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Q7UTS2 (SPEA_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:RB3708
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length668 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

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 – 668668Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149974

Regions

Region286 – 29611Substrate-binding Potential

Amino acid modifications

Modified residue1051N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UTS2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3851560B071E60A9

FASTA66874,081
        10         20         30         40         50         60 
MSSVLDSKWT RSDASKTYDI DRWGAGYFSI SDAGTVLVSP DRDPSQSIDL KELVDRLGQR 

        70         80         90        100        110        120 
NLDLPILLRF NGILRDRLRE LDRCFKNAIH DHKYQSRYRC VFPIKVNQQR EVVQQIVSEG 

       130        140        150        160        170        180 
ARLGFGIEAG SKPELVAAVA MGDANVPIVC NGFKDEEFIR LALLAQRLGR NVLPVVEKVS 

       190        200        210        220        230        240 
ELDLILDVAK DIGVRPTIGM RVKLATRGSG RWQASGGYRS KFGLTVAELL AQLDRLIAMD 

       250        260        270        280        290        300 
MGDCLQLLHF HVGSQIGNIR QLKSAILEAA RIYVDLVRRG AGMRYLDVGG GLGVDYDGSR 

       310        320        330        340        350        360 
SDSESSMNYT MQEYANDVVY HTQTVCDEAG VPHPELISES GRAVAAHHSV LVMETLGVTS 

       370        380        390        400        410        420 
QGVANLPCWA KVEGEPVSPD HGGIEMDSVG AIETSEMEGP PESYEQPVHD LWVGYVNMTQ 

       430        440        450        460        470        480 
ANMMETFHDA QVALDLCMNL FSGGYLPLEQ RVAAENLYFA ICHRVRELAE SMKERPDDLK 

       490        500        510        520        530        540 
HLDRMLSDIY FANFSLFQSM PDSWAIDQLF PIMPIHRLLE KPSRHAVLGD ITCDSDGKVD 

       550        560        570        580        590        600 
AFVCGGGRQR TLMLHPLKSG EPYQLAVFMV GAYQEILGDL HNLFGDTHAV HVDIEDGVTK 

       610        620        630        640        650        660 
VRSIVKGDTV SEVLGYVQYE DRELIENLQE SVESAIGNGH IDHQQAGETV AAYERALSGY 


TYLSTRTK 

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References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294139 Genomic DNA. Translation: CAD73363.1.
RefSeqNP_865678.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UTS2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB3708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD73363; CAD73363; RB3708.
GeneID1797121.
KEGGrba:RB3708.
PATRIC23244879. VBIRhoBal59814_1723.

Phylogenomic databases

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

Family and domain databases

Gene3D2.40.37.10. 2 hits.
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.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEA_RHOBA
AccessionPrimary (citable) accession number: Q7UTS2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 64 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