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A0A4W3 (SPEA_GEOSL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:GSU2537
OrganismGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) [Reference proteome] [HAMAP]
Taxonomic identifier243231 [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_1000068491

Regions

Region282 – 29211Substrate-binding Potential

Amino acid modifications

Modified residue1001N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0A4W3 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 5688D3984B1DAF99

FASTA63571,637
        10         20         30         40         50         60 
MERWSINESA KIYNLPNWGA DLFSINKKGN VCVHPSPTSK HSIDLRALVD DLIKRKIKPP 

        70         80         90        100        110        120 
ILLRFMDVLQ GRIASINRVF KNAIDENDYP ATYQTFYPIK VNQQRQVVEA IAKFGKRYNI 

       130        140        150        160        170        180 
GLEVGSKPEL VIGISFATGN GIPIICNGYK DTEYIETVLY ATKIGYDITI VVEKMFELEK 

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

       250        260        270        280        290        300 
VKLLHFHIGS QITKIDKIKS ALIEGTRIYA EMRKLGVGIR YVDIGGGLGV DYDGSKSSYF 

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

       370        380        390        400        410        420 
PDFEETLNGT EKLAPTVKKL VDIYKSIDRY SLREDYHDTV QLIQEAVSLF NLGYLTLNER 

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

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

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

       610        620        630 
TLEKDVALRK VTIEESSHFL ELLDRTLLGY TYLGE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017180 Genomic DNA. Translation: AAR35910.1.
RefSeqNP_953583.1. NC_002939.5.

3D structure databases

ProteinModelPortalA0A4W3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243231.GSU2537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAR35910; AAR35910; GSU2537.
GeneID2687789.
KEGGgsu:GSU2537.
PATRIC22027923. VBIGeoSul17553_2566.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGSUL243231:GH27-2570-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_GEOSL
AccessionPrimary (citable) accession number: A0A4W3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 28, 2006
Last modified: February 19, 2014
This is version 58 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