"Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000482 Genomic DNA. Translation: ABL00211.1.
RefSeqYP_902268.1. NC_008609.1.

3D structure databases

ProteinModelPortalA1AS90.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338966.Ppro_2606.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL00211; ABL00211; Ppro_2606.
GeneID4572939.
KEGGppd:Ppro_2606.
PATRIC22898311. VBIPelPro64470_2761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAIDHYVDG.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycPPRO338966:GHL0-2647-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
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.
IPR029066. PLP-binding_barrel.
[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.
SSF51419. SSF51419. 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_PELPD
AccessionPrimary (citable) accession number: A1AS90
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 51 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