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Q8DHY6 (SPEA_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:tll1807
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length637 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 – 637637Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149979

Regions

Region289 – 29911Substrate-binding Potential

Amino acid modifications

Modified residue1071N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DHY6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A924C72CB50F29C5

FASTA63770,856
        10         20         30         40         50         60 
MALTVTKTSN WTIEDSEQLY RIQGWGEPYF GINAAGHVTV SPKGDRGGSL DLYELVQALQ 

        70         80         90        100        110        120 
QRNISLPLLL RFSDILEDRI ERLNACFARA IARYGYQGAY KGVFPIKCNQ QRHIIEALVR 

       130        140        150        160        170        180 
FGQSHQFGLE AGSKPELLIA LAMLNTPGAL LICNGYKDRS YIETAILARR LGHTSIIVLE 

       190        200        210        220        230        240 
QPEEVAEVIA VSQALGIEPI VGVRAKLSTQ GVGRWGTSAG DRAKFGLTVP EILTAVEQLR 

       250        260        270        280        290        300 
AAGMLNALQL LHFHIGSQIS AISVIKDAIR EAGQIYGELV RLGANMQYLD VGGGLGVDYD 

       310        320        330        340        350        360 
GSKTNFHASK NYSMQNYASD VVAGIKDACR QRGIPDPTLI SESGRAIASH QSVLIFNVLG 

       370        380        390        400        410        420 
VSEVPKITPE PATAEEHLII RNLYDTYQAI DENNYQEAYN DALQFKGEAI SLFNFGYLSL 

       430        440        450        460        470        480 
PERARAESLF WACCAKILGI ARQQEYVPDD LEDLEKIMAS IYYINLSVFQ SVPDSWAIDQ 

       490        500        510        520        530        540 
LFPIMPIHRL DEEPTERGIL ADLTCDSDGK IDQFIDLRDV KSVLELHPFR PGEPYYLGLF 

       550        560        570        580        590        600 
LNGAYQEIMG NLHNLFGDTN AVHIRLTPKG YEIEHLVRGD TMQEVLGYVQ YQGDALLEKI 

       610        620        630 
RCRTEAALAE EQITLAEAQH LLENYERSLR SYTYLSS 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC09359.1.
RefSeqNP_682597.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DHY6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll1807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC09359; BAC09359; BAC09359.
GeneID1012401.
KEGGtel:tll1807.
PATRIC23928998. VBITheElo119873_1889.

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.
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_THEEB
AccessionPrimary (citable) accession number: Q8DHY6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 67 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