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B3EAF3 (SPEA_GEOLS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Glov_1675
OrganismGeobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) [Complete proteome] [HAMAP]
Taxonomic identifier398767 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

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_1000145595

Regions

Region282 – 29211Substrate-binding Potential

Amino acid modifications

Modified residue1001N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3EAF3 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 9165D56672C0CBF9

FASTA63571,685
        10         20         30         40         50         60 
MERWSINESA KVYNLDNWGA DLFSINKKGN ICVHPSSNSK NAIDLRALVD DLIKRKIKPP 

        70         80         90        100        110        120 
ILLRFMDVLQ GRIASINRVF RNAIAENDYP AKYQTFYPIK VNQQRQVVEA IASYGKRYNI 

       130        140        150        160        170        180 
GLEVGSKPEL VAGIAISTGN GLPIICNGYK DAEYIETVLF ATRVGYNITI VVEKLFELEK 

       190        200        210        220        230        240 
IIELAKKTGI RPSLGIRVKL SSKGTGKWAT SGGEDAKFGL RMSEIMAAIK MLQEADLLDC 

       250        260        270        280        290        300 
VNLLHSHIGS QVTKIDKIKT ALIEAARIYS EMRKLGVNIQ YLDIGGGLGV DYDGSKSSYF 

       310        320        330        340        350        360 
SSVNYTVEEY ANDVIYQIKN ICDEAGVDCP NIISESGRAT VAHYSVLVTN VLNTNTQNLM 

       370        380        390        400        410        420 
PDYEQILEEM EKPAPTVKKL LDIYKSIDRY SLREDYHDTL QLINEAVSLF NLGYLTLQDR 

       430        440        450        460        470        480 
AIAEWLYSKI IKKINSIVEK IKPIPEELQN FQLALRQTYF ANFSLFQSIP DSWAIDQLFP 

       490        500        510        520        530        540 
IMPLQRLGQR PDVMASIADI TCDSDGEITS FVGENGRSKF LPMHKLKKDE DYYIGFFLIG 

       550        560        570        580        590        600 
AYQEILGDLH NLFGDTNAVH ITFNKKTGYM IDTVINGDAT WETLKYVQYK GPEILKHVRD 

       610        620        630 
NLEKQVAIKK VSIEESSHFI ELLDRTLLGY TYLGE 

« Hide

References

[1]"Complete sequence of chromosome of Geobacter lovleyi SZ."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1151 / DSM 17278 / SZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001089 Genomic DNA. Translation: ACD95391.1.
RefSeqYP_001951911.1. NC_010814.1.

3D structure databases

ProteinModelPortalB3EAF3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398767.Glov_1675.

Proteomic databases

PRIDEB3EAF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD95391; ACD95391; Glov_1675.
GeneID6368497.
KEGGglo:Glov_1675.
PATRIC21995027. VBIGeoLov31523_1620.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAIDHYVDG.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycGLOV398767:GH32-1700-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_GEOLS
AccessionPrimary (citable) accession number: B3EAF3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: June 11, 2014
This is version 44 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