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A5GB52 (SPEA_GEOUR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Gura_0983
OrganismGeobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens) [Complete proteome] [HAMAP]
Taxonomic identifier351605 [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_1000087404

Regions

Region282 – 29211Substrate-binding Potential

Amino acid modifications

Modified residue1001N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GB52 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 7CE13746E2FB8758

FASTA63571,778
        10         20         30         40         50         60 
MERWSINDSA KIYNLNNWGA DLFSINKKGN VCVHPSSNSK HSIDLRALVD DLIKRKIKPP 

        70         80         90        100        110        120 
ILLRFMDVLQ GRIASINRVF KNAIQENNYP AKYQTFYPIK VNQQRQVVEA IANFGKRYNI 

       130        140        150        160        170        180 
GLEVGSKPEL VAGISFATGN NLPIICNGYK DTEYIEMVLS ATKIGYDITL VVEKLFELEK 

       190        200        210        220        230        240 
IIELVKKTGV QPKLGIRVKL SSKGIGKWAT SGGEDAKFGL RMSEIIAAIE MLEKHDLIKC 

       250        260        270        280        290        300 
VKLLHFHIGS QITKIDKIKT ALIEGARIYA EMRKLGVGIE YLDIGGGLGV DYDGSKSSNF 

       310        320        330        340        350        360 
SSVNYSIEEY ANDVIYQIKN ICEDAGVECP NIISESGRAT VAHYSVLVTN VLNTNTQNIM 

       370        380        390        400        410        420 
PDFEATLNEA EKLAPTVKKL EDIYKSIDRY SLREDYHDTL QLIQEAVSLF NLGYLTLNDR 

       430        440        450        460        470        480 
AMAEWLYGKI IRKINSIVEK IKPIPEELQN FQLSLRQTYF ANFSLFQSVP DSWAIDQLFP 

       490        500        510        520        530        540 
IVPIQRLNQK PDVIASIADI TCDSDGEITS FVGENGRTKF LPLHKIRKDE AYYIGFFLIG 

       550        560        570        580        590        600 
AYQEILGDMH NLFGDTNAVH ITFNKKTGYI IDTVINGDAT WESLKYVQYK GPEILKRVRD 

       610        620        630 
NLEKDVALRK ISIEESSHFL ELLDRTLLGY TYLGE 

« Hide

References

[1]"Complete sequence of Geobacter uraniireducens Rf4."
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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., Lovley D., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Rf4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000698 Genomic DNA. Translation: ABQ25189.1.
RefSeqYP_001229762.1. NC_009483.1.

3D structure databases

ProteinModelPortalA5GB52.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351605.Gura_0983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ25189; ABQ25189; Gura_0983.
GeneID5163174.
KEGGgur:Gura_0983.
PATRIC22031920. VBIGeoUra13052_1053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGURA351605:GI6A-992-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

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_GEOUR
AccessionPrimary (citable) accession number: A5GB52
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 53 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