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Q39X78 (SPEA_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Gmet_0904
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [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_1000068490

Regions

Region282 – 29211Substrate-binding Potential

Amino acid modifications

Modified residue1001N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39X78 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 689186DAE924266B

FASTA63571,521
        10         20         30         40         50         60 
MERWSINDSA KIYNLPNWGA DLFSINKKGN VCVHPSPTSK HSIDLRALVD DLIKRKIKPP 

        70         80         90        100        110        120 
ILLRFMDVLQ GRIAAINRAF KYAIDENDYP STYQTFYPIK VNQQRQVVEA IAKFGKRYNI 

       130        140        150        160        170        180 
GIEVGSKPEL VIGISFATGN GIPIICNGYK DKEYIETVLY ATKIGYDITI VVEKMFELEK 

       190        200        210        220        230        240 
IIALSKKTGI KPKLGIRVKL SSKGTGKWAT SGGEDAKFGL RMSEIIAAIG LLEQNELLDS 

       250        260        270        280        290        300 
VKLIHFHIGS QITKIDKIKS ALIEGTRVYA EMRKLGVGIE YVDIGGGLGV DYDGSKSSYF 

       310        320        330        340        350        360 
SSVNYSIEEY ANDVIYQIKN ICEDAGVECP NIISESGRAT AAHYSVLVTN LLNTNTQNLM 

       370        380        390        400        410        420 
PDFEETLNGA EKLAPTVKKL VDIYKSIDRY SLREDYHDTV QLIQEAVSLF SLGYLTLAER 

       430        440        450        460        470        480 
AMAEWLHGKI LRKINGIVEK IKPIPEELQN FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP 

       490        500        510        520        530        540 
IVPIQRLNQK PDVMASIADI TCDSDGEITS FVGENGRTKY LPLHKIRKDE DYFVGFFLIG 

       550        560        570        580        590        600 
AYQEILGDMH NLFGDTNAVH VTFNKKTGYK IDTVINGDAT WESLKYVQYK GPEILKHVRD 

       610        620        630 
TMEKDVALRK VSIEESSHFL ELLDRTLLGY TYLGE 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB31146.1.
RefSeqYP_006719870.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39X78.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269799.Gmet_0904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB31146; ABB31146; Gmet_0904.
GeneID3738242.
KEGGgme:Gmet_0904.
PATRIC22000996. VBIGeoMet55070_0939.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGMET269799:GHNY-912-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_GEOMG
AccessionPrimary (citable) accession number: Q39X78
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 60 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